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Conserved domains on  [gi|159032016|ref|NP_001103682|]
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GRB10-interacting GYF protein 2 isoform b [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 ...
528-583 5.18e-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: 5.18e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 159032016  528 MQKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRA-CDESFQPLGDIMKMWG 583
Cdd:cd00072     1 EVQWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLdNGGEFYTLGDILFDLG 57
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
324-468 5.67e-05

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 47.76  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016  324 EEGEERSDSDSSHNEEAKEPDK-TNRREGEKTDragaeaseevpqtslssaRPGTPSDHQPQEATQFERKDE-PKAEQVE 401
Cdd:PTZ00449  527 KEGEEGEHEDSKESDEPKEGGKpGETKEGEVGK------------------KPGPAKEHKPSKIPTLSKKPEfPKDPKHP 588
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159032016  402 KAEEENRSENS-LSAKVP-SRGDETVPASQQ-PSTPLPPDtaSPLLILSPPVPT-PSSASRPVETAAVEAP 468
Cdd:PTZ00449  589 KDPEEPKKPKRpRSAQRPtRPKSPKLPELLDiPKSPKRPE--SPKSPKRPPPPQrPSSPERPEGPKIIKSP 657
 
Name Accession Description Interval E-value
GYF cd00072
GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and ...
528-583 5.18e-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: 5.18e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 159032016  528 MQKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRA-CDESFQPLGDIMKMWG 583
Cdd:cd00072     1 EVQWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLdNGGEFYTLGDILFDLG 57
GYF smart00444
Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. ...
529-584 3.44e-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: 3.44e-22
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 159032016    529 QKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPLGDIMKMWGR 584
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 ...
531-575 7.72e-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: 7.72e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 159032016   531 WYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPL 575
Cdd:pfam02213    1 WEYKDPQGEVQGPFSSAEMQEWYKAGYFPDDLPVRRVGDTEFYPL 45
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
324-468 5.67e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 47.76  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016  324 EEGEERSDSDSSHNEEAKEPDK-TNRREGEKTDragaeaseevpqtslssaRPGTPSDHQPQEATQFERKDE-PKAEQVE 401
Cdd:PTZ00449  527 KEGEEGEHEDSKESDEPKEGGKpGETKEGEVGK------------------KPGPAKEHKPSKIPTLSKKPEfPKDPKHP 588
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159032016  402 KAEEENRSENS-LSAKVP-SRGDETVPASQQ-PSTPLPPDtaSPLLILSPPVPT-PSSASRPVETAAVEAP 468
Cdd:PTZ00449  589 KDPEEPKKPKRpRSAQRPtRPKSPKLPELLDiPKSPKRPE--SPKSPKRPPPPQrPSSPERPEGPKIIKSP 657
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
338-509 8.46e-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: 43.99  E-value: 8.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016   338 EEAKEPDKTNRREGEKtdraGAEASEEVPQTSLSS------ARPGTPSDHQPQEATQFERKDEPKAEQvEKAEEENRSEn 411
Cdd:pfam03154   71 EEAPSPLKSAKRQREK----GASDTEEPERATAKKsktqeiSRPNSPSEGEGESSDGRSVNDEGSSDP-KDIDQDNRST- 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016   412 slSAKVPS----RGDETVPASQQPSTPLPPDTASPllilSPPVPTPSSASRPVETAAVEAPGMSSVSTEPDDEEGLKHLE 487
Cdd:pfam03154  145 --SPSIPSpqdnESDSDSSAQQQILQTQPPVLQAQ----SGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218
                          170       180
                   ....*....|....*....|....*.
gi 159032016   488 QQAEKMVAYL----QDSALDDERLTS 509
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 ...
528-583 5.18e-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: 5.18e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 159032016  528 MQKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRA-CDESFQPLGDIMKMWG 583
Cdd:cd00072     1 EVQWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLdNGGEFYTLGDILFDLG 57
GYF smart00444
Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. ...
529-584 3.44e-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: 3.44e-22
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 159032016    529 QKWYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPLGDIMKMWGR 584
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 ...
531-575 7.72e-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: 7.72e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 159032016   531 WYYKDPQGEIQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPL 575
Cdd:pfam02213    1 WEYKDPQGEVQGPFSSAEMQEWYKAGYFPDDLPVRRVGDTEFYPL 45
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
324-468 5.67e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 47.76  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016  324 EEGEERSDSDSSHNEEAKEPDK-TNRREGEKTDragaeaseevpqtslssaRPGTPSDHQPQEATQFERKDE-PKAEQVE 401
Cdd:PTZ00449  527 KEGEEGEHEDSKESDEPKEGGKpGETKEGEVGK------------------KPGPAKEHKPSKIPTLSKKPEfPKDPKHP 588
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159032016  402 KAEEENRSENS-LSAKVP-SRGDETVPASQQ-PSTPLPPDtaSPLLILSPPVPT-PSSASRPVETAAVEAP 468
Cdd:PTZ00449  589 KDPEEPKKPKRpRSAQRPtRPKSPKLPELLDiPKSPKRPE--SPKSPKRPPPPQrPSSPERPEGPKIIKSP 657
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
310-481 8.44e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.09  E-value: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016  310 EPIPEEQEMDFRPVEEGEERSDsdsshneEAKEPDKTNRREGEKTDRAGAEASEEVPQTSLSSARPGTPSDHQPQEATQF 389
Cdd:PHA03307   74 GPGTEAPANESRSTPTWSLSTL-------APASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGP 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016  390 ERKDEPKAEQVEKAEEENRSENSLSAKVP-SRGDETVPASQQPSTPLPPDTASPLLILSPPVPT-------PSSASRPVE 461
Cdd:PHA03307  147 PPAASPPAAGASPAAVASDAASSRQAALPlSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSspisasaSSPAPAPGR 226
                         170       180
                  ....*....|....*....|
gi 159032016  462 TAAVEAPGMSSVSTEPDDEE 481
Cdd:PHA03307  227 SAADDAGASSSDSSSSESSG 246
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
338-509 8.46e-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: 43.99  E-value: 8.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016   338 EEAKEPDKTNRREGEKtdraGAEASEEVPQTSLSS------ARPGTPSDHQPQEATQFERKDEPKAEQvEKAEEENRSEn 411
Cdd:pfam03154   71 EEAPSPLKSAKRQREK----GASDTEEPERATAKKsktqeiSRPNSPSEGEGESSDGRSVNDEGSSDP-KDIDQDNRST- 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016   412 slSAKVPS----RGDETVPASQQPSTPLPPDTASPllilSPPVPTPSSASRPVETAAVEAPGMSSVSTEPDDEEGLKHLE 487
Cdd:pfam03154  145 --SPSIPSpqdnESDSDSSAQQQILQTQPPVLQAQ----SGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPP 218
                          170       180
                   ....*....|....*....|....*.
gi 159032016   488 QQAEKMVAYL----QDSALDDERLTS 509
Cdd:pfam03154  219 NQTQSTAAPHtliqQTPTLHPQRLPS 244
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
323-477 1.15e-03

