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Conserved domains on  [gi|568908820|ref|XP_006529530|]
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GRB10-interacting GYF protein 2 isoform X5 [Mus musculus]

Protein Classification

GYF domain-containing protein( domain architecture ID 10049341)

GYF (glycine-tyrosine-phenylalanine) domain-containing protein binds proline-rich sequences and is involved in protein-protein interactions

CATH:  3.30.1490.40
Gene Ontology:  GO:0005515|GO:0070064
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 ...
 527-582 5.17e-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: 93.14  E-value: 5.17e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568908820  527 MQKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRA-CDESFQPLGDIMKMWG 582
Cdd:cd00072     1 EVQWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLdNGGEFYTLGDILFDLG 57
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 286-480 1.02e-04

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820  286 EDAEEEMGTFDSSGAFLSLKKVQKEPIPEEqemdfrPVEEGEERSDSDSSHNEEAKEPdKTNRREGEKTDRAGAASEEVP 365
Cdd:PHA03307   46 DSAELAAVTVVAGAAACDRFEPPTGPPPGP------GTEAPANESRSTPTWSLSTLAP-ASPAREGSPTPPGPSSPDPPP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820  366 QTSlSSARPGTPSDHQPQEATQFERKDEPKAEQVEKAEEENRSE------NSLSAKVP-SRGDETVPASQQPSTPLPPDT 438
Cdd:PHA03307  119 PTP-PPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAvasdaaSSRQAALPlSSPEETARAPSSPPAEPPPST 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568908820  439 ASPLLILSPPVPT-------PSSASRPVETAAVEAPGMSSVSTEPDDEE 480
Cdd:PHA03307  198 PPAAASPRPPRRSspisasaSSPAPAPGRSAADDAGASSSDSSSSESSG 246
 
Name Accession Description Interval E-value
GYF cd00072
GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and ...
 527-582 5.17e-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: 93.14  E-value: 5.17e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568908820  527 MQKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRA-CDESFQPLGDIMKMWG 582
Cdd:cd00072     1 EVQWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLdNGGEFYTLGDILFDLG 57
GYF smart00444
Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. ...
 528-583 3.57e-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: 90.85  E-value: 3.57e-22
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568908820    528 QKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPLGDIMKMWGR 583
Cdd:smart00444    1 VLWLYKDPDGEIQGPFTASQMSQWYQAGYFPDSLQIKRLNEPPYETLGDLDRLLGL 56
GYF pfam02213
GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF ...
 530-574 7.64e-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: 89.56  E-value: 7.64e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568908820   530 WYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPL 574
Cdd:pfam02213    1 WEYKDPQGEVQGPFSSAEMQEWYKAGYFPDDLPVRRVGDTEFYPL 45
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 286-480 1.02e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820  286 EDAEEEMGTFDSSGAFLSLKKVQKEPIPEEqemdfrPVEEGEERSDSDSSHNEEAKEPdKTNRREGEKTDRAGAASEEVP 365
Cdd:PHA03307   46 DSAELAAVTVVAGAAACDRFEPPTGPPPGP------GTEAPANESRSTPTWSLSTLAP-ASPAREGSPTPPGPSSPDPPP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820  366 QTSlSSARPGTPSDHQPQEATQFERKDEPKAEQVEKAEEENRSE------NSLSAKVP-SRGDETVPASQQPSTPLPPDT 438
Cdd:PHA03307  119 PTP-PPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAvasdaaSSRQAALPlSSPEETARAPSSPPAEPPPST 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568908820  439 ASPLLILSPPVPT-------PSSASRPVETAAVEAPGMSSVSTEPDDEE 480
Cdd:PHA03307  198 PPAAASPRPPRRSspisasaSSPAPAPGRSAADDAGASSSDSSSSESSG 246
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 338-508 5.82e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.37  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820   338 EEAKEPDKTNRREGEK-------TDRAGAASEEVPQTSlssaRPGTPSDHQPQEATQFERKDEPKAEQvEKAEEENRSEn 410
Cdd:pfam03154   71 EEAPSPLKSAKRQREKgasdteePERATAKKSKTQEIS----RPNSPSEGEGESSDGRSVNDEGSSDP-KDIDQDNRST- 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820   411 slSAKVPS----RGDETVPASQQPSTPLPPDTASPllilSPPVPTPSSASRPVETAAVEAPGMSSVSTEPDDEEGLKHLE 486
Cdd:pfam03154  145 --SPSIPSpqdnESDSDSSAQQQILQTQPPVLQAQ----SGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218

                          170       180
                   ....*....|....*....|....*.
gi 568908820   487 QQAEKMVAYL----QDSALDDERLTS 508
Cdd:pfam03154  219 NQTQSTAAPHtliqQTPTLHPQRLPS 244
 
