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Conserved domains on  [gi|1771853668|ref|NP_001362688|]
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GRB10-interacting GYF protein 1 isoform a [Homo sapiens]

Protein Classification

GYF domain-containing protein( domain architecture ID 10049341)

GYF (glycine-tyrosine-phenylalanine) domain-containing protein similar to Arabidopsis thaliana protein ESSENTIAL FOR POTEXVIRUS ACCUMULATION 1, a translational repressor involved in the negative regulation of immune receptor accumulation via the inhibition of nucleotide-binding leucine-rich repeat (NLR) receptor mediated defense

CATH:  3.30.1490.40
Gene Ontology:  GO:0005515
PubMed:  10404223|16403013
SCOP:  4001496

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GYF cd00072
GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and ...
 476-529 6.15e-23

GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and other proteins. Involved in signaling lymphocyte activity. Also present in other unrelated proteins (mainly unknown) derived from diverse eukaryotic species.


:

Pssm-ID: 238027  Cd Length: 57  Bit Score: 92.76  E-value: 6.15e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1771853668  476 KWFYKDPQGEIQGPFTTQEMAEWFQAGYFSMSLLVKR-GCDEGFQPLGEVIKMWG 529
Cdd:cd00072      3 QWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRlDNGGEFYTLGDILFDLG 57
 
Name Accession Description Interval E-value
GYF cd00072
GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and ...
 476-529 6.15e-23

GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and other proteins. Involved in signaling lymphocyte activity. Also present in other unrelated proteins (mainly unknown) derived from diverse eukaryotic species.


Pssm-ID: 238027  Cd Length: 57  Bit Score: 92.76  E-value: 6.15e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1771853668  476 KWFYKDPQGEIQGPFTTQEMAEWFQAGYFSMSLLVKR-GCDEGFQPLGEVIKMWG 529
Cdd:cd00072      3 QWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRlDNGGEFYTLGDILFDLG 57
GYF smart00444
Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. ...
 476-530 6.33e-22

Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. Contains conserved Gly-Tyr-Phe residues.


Pssm-ID: 214666  Cd Length: 56  Bit Score: 89.70  E-value: 6.33e-22
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1771853668   476 KWFYKDPQGEIQGPFTTQEMAEWFQAGYFSMSLLVKRGCDEGFQPLGEVIKMWGR 530
Cdd:smart00444    2 LWLYKDPDGEIQGPFTASQMSQWYQAGYFPDSLQIKRLNEPPYETLGDLDRLLGL 56
GYF pfam02213
GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF ...
 477-521 7.06e-22

GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF domain is a proline-binding domain in CD2-binding protein Swiss:O95400.


Pssm-ID: 460496  Cd Length: 45  Bit Score: 89.18  E-value: 7.06e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1771853668  477 WFYKDPQGEIQGPFTTQEMAEWFQAGYFSMSLLVKRGCDEGFQPL 521
Cdd:pfam02213    1 WEYKDPQGEVQGPFSSAEMQEWYKAGYFPDDLPVRRVGDTEFYPL 45
 
Name Accession Description Interval E-value
GYF cd00072
GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and ...
 476-529 6.15e-23

GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and other proteins. Involved in signaling lymphocyte activity. Also present in other unrelated proteins (mainly unknown) derived from diverse eukaryotic species.


Pssm-ID: 238027  Cd Length: 57  Bit Score: 92.76  E-value: 6.15e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1771853668  476 KWFYKDPQGEIQGPFTTQEMAEWFQAGYFSMSLLVKR-GCDEGFQPLGEVIKMWG 529
Cdd:cd00072      3 QWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRlDNGGEFYTLGDILFDLG 57
GYF smart00444
Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. ...
 476-530 6.33e-22

Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. Contains conserved Gly-Tyr-Phe residues.


Pssm-ID: 214666  Cd Length: 56  Bit Score: 89.70  E-value: 6.33e-22
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1771853668   476 KWFYKDPQGEIQGPFTTQEMAEWFQAGYFSMSLLVKRGCDEGFQPLGEVIKMWGR 530
Cdd:smart00444    2 LWLYKDPDGEIQGPFTASQMSQWYQAGYFPDSLQIKRLNEPPYETLGDLDRLLGL 56
GYF pfam02213
GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF ...
 477-521 7.06e-22

GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF domain is a proline-binding domain in CD2-binding protein Swiss:O95400.


Pssm-ID: 460496  Cd Length: 45  Bit Score: 89.18  E-value: 7.06e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1771853668  477 WFYKDPQGEIQGPFTTQEMAEWFQAGYFSMSLLVKRGCDEGFQPL 521
Cdd:pfam02213    1 WEYKDPQGEVQGPFSSAEMQEWYKAGYFPDDLPVRRVGDTEFYPL 45
 
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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