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Conserved domains on  [gi|1958805500|ref|XP_038940647|]
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GRB10-interacting GYF protein 2 isoform X10 [Rattus norvegicus]

Protein Classification

GYF domain-containing protein; ParB/RepB/Spo0J family partition protein( domain architecture ID 11907814)

GYF (glycine-tyrosine-phenylalanine) domain-containing protein binds proline-rich sequences and is involved in protein-protein interactions| ParB/RepB/Spo0J family partition protein which may be involved in segregation and competition between plasmids and chromosomes such as the ParB/SpoJ-type DNA-binding component of the prokaryotic parABS partitioning system

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 ...
 285-340 3.24e-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: 93.53  E-value: 3.24e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958805500  285 MQKWYYKDPQGEVQGPFNNQEMAEWFQAGYFTMSLLVKRA-CDESFQPLGDIMKMWG 340
Cdd:cd00072      1 EVQWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLdNGGEFYTLGDILFDLG 57
PHA03169 super family cl27451
hypothetical protein; Provisional
 81-248 4.66e-03

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805500   81 EEGEERSDSDSSHNEEAKEPDKTNRRDGEKTDRAGTDANEEVPQTSLSSARPGTPSDHQPQEAAQFERKDEPKAEQMEKA 160
Cdd:PHA03169    69 TESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHE 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805500  161 EEESRSENSLPAKIPSRGD----ETVPASQQPSTQLPPDTASPLLILSPPLPTPSSASRPVETAAVEAPGMSSvSTEPDD 236
Cdd:PHA03169   149 PAPPESHNPSPNQQPSSFLqpshEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQ-APSPNT 227

                          170
                   ....*....|..
gi 1958805500  237 EEGLKHLEQQAE 248
Cdd:PHA03169   228 QQAVEHEDEPTE 239
 
Name Accession Description Interval E-value
GYF cd00072
GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and ...
 285-340 3.24e-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: 93.53  E-value: 3.24e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958805500  285 MQKWYYKDPQGEVQGPFNNQEMAEWFQAGYFTMSLLVKRA-CDESFQPLGDIMKMWG 340
Cdd:cd00072      1 EVQWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLdNGGEFYTLGDILFDLG 57
GYF smart00444
Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. ...
 286-341 3.37e-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: 90.47  E-value: 3.37e-22
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958805500   286 QKWYYKDPQGEVQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPLGDIMKMWGR 341
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 ...
 288-332 3.91e-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: 89.95  E-value: 3.91e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958805500  288 WYYKDPQGEVQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPL 332
Cdd:pfam02213    1 WEYKDPQGEVQGPFSSAEMQEWYKAGYFPDDLPVRRVGDTEFYPL 45
PHA03169 PHA03169
hypothetical protein; Provisional
 81-248 4.66e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805500   81 EEGEERSDSDSSHNEEAKEPDKTNRRDGEKTDRAGTDANEEVPQTSLSSARPGTPSDHQPQEAAQFERKDEPKAEQMEKA 160
Cdd:PHA03169    69 TESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHE 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805500  161 EEESRSENSLPAKIPSRGD----ETVPASQQPSTQLPPDTASPLLILSPPLPTPSSASRPVETAAVEAPGMSSvSTEPDD 236
Cdd:PHA03169   149 PAPPESHNPSPNQQPSSFLqpshEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQ-APSPNT 227

                          170
                   ....*....|..
gi 1958805500  237 EEGLKHLEQQAE 248
Cdd:PHA03169   228 QQAVEHEDEPTE 239
 
Name Accession Description Interval E-value
GYF cd00072
GYF domain: contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding and ...
 285-340 3.24e-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: 93.53  E-value: 3.24e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958805500  285 MQKWYYKDPQGEVQGPFNNQEMAEWFQAGYFTMSLLVKRA-CDESFQPLGDIMKMWG 340
Cdd:cd00072      1 EVQWFYKDPQGEIQGPFSASQMLQWYQAGYFPDGLQVRRLdNGGEFYTLGDILFDLG 57
GYF smart00444
Contains conserved Gly-Tyr-Phe residues; Proline-binding domain in CD2-binding protein. ...
 286-341 3.37e-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: 90.47  E-value: 3.37e-22
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958805500   286 QKWYYKDPQGEVQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPLGDIMKMWGR 341
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 ...
 288-332 3.91e-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: 89.95  E-value: 3.91e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958805500  288 WYYKDPQGEVQGPFNNQEMAEWFQAGYFTMSLLVKRACDESFQPL 332
Cdd:pfam02213    1 WEYKDPQGEVQGPFSSAEMQEWYKAGYFPDDLPVRRVGDTEFYPL 45
PHA03169 PHA03169
hypothetical protein; Provisional
 81-248 4.66e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805500   81 EEGEERSDSDSSHNEEAKEPDKTNRRDGEKTDRAGTDANEEVPQTSLSSARPGTPSDHQPQEAAQFERKDEPKAEQMEKA 160
Cdd:PHA03169    69 TESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHE 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805500  161 EEESRSENSLPAKIPSRGD----ETVPASQQPSTQLPPDTASPLLILSPPLPTPSSASRPVETAAVEAPGMSSvSTEPDD 236
Cdd:PHA03169   149 PAPPESHNPSPNQQPSSFLqpshEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQ-APSPNT 227

                          170
                   ....*....|..
gi 1958805500  237 EEGLKHLEQQAE 248
Cdd:PHA03169   228 QQAVEHEDEPTE 239
rne PRK10811
ribonuclease E; Reviewed
 62-248 6.96e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.41  E-value: 6.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805500   62 KKVQKEPIPEEQEMDFRPVEE-----------GEERSDSDSSHNEEAKEPDKTNRRDGEKTDRAGTDANEEVPQTSLSSA 130
Cdd:PRK10811   586 TKPQEQPAPKAEAKPERQQDRrkprqnnrrdrNERRDTRDNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEKA 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958805500  131 RPGTPSDHQPQEAAQFERKDEPKAEQMEKAEEESRSENSLPAKIPSRGDETVPASQQpsTQLPPDTASPLLILSPPLPTP 210
Cdd:PRK10811   666 RTQDEQQQAPRRERQRRRNDEKRQAQQEAKALNVEEQSVQETEQEERVQQVQPRRKQ--RQLNQKVRIEQSVAEEAVAPV 743

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1958805500  211 SSASRPVETAAVEAPGMSSVSTEPDDEEGLKHLEQQAE 248
Cdd:PRK10811   744 VEETVAAEPVVQEVPAPRTELVKVPLPVVAQTAPEQDE 781
 
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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