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Conserved domains on  [gi|12855344|dbj|BAB30299|]
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unnamed protein product, partial [Mus musculus]

Protein Classification

Zpr1 domain-containing protein( domain architecture ID 10653829)

Zpr1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 23-182 4.79e-79

Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein Zpr1. Also present in archaeal proteins;


:

Pssm-ID: 128949  Cd Length: 160  Bit Score: 234.08  E-value: 4.79e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344     23 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIP 102
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344    103 ELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPDQSEKLQEFSQKLGQIIEGKMKAHFIMNDPAGNSYLQN 182
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAIQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
 
Name Accession Description Interval E-value
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 23-182 4.79e-79

Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein Zpr1. Also present in archaeal proteins;


Pssm-ID: 128949  Cd Length: 160  Bit Score: 234.08  E-value: 4.79e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344     23 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIP 102
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344    103 ELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPDQSEKLQEFSQKLGQIIEGKMKAHFIMNDPAGNSYLQN 182
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAIQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 23-181 2.34e-76

ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is indeed known to be an essential protein in yeast. In quiescent cells, ZPR1 is localized to the cytoplasm. But in proliferating cells treated with EGF or with other mitogens, ZPR1 accumulates in the nucleolus. ZPR1 interacts with the cytoplasmic domain of the inactive EGF receptor (EGFR) and is thought to inhibit the basal protein tyrosine kinase activity of EGFR. This interaction is disrupted when cells are treated with EGF, though by themselves, inactive EGFRs are not sufficient to sequester ZPR1 to the cytoplasm. Upon stimulation by EGF, ZPR1 directly binds the eukaryotic translation elongation factor-1alpha (eEF-1alpha) to form ZPR1/eEF-1alpha complexes. These move into the nucleus, localising particularly at the nucleolus. Indeed, the interaction between ZPR1 and eEF-1alpha has been shown to be essential for normal cellular proliferation, and ZPR1 is thought to be involved in pre-ribosomal RNA expression. The ZPR1 domain consists of an elongation initiation factor 2-like zinc finger and a double-stranded beta helix with a helical hairpin insertion. ZPR1 binds preferentially to GDP-bound eEF1A but does not directly influence the kinetics of nucleotide exchange or GTP hydrolysis. The alignment for this family shows a domain of which there are two copies in ZPR1 proteins. This family also includes several hypothetical archaeal proteins (from both Crenarchaeota and Euryarchaeota), which only contain one copy of the aligned region. This similarity between ZPR1 and archaeal proteins was not previously noted.


Pssm-ID: 427263  Cd Length: 161  Bit Score: 227.39  E-value: 2.34e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344    23 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIP 102
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344   103 ELEFELGMAVLGGKFTTLEGLLKDIRE-LVTKNPFtLGDSSNPDQS--EKLQEFSQKLGQIIEGKMKAHFIMNDPAGNSY 179
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDdLETADDF-EGDQPEREDEvkEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSF 159


                  ..
gi 12855344   180 LQ 181
Cdd:pfam03367 160 IQ 161
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 25-215 4.67e-48

ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal genomes corresponds to a zinc finger-containing domain repeated as the N-terminal and C-terminal halves of the mouse protein ZPR1. ZPR1 is an experimentally proven zinc-binding protein that binds the tyrosine kinase domain of the epidermal growth factor receptor (EGFR); binding is inhibited by EGF stimulation and tyrosine phosphorylation, and activation by EGF is followed by some redistribution of ZPR1 to the nucleus. By analogy, other proteins with the ZPR1 zinc finger domain may be regulatory proteins that sense protein phosphorylation state and/or participate in signal transduction.