Name Accession Description Interval E-value
GYF cd00072
GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and ...
 527-582 5.17e-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: 93.14  E-value: 5.17e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568908820  527 MQKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRA-CDESFQPLGDIMKMWG 582
Cdd:cd00072     1 EVQWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLdNGGEFYTLGDILFDLG 57
GYF smart00444
Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. ...
 528-583 3.57e-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: 90.85  E-value: 3.57e-22
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 568908820    528 QKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPLGDIMKMWGR 583
Cdd:smart00444    1 VLWLYKDPDGEIQGPFTASQMSQWYQAGYFPDSLQIKRLNEPPYETLGDLDRLLGL 56
GYF pfam02213
GYF domain; The GYF domain is named because of the presence of Gly-Tyr-Phe residues. The GYF ...
 530-574 7.64e-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: 89.56  E-value: 7.64e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 568908820   530 WYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPL 574
Cdd:pfam02213    1 WEYKDPQGEVQGPFSSAEMQEWYKAGYFPDDLPVRRVGDTEFYPL 45
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 286-480 1.02e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820  286 EDAEEEMGTFDSSGAFLSLKKVQKEPIPEEqemdfrPVEEGEERSDSDSSHNEEAKEPdKTNRREGEKTDRAGAASEEVP 365
Cdd:PHA03307   46 DSAELAAVTVVAGAAACDRFEPPTGPPPGP------GTEAPANESRSTPTWSLSTLAP-ASPAREGSPTPPGPSSPDPPP 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820  366 QTSlSSARPGTPSDHQPQEATQFERKDEPKAEQVEKAEEENRSE------NSLSAKVP-SRGDETVPASQQPSTPLPPDT 438
Cdd:PHA03307  119 PTP-PPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAvasdaaSSRQAALPlSSPEETARAPSSPPAEPPPST 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568908820  439 ASPLLILSPPVPT-------PSSASRPVETAAVEAPGMSSVSTEPDDEE 480
Cdd:PHA03307  198 PPAAASPRPPRRSspisasaSSPAPAPGRSAADDAGASSSDSSSSESSG 246
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 338-508 5.82e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 44.37  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820   338 EEAKEPDKTNRREGEK-------TDRAGAASEEVPQTSlssaRPGTPSDHQPQEATQFERKDEPKAEQvEKAEEENRSEn 410
Cdd:pfam03154   71 EEAPSPLKSAKRQREKgasdteePERATAKKSKTQEIS----RPNSPSEGEGESSDGRSVNDEGSSDP-KDIDQDNRST- 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820   411 slSAKVPS----RGDETVPASQQPSTPLPPDTASPllilSPPVPTPSSASRPVETAAVEAPGMSSVSTEPDDEEGLKHLE 486
Cdd:pfam03154  145 --SPSIPSpqdnESDSDSSAQQQILQTQPPVLQAQ----SGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218

                          170       180
                   ....*....|....*....|....*.
gi 568908820   487 QQAEKMVAYL----QDSALDDERLTS 508
Cdd:pfam03154  219 NQTQSTAAPHtliqQTPTLHPQRLPS 244
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
323-476 1.19e-03

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 43.14  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820   323 VEEGEERSDSDSSHNEEAKEPDKT-------NRREGEKTDRAGAASEEVPQTSLSSARPGTPsdhqpqeatqfeRKDEPK 395
Cdd:pfam03546  307 VARGAQRPEEDSSSSEESESEEETapaaavgQAKSVGKGLQGKAASAPTKGPSGQGTAPVPP------------GKTGPA 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820   396 AEQVeKAEEENRSENSLSAKVPSRGDETvPASQQPSTPLPPDTASPLLILSPPVPTPSSASRPVETAAVEAPGMSSVSTE 475
Cdd:pfam03546  375 VAQV-KAEAQEDSESSEEESDSEEAAAT-PAQVKASGKTPQAKANPAPTKASSAKGAASAPGKVVAAAAQAKQGSPAKVK 452


                   .
gi 568908820   476 P 476
Cdd:pfam03546  453 P 453
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 357-483 4.46e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568908820  357 AGAASEEVPQTSLSSARPGTPSDHQPQEATQFERKDEPKA--EQVEKAEEENRSENSLSAKVPSRGDETVPASQQPSTPL 434
Cdd:PRK07764  388 AGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAapQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPA 467

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568908820  435 PPDTASPLLILSPPvPTPSSASRPVETAAVEAPgmSSVSTEPDDEEGLK 483
Cdd:PRK07764  468 PAPAAAPEPTAAPA-PAPPAAPAPAAAPAAPAA--PAAPAGADDAATLR 513
 
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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