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Conserved domains on  [gi|119587671|gb|EAW67267|]
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zinc finger protein 259, isoform CRA_a [Homo sapiens]

Protein Classification

ZPR1-type zinc finger protein( domain architecture ID 10505851)

ZPR1-type zinc finger protein similar to ZPR1 that interacts with the cytoplasmic domain of the inactive EGF receptor (EGFR) and is thought to inhibit the basal protein tyrosine kinase activity of EGFR

Gene Ontology:  GO:0008270
PubMed:  12665246|11179890

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 49-206 2.64e-79

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: 242.03  E-value: 2.64e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671   49 SLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRIQDQGVRYTLSVRALEDMNREVVKTDSAATRIP 128
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  129 ELDFEIPAFSQKGALTTVEGLITRAISGLE------QDQPARranKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGN 202
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDDLEtaddfeGDQPER---EDEVKEKIEEFIEKLDKAIEGKEPFTLILDDPSGN 157


                  ....
gi 119587671  203 SFVE 206
Cdd:pfam03367 158 SFIQ 161
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 257-413 3.06e-72

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: 223.92  E-value: 3.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  257 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIP 336
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  337 ELEFELGMAVLGGKFTTLEGLLKDIRE-LVTKNPFtLGDSSNPGQT--ERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSY 413
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDdLETADDF-EGDQPEREDEvkEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSF 159
 
Name Accession Description Interval E-value
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 49-206 2.64e-79

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: 242.03  E-value: 2.64e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671   49 SLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRIQDQGVRYTLSVRALEDMNREVVKTDSAATRIP 128
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  129 ELDFEIPAFSQKGALTTVEGLITRAISGLE------QDQPARranKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGN 202
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDDLEtaddfeGDQPER---EDEVKEKIEEFIEKLDKAIEGKEPFTLILDDPSGN 157


                  ....
gi 119587671  203 SFVE 206
Cdd:pfam03367 158 SFIQ 161
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 49-207 1.72e-75

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: 232.16  E-value: 1.72e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671    49 SLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRIQDQGVRYTLSVRALEDMNREVVKTDSAATRIP 128
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671   129 ELDFEIPAFSQKGALTTVEGLITRAISGLEQD-QPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVEN 207
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAiQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 257-413 3.06e-72

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: 223.92  E-value: 3.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  257 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIP 336
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  337 ELEFELGMAVLGGKFTTLEGLLKDIRE-LVTKNPFtLGDSSNPGQT--ERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSY 413
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDdLETADDF-EGDQPEREDEvkEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSF 159
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 257-413 3.59e-72

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: 223.68  E-value: 3.59e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671   257 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIP 336
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119587671   337 ELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSY 413
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAIQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSY 157
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 259-413 3.64e-32

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: 120.69  E-value: 3.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  259 CPECNAPAQTNMKLVQ-IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDASDMTRDLLKSETCSVEIPE 337
Cdd:TIGR00310   3 CPSCGGECETVMKTVNdIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119587671  338 L--EFELGMAvLGGKFTTLEGLLKDIRELVTKNPFTlgDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSY 413
Cdd:TIGR00310  81 LglDIEPGPT-SGGFITNLEGVLRRVEEELETAIRW--QSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSY 155
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 66-234 8.66e-29

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: 111.44  E-value: 8.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671   66 KIPFFREIIVSSFSCEHCGWNNTEIQSAGRIQDqgVRYTLSVRALEDMNREVVKTDSAATRIPELDFEI-PAFSQKGALT 144
Cdd:TIGR00310  19 DIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPELGLDIePGPTSGGFIT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  145 TVEGLITRaISGLEQDQPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKD-DALVITHYN 223
Cdd:TIGR00310  97 NLEGVLRR-VEEELETAIRWQSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQNVYAPKEIlSEEEIEDLK 175

                         170
                  ....*....|.
gi 119587671  224 RTRQQEEMLGL 234
Cdd:TIGR00310 176 TGKEINEDLGL 186
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
67-210 1.35e-27

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 108.08  E-value: 1.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  67 IPFFREIIVSSFSCEHCGWNNTEIqsagRIQDQG--VRYTLSVRALEDMNREVVKTDSAATRIPELDFEI---PAfSQkG 141
Cdd:COG1779   29 IPYFGEVLIITGRCSSCGYRFSDV----MILEQKepVRYTLKVEKEEDLNARVVRSSSGTIRIPELGLEIepgPA-SE-G 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671 142 ALTTVEGLITRAISGLEQdqpARRANKD-ATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHA 210
Cdd:COG1779  103 FITNVEGVLNRFEEVVET---ACKWAEDeEEKEKALEILEKIEEAKDGKRPFTLIIEDPLGNSAIISDKA 169
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
257-412 5.61e-21

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 89.98  E-value: 5.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671 257 TNCPECNapaQTNMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDASDMTRDLLKSETCS 332
Cdd:COG1779   10 VKCPVCG---GKTLKVIWqtynIPYFGEVLIITGRCSSCGYRFSDVMILEQKEP--VRYTLKVEKEEDLNARVVRSSSGT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671 333 VEIPELEFEL--GMAVLGgkF-TTLEGLLKDIRELVTknpFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPA 409
Cdd:COG1779   85 IRIPELGLEIepGPASEG--FiTNVEGVLNRFEEVVE---TACKWAEDEEEKEKALEILEKIEEAKDGKRPFTLIIEDPL 159


                 ...
gi 119587671 410 GNS 412
Cdd:COG1779  160 GNS 162
 
Name Accession Description Interval E-value
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 49-206 2.64e-79

