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Conserved domains on  [gi|952556267|ref|NP_001304015|]
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zinc finger protein ZPR1 isoform 2 [Homo sapiens]

Protein Classification

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 ...
 203-362 1.56e-74

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: 229.08  E-value: 1.56e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267   203 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIP 282
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267   283 ELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQN 362
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAIQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 super family cl19251
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 58-153 9.60e-38

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.


The actual alignment was detected with superfamily member smart00709:

Pssm-ID: 450280  Cd Length: 160  Bit Score: 133.93  E-value: 9.60e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267    58 DMNREVVKTDSAATRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQD-QPARRANKDATAERIDEFIVKLKELKQVAS 136
Cdd:smart00709  64 DLNRDVVKSETATISIPELDLEIPPGPLGGFITTVEGLLSRVREVLSQAiQETRDDSDPETKEKIDEFLEKLKELIEGKE 143

                           90
                   ....*....|....*..
gi 952556267   137 PFTLIIDDPSGNSFVEN 153
Cdd:smart00709 144 PFTLILDDPAGNSYIQN 160
 
Name Accession Description Interval E-value
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 203-362 1.56e-74

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: 229.08  E-value: 1.56e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267   203 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIP 282
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267   283 ELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQN 362
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAIQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 203-361 4.83e-74

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: 227.78  E-value: 4.83e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  203 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIP 282
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  283 ELEFELGMAVLGGKFTTLEGLLKDIRE-LVTKNPFtLGDSSNPGQT--ERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSY 359
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDdLETADDF-EGDQPEREDEvkEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSF 159


                  ..
gi 952556267  360 LQ 361
Cdd:pfam03367 160 IQ 161
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 205-395 3.09e-45

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: 154.59  E-value: 3.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  205 CPECNAPAQTNMKLVQ-IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDASDMTRDLLKSETCSVEIPE 283
Cdd:TIGR00310   3 CPSCGGECETVMKTVNdIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  284 L--EFELGMAvLGGKFTTLEGLLKDIRELVTKNPFTlgDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQ 361
Cdd:TIGR00310  81 LglDIEPGPT-SGGFITNLEGVLRRVEEELETAIRW--QSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQ 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 952556267  362 NVYAPEDDP-EMKVERYKRTFDQNEELGLNDMKTE 395
Cdd:TIGR00310 158 NVYAPKEILsEEEIEDLKTGKEINEDLGLSDEEVE 192
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 58-153 9.60e-38

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: 133.93  E-value: 9.60e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267    58 DMNREVVKTDSAATRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQD-QPARRANKDATAERIDEFIVKLKELKQVAS 136
Cdd:smart00709  64 DLNRDVVKSETATISIPELDLEIPPGPLGGFITTVEGLLSRVREVLSQAiQETRDDSDPETKEKIDEFLEKLKELIEGKE 143

                           90
                   ....*....|....*..
gi 952556267   137 PFTLIIDDPSGNSFVEN 153
Cdd:smart00709 144 PFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 58-152 2.30e-37

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: 133.02  E-value: 2.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267   58 DMNREVVKTDSAATRIPELDFEIPAFSQKGALTTVEGLITRAISGLE------QDQPARranKDATAERIDEFIVKLKEL 131
Cdd:pfam03367  64 DLNRQVVKSDTATIRIPELDLEIPPGTLGGRITTVEGLLTRIIDDLEtaddfeGDQPER---EDEVKEKIEEFIEKLDKA 140

                          90       100
                  ....*....|....*....|.
gi 952556267  132 KQVASPFTLIIDDPSGNSFVE 152
Cdd:pfam03367 141 IEGKEPFTLILDDPSGNSFIQ 161
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
203-358 5.28e-21