Pssm-ID: 273007  Cd Length: 192  Bit Score: 156.51  E-value: 4.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344    25 CPECNAPAQTNMKLVQ-IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDPSDMTRDLLKSETCSVEIPE 103
Cdd:TIGR00310   3 CPSCGGECETVMKTVNdIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344   104 L--EFELGMAvLGGKFTTLEGLLKDIRELVTKNPFTlgDSSNPDQSEKLQEFSQKLGQIIEGKMKAHFIMNDPAGNSYLQ 181
Cdd:TIGR00310  81 LglDIEPGPT-SGGFITNLEGVLRRVEEELETAIRW--QSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQ 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 12855344   182 NVYAPEDDP-EMKVERYKRTFDQNEELGLNDMKTE 215
Cdd:TIGR00310 158 NVYAPKEILsEEEIEDLKTGKEINEDLGLSDEEVE 192
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
22-178 1.63e-24

C4-type Zn-finger protein [General function prediction only];


Pssm-ID: 441385  Cd Length: 191  Bit Score: 95.76  E-value: 1.63e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344  22 NTNCPECNapaQTNMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDPSDMTRDLLKSETC 97
Cdd:COG1779   9 EVKCPVCG---GKTLKVIWqtynIPYFGEVLIITGRCSSCGYRFSDVMILEQKEP--VRYTLKVEKEEDLNARVVRSSSG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344  98 SVEIPELEFEL--GMAVLGgkF-TTLEGLLKDIRELVTknpFTLGDSSNPDQSEKLQEFSQKLGQIIEGKMKAHFIMNDP 174
Cdd:COG1779  84 TIRIPELGLEIepGPASEG--FiTNVEGVLNRFEEVVE---TACKWAEDEEEKEKALEILEKIEEAKDGKRPFTLIIEDP 158


                ....
gi 12855344 175 AGNS 178
Cdd:COG1779 159 LGNS 162
 
Name Accession Description Interval E-value
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 23-182 4.79e-79

Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein Zpr1. Also present in archaeal proteins;


Pssm-ID: 128949  Cd Length: 160  Bit Score: 234.08  E-value: 4.79e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344     23 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIP 102
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344    103 ELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPDQSEKLQEFSQKLGQIIEGKMKAHFIMNDPAGNSYLQN 182
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAIQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 23-181 2.34e-76

ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is indeed known to be an essential protein in yeast. In quiescent cells, ZPR1 is localized to the cytoplasm. But in proliferating cells treated with EGF or with other mitogens, ZPR1 accumulates in the nucleolus. ZPR1 interacts with the cytoplasmic domain of the inactive EGF receptor (EGFR) and is thought to inhibit the basal protein tyrosine kinase activity of EGFR. This interaction is disrupted when cells are treated with EGF, though by themselves, inactive EGFRs are not sufficient to sequester ZPR1 to the cytoplasm. Upon stimulation by EGF, ZPR1 directly binds the eukaryotic translation elongation factor-1alpha (eEF-1alpha) to form ZPR1/eEF-1alpha complexes. These move into the nucleus, localising particularly at the nucleolus. Indeed, the interaction between ZPR1 and eEF-1alpha has been shown to be essential for normal cellular proliferation, and ZPR1 is thought to be involved in pre-ribosomal RNA expression. The ZPR1 domain consists of an elongation initiation factor 2-like zinc finger and a double-stranded beta helix with a helical hairpin insertion. ZPR1 binds preferentially to GDP-bound eEF1A but does not directly influence the kinetics of nucleotide exchange or GTP hydrolysis. The alignment for this family shows a domain of which there are two copies in ZPR1 proteins. This family also includes several hypothetical archaeal proteins (from both Crenarchaeota and Euryarchaeota), which only contain one copy of the aligned region. This similarity between ZPR1 and archaeal proteins was not previously noted.


Pssm-ID: 427263  Cd Length: 161  Bit Score: 227.39  E-value: 2.34e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344    23 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIP 102
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344   103 ELEFELGMAVLGGKFTTLEGLLKDIRE-LVTKNPFtLGDSSNPDQS--EKLQEFSQKLGQIIEGKMKAHFIMNDPAGNSY 179
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDdLETADDF-EGDQPEREDEvkEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSF 159


                  ..
gi 12855344   180 LQ 181
Cdd:pfam03367 160 IQ 161
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 25-215 4.67e-48

ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal genomes corresponds to a zinc finger-containing domain repeated as the N-terminal and C-terminal halves of the mouse protein ZPR1. ZPR1 is an experimentally proven zinc-binding protein that binds the tyrosine kinase domain of the epidermal growth factor receptor (EGFR); binding is inhibited by EGF stimulation and tyrosine phosphorylation, and activation by EGF is followed by some redistribution of ZPR1 to the nucleus. By analogy, other proteins with the ZPR1 zinc finger domain may be regulatory proteins that sense protein phosphorylation state and/or participate in signal transduction.