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 43.14  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016   323 VEEGEERSDSDSSHNEEAKEPDKTnrreGEKTDRAGAEASEEVPQTSLSSARPGTPSDhqPQEATQFERKDEPKAEQVeK 402
Cdd:pfam03546  307 VARGAQRPEEDSSSSEESESEEET----APAAAVGQAKSVGKGLQGKAASAPTKGPSG--QGTAPVPPGKTGPAVAQV-K 379
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 159032016   403 AEEENRSENSLSAKVPSRGDETvPASQQPSTPLPPDTASPLLILSPPVPTPSSASRPVETAAVEAPGMSSVSTEP 477
Cdd:pfam03546  380 AEAQEDSESSEEESDSEEAAAT-PAQVKASGKTPQAKANPAPTKASSAKGAASAPGKVVAAAAQAKQGSPAKVKP 453
rne PRK10811
ribonuclease E; Reviewed
305-480 1.25e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.10  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016  305 KKVQKEPIPEEQEMDFRPVEE-----------GEERSDSDSSHNEEAKEPDKTNRREGEKTDRAGAEASEEVPQTSLSSA 373
Cdd:PRK10811  586 TKPQEQPAPKAEAKPERQQDRrkprqnnrrdrNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEKA 665
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016  374 RPGTPSDHQPQEATQFERKDEPKAEQVEKAEEENRSENSLSAKVPSRGDETVPASQQ-----------PSTPLPPDTASP 442
Cdd:PRK10811  666 RTQDEQQQAPRRERQRRRNDEKRQAQQEAKALNVEEQSVQETEQEERVQQVQPRRKQrqlnqkvrieqSVAEEAVAPVVE 745
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 159032016  443 LLILSPPVPTPSSASRPvETAAVEAPGMSSVSTEPDDE 480
Cdd:PRK10811  746 ETVAAEPVVQEVPAPRT-ELVKVPLPVVAQTAPEQDEE 782
PRK10927 PRK10927
cell division protein FtsN;
302-480 6.76e-03

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 40.05  E-value: 6.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016  302 LSLKKVQKEPIPEEQEMDFRPVEEGEER-----SDSDSSHNEEAKEPDKTNRREGEKTDRAGAEASEEVPQTSLSSARPG 376
Cdd:PRK10927   65 LQSQKVTGNGLPPKPEERWRYIKELESRqpgvrAPTEPSAGGEVKTPEQLTPEQRQLLEQMQADMRQQPTQLVEVPWNEQ 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159032016  377 TPSdhQPQEATQFERKDEPKAEQVEKAEEENRSENSlsAKVPSRGDETVPASQQPSTPLPPDTASPLL-ILSPPVPTPSS 455
Cdd:PRK10927  145 TPE--QRQQTLQRQRQAQQLAEQQRLAQQSRTTEQS--WQQQTRTSQAAPVQAQPRQSKPASTQQPYQdLLQTPAHTTAQ 220
                         170       180
                  ....*....|....*....|....*
gi 159032016  456 ASRPVETAAVEAPGMSSVSTEPDDE 480
Cdd:PRK10927  221 SKPQQAAPVTRAADAPKPTAEKKDE 245
 
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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