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 89.98  E-value: 5.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267 203 TNCPECNapaQTNMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDASDMTRDLLKSETCS 278
Cdd:COG1779   10 VKCPVCG---GKTLKVIWqtynIPYFGEVLIITGRCSSCGYRFSDVMILEQKEP--VRYTLKVEKEEDLNARVVRSSSGT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267 279 VEIPELEFEL--GMAVLGgkF-TTLEGLLKDIRELVTknpFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPA 355
Cdd:COG1779   85 IRIPELGLEIepGPASEG--FiTNVEGVLNRFEEVVE---TACKWAEDEEEKEKALEILEKIEEAKDGKRPFTLIIEDPL 159


                 ...
gi 952556267 356 GNS 358
Cdd:COG1779  160 GNS 162
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
58-156 4.09e-16

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 76.11  E-value: 4.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  58 DMNREVVKTDSAATRIPELDFEI---PAfSQkGALTTVEGLITRAISGLEQdqpARRANKD-ATAERIDEFIVKLKELKQ 133
Cdd:COG1779   72 DLNARVVRSSSGTIRIPELGLEIepgPA-SE-GFITNVEGVLNRFEEVVET---ACKWAEDeEEKEKALEILEKIEEAKD 146

                         90       100
                 ....*....|....*....|...
gi 952556267 134 VASPFTLIIDDPSGNSFVENPHA 156
Cdd:COG1779  147 GKRPFTLIIEDPLGNSAIISDKA 169
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 55-180 5.54e-15

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: 72.92  E-value: 5.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267   55 YCN---DMNREVVKTDSAATRIPELDFEI-PAFSQKGALTTVEGLITRaISGLEQDQPARRANKDATAERIDEFIVKLKE 130
Cdd:TIGR00310  57 KIDdeaDLNRRVVKSESATIRIPELGLDIePGPTSGGFITNLEGVLRR-VEEELETAIRWQSEDEETKKRAEEILERLKE 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 952556267  131 LKQVASPFTLIIDDPSGNSFVENPHAPQKD-DALVITHYNRTRQQEEMLGL 180
Cdd:TIGR00310 136 AIEGKEKFTVILEDPLGGSYIQNVYAPKEIlSEEEIEDLKTGKEINEDLGL 186
 
Name Accession Description Interval E-value
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 203-362 1.56e-74

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: 229.08  E-value: 1.56e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267   203 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIP 282
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267   283 ELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQN 362
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAIQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 203-361 4.83e-74

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: 227.78  E-value: 4.83e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  203 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDASDMTRDLLKSETCSVEIP 282
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  283 ELEFELGMAVLGGKFTTLEGLLKDIRE-LVTKNPFtLGDSSNPGQT--ERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSY 359
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDdLETADDF-EGDQPEREDEvkEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSF 159


                  ..
gi 952556267  360 LQ 361
Cdd:pfam03367 160 IQ 161
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 205-395 3.09e-45

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: 154.59  E-value: 3.09e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  205 CPECNAPAQTNMKLVQ-IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDASDMTRDLLKSETCSVEIPE 283
Cdd:TIGR00310   3 CPSCGGECETVMKTVNdIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  284 L--EFELGMAvLGGKFTTLEGLLKDIRELVTKNPFTlgDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQ 361
Cdd:TIGR00310  81 LglDIEPGPT-SGGFITNLEGVLRRVEEELETAIRW--QSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQ 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 952556267  362 NVYAPEDDP-EMKVERYKRTFDQNEELGLNDMKTE 395
Cdd:TIGR00310 158 NVYAPKEILsEEEIEDLKTGKEINEDLGLSDEEVE 192
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 58-153 9.60e-38

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: 133.93  E-value: 9.60e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267    58 DMNREVVKTDSAATRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQD-QPARRANKDATAERIDEFIVKLKELKQVAS 136
Cdd:smart00709  64 DLNRDVVKSETATISIPELDLEIPPGPLGGFITTVEGLLSRVREVLSQAiQETRDDSDPETKEKIDEFLEKLKELIEGKE 143

                           90
                   ....*....|....*..
gi 952556267   137 PFTLIIDDPSGNSFVEN 153
Cdd:smart00709 144 PFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 58-152 2.30e-37