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: 242.03  E-value: 2.64e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671   49 SLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRIQDQGVRYTLSVRALEDMNREVVKTDSAATRIP 128
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  129 ELDFEIPAFSQKGALTTVEGLITRAISGLE------QDQPARranKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGN 202
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDDLEtaddfeGDQPER---EDEVKEKIEEFIEKLDKAIEGKEPFTLILDDPSGN 157


                  ....
gi 119587671  203 SFVE 206
Cdd:pfam03367 158 SFIQ 161
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 49-207 1.72e-75

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: 232.16  E-value: 1.72e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671    49 SLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRIQDQGVRYTLSVRALEDMNREVVKTDSAATRIP 128
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671   129 ELDFEIPAFSQKGALTTVEGLITRAISGLEQD-QPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVEN 207
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAiQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 257-413 3.06e-72

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: 223.92  E-value: 3.06e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  257 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIP 336
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  337 ELEFELGMAVLGGKFTTLEGLLKDIRE-LVTKNPFtLGDSSNPGQT--ERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSY 413
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDdLETADDF-EGDQPEREDEvkEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSF 159
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 257-413 3.59e-72

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: 223.68  E-value: 3.59e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671   257 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIP 336
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119587671   337 ELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSY 413
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAIQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSY 157
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 259-413 3.64e-32

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: 120.69  E-value: 3.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  259 CPECNAPAQTNMKLVQ-IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDASDMTRDLLKSETCSVEIPE 337
Cdd:TIGR00310   3 CPSCGGECETVMKTVNdIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119587671  338 L--EFELGMAvLGGKFTTLEGLLKDIRELVTKNPFTlgDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSY 413
Cdd:TIGR00310  81 LglDIEPGPT-SGGFITNLEGVLRRVEEELETAIRW--QSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSY 155
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 66-234 8.66e-29

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: 111.44  E-value: 8.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671   66 KIPFFREIIVSSFSCEHCGWNNTEIQSAGRIQDqgVRYTLSVRALEDMNREVVKTDSAATRIPELDFEI-PAFSQKGALT 144
Cdd:TIGR00310  19 DIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPELGLDIePGPTSGGFIT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  145 TVEGLITRaISGLEQDQPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKD-DALVITHYN 223
Cdd:TIGR00310  97 NLEGVLRR-VEEELETAIRWQSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQNVYAPKEIlSEEEIEDLK 175

                         170
                  ....*....|.
gi 119587671  224 RTRQQEEMLGL 234
Cdd:TIGR00310 176 TGKEINEDLGL 186
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
67-210 1.35e-27

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 108.08  E-value: 1.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  67 IPFFREIIVSSFSCEHCGWNNTEIqsagRIQDQG--VRYTLSVRALEDMNREVVKTDSAATRIPELDFEI---PAfSQkG 141
Cdd:COG1779   29 IPYFGEVLIITGRCSSCGYRFSDV----MILEQKepVRYTLKVEKEEDLNARVVRSSSGTIRIPELGLEIepgPA-SE-G 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671 142 ALTTVEGLITRAISGLEQdqpARRANKD-ATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHA 210
Cdd:COG1779  103 FITNVEGVLNRFEEVVET---ACKWAEDeEEKEKALEILEKIEEAKDGKRPFTLIIEDPLGNSAIISDKA 169
zpr1_rel TIGR00340
ZPR1-related zinc finger protein; This model describes a strictly archaeal family homologous ...
 64-210 3.06e-25

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: 101.03  E-value: 3.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671   64 LTKIPFFREIIVSSFSCEHCGWNNTEIQSAGriQDQGVRYTLSVRALEDMNREVVKTDSAATRIPELDFEI-PAFSQKGA 142
Cdd:TIGR00340  15 DYDIPYFGKIMLSTYICEKCGYRSTDVYQLE--EKEPVRYIIKIENEDDLFTLVYRSRSATIRIPELGIKIePGPASQGY 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119587671  143 LTTVEGLITRAisgLEQDQPARRANKDATA-ERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHA 210
Cdd:TIGR00340  93 ISNIEGVLERI---EEVLDTASDDDEDDEAvKKCEEILKRIREVIEGKFKFTLIIEDPFGNSFIESEKA 158
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
257-412 5.61e-21

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 89.98  E-value: 5.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671 257 TNCPECNapaQTNMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDASDMTRDLLKSETCS 332
Cdd:COG1779   10 VKCPVCG---GKTLKVIWqtynIPYFGEVLIITGRCSSCGYRFSDVMILEQKEP--VRYTLKVEKEEDLNARVVRSSSGT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671 333 VEIPELEFEL--GMAVLGgkF-TTLEGLLKDIRELVTknpFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPA 409
Cdd:COG1779   85 IRIPELGLEIepGPASEG--FiTNVEGVLNRFEEVVE---TACKWAEDEEEKEKALEILEKIEEAKDGKRPFTLIIEDPL 159


                 ...
gi 119587671 410 GNS 412
Cdd:COG1779  160 GNS 162
zpr1_rel TIGR00340
ZPR1-related zinc finger protein; This model describes a strictly archaeal family homologous ...
 259-413 1.13e-14

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: 71.37  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  259 CPECNAPAqtnMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDASDMTRDLLKSETCSVE 334
Cdd:TIGR00340   1 CPVCGSRT---LKAVTydydIPYFGKIMLSTYICEKCGYRSTDVYQLEEKEP--VRYIIKIENEDDLFTLVYRSRSATIR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119587671  335 IPELEFEL---GMAvlGGKFTTLEGLLKDIRELVTKnpfTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGN 411
Cdd:TIGR00340  76 IPELGIKIepgPAS--QGYISNIEGVLERIEEVLDT---ASDDDEDDEAVKKCEEILKRIREVIEGKFKFTLIIEDPFGN 150


                  ..
gi 119587671  412 SY 413
Cdd:TIGR00340 151 SF 152
 
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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