Pssm-ID: 273007  Cd Length: 192  Bit Score: 156.51  E-value: 4.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344    25 CPECNAPAQTNMKLVQ-IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDPSDMTRDLLKSETCSVEIPE 103
Cdd:TIGR00310   3 CPSCGGECETVMKTVNdIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344   104 L--EFELGMAvLGGKFTTLEGLLKDIRELVTKNPFTlgDSSNPDQSEKLQEFSQKLGQIIEGKMKAHFIMNDPAGNSYLQ 181
Cdd:TIGR00310  81 LglDIEPGPT-SGGFITNLEGVLRRVEEELETAIRW--QSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQ 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 12855344   182 NVYAPEDDP-EMKVERYKRTFDQNEELGLNDMKTE 215
Cdd:TIGR00310 158 NVYAPKEILsEEEIEDLKTGKEINEDLGLSDEEVE 192
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
22-178 1.63e-24

C4-type Zn-finger protein [General function prediction only];


Pssm-ID: 441385  Cd Length: 191  Bit Score: 95.76  E-value: 1.63e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344  22 NTNCPECNapaQTNMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDPSDMTRDLLKSETC 97
Cdd:COG1779   9 EVKCPVCG---GKTLKVIWqtynIPYFGEVLIITGRCSSCGYRFSDVMILEQKEP--VRYTLKVEKEEDLNARVVRSSSG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344  98 SVEIPELEFEL--GMAVLGgkF-TTLEGLLKDIRELVTknpFTLGDSSNPDQSEKLQEFSQKLGQIIEGKMKAHFIMNDP 174
Cdd:COG1779  84 TIRIPELGLEIepGPASEG--FiTNVEGVLNRFEEVVE---TACKWAEDEEEKEKALEILEKIEEAKDGKRPFTLIIEDP 158


                ....
gi 12855344 175 AGNS 178
Cdd:COG1779 159 LGNS 162
zpr1_rel TIGR00340
ZPR1-related zinc finger protein; This model describes a strictly archaeal family homologous ...
 25-180 6.55e-17

ZPR1-related zinc finger protein; This model describes a strictly archaeal family homologous to the domain duplicated in the eukaryotic zinc-binding protein ZPR1. ZPR1 was shown experimentally to bind approximately two moles of zinc; each copy of the domain contains a putative zinc finger of the form CXXCX(25)CXXC. ZPR1 binds the tyrosine kinase domain of epidermal growth factor receptor, but is displaced by receptor activation and autophosphorylation after which it redistributes in part to the nucleus. The proteins described by this model by analogy may be suggested to play a role in signal transduction. A model ZPR1_znf (TIGR00310) has been created to describe the domain shared by this protein and ZPR1. [Unknown function, General]


Pssm-ID: 129440  Cd Length: 163  Bit Score: 74.84  E-value: 6.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344    25 CPECNAPAqtnMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDPSDMTRDLLKSETCSVE 100
Cdd:TIGR00340   1 CPVCGSRT---LKAVTydydIPYFGKIMLSTYICEKCGYRSTDVYQLEEKEP--VRYIIKIENEDDLFTLVYRSRSATIR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12855344   101 IPELEFEL---GMAvlGGKFTTLEGLLKDIRELVTknpfTLGDSSNPDQS-EKLQEFSQKLGQIIEGKMKAHFIMNDPAG 176
Cdd:TIGR00340  76 IPELGIKIepgPAS--QGYISNIEGVLERIEEVLD----TASDDDEDDEAvKKCEEILKRIREVIEGKFKFTLIIEDPFG 149


                  ....
gi 12855344   177 NSYL 180
Cdd:TIGR00340 150 NSFI 153
 
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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