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: 133.02  E-value: 2.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267   58 DMNREVVKTDSAATRIPELDFEIPAFSQKGALTTVEGLITRAISGLE------QDQPARranKDATAERIDEFIVKLKEL 131
Cdd:pfam03367  64 DLNRQVVKSDTATIRIPELDLEIPPGTLGGRITTVEGLLTRIIDDLEtaddfeGDQPER---EDEVKEKIEEFIEKLDKA 140

                          90       100
                  ....*....|....*....|.
gi 952556267  132 KQVASPFTLIIDDPSGNSFVE 152
Cdd:pfam03367 141 IEGKEPFTLILDDPSGNSFIQ 161
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
203-358 5.28e-21

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 89.98  E-value: 5.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267 203 TNCPECNapaQTNMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDASDMTRDLLKSETCS 278
Cdd:COG1779   10 VKCPVCG---GKTLKVIWqtynIPYFGEVLIITGRCSSCGYRFSDVMILEQKEP--VRYTLKVEKEEDLNARVVRSSSGT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267 279 VEIPELEFEL--GMAVLGgkF-TTLEGLLKDIRELVTknpFTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPA 355
Cdd:COG1779   85 IRIPELGLEIepGPASEG--FiTNVEGVLNRFEEVVE---TACKWAEDEEEKEKALEILEKIEEAKDGKRPFTLIIEDPL 159


                 ...
gi 952556267 356 GNS 358
Cdd:COG1779  160 GNS 162
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
58-156 4.09e-16

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 76.11  E-value: 4.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  58 DMNREVVKTDSAATRIPELDFEI---PAfSQkGALTTVEGLITRAISGLEQdqpARRANKD-ATAERIDEFIVKLKELKQ 133
Cdd:COG1779   72 DLNARVVRSSSGTIRIPELGLEIepgPA-SE-GFITNVEGVLNRFEEVVET---ACKWAEDeEEKEKALEILEKIEEAKD 146

                         90       100
                 ....*....|....*....|...
gi 952556267 134 VASPFTLIIDDPSGNSFVENPHA 156
Cdd:COG1779  147 GKRPFTLIIEDPLGNSAIISDKA 169
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 55-180 5.54e-15

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: 72.92  E-value: 5.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267   55 YCN---DMNREVVKTDSAATRIPELDFEI-PAFSQKGALTTVEGLITRaISGLEQDQPARRANKDATAERIDEFIVKLKE 130
Cdd:TIGR00310  57 KIDdeaDLNRRVVKSESATIRIPELGLDIePGPTSGGFITNLEGVLRR-VEEELETAIRWQSEDEETKKRAEEILERLKE 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 952556267  131 LKQVASPFTLIIDDPSGNSFVENPHAPQKD-DALVITHYNRTRQQEEMLGL 180
Cdd:TIGR00310 136 AIEGKEKFTVILEDPLGGSYIQNVYAPKEIlSEEEIEDLKTGKEINEDLGL 186
zpr1_rel TIGR00340
ZPR1-related zinc finger protein; This model describes a strictly archaeal family homologous ...
 205-360 7.28e-15

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: 71.76  E-value: 7.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  205 CPECNAPAqtnMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDASDMTRDLLKSETCSVE 280
Cdd:TIGR00340   1 CPVCGSRT---LKAVTydydIPYFGKIMLSTYICEKCGYRSTDVYQLEEKEP--VRYIIKIENEDDLFTLVYRSRSATIR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 952556267  281 IPELEFEL---GMAvlGGKFTTLEGLLKDIRELVTKnpfTLGDSSNPGQTERLQEFSQKMDQIIEGNMKAHFIMDDPAGN 357
Cdd:TIGR00340  76 IPELGIKIepgPAS--QGYISNIEGVLERIEEVLDT---ASDDDEDDEAVKKCEEILKRIREVIEGKFKFTLIIEDPFGN 150


                  ...
gi 952556267  358 SYL 360
Cdd:TIGR00340 151 SFI 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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