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Conserved domains on  [gi|1622866761|ref|XP_028689836|]
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zinc finger protein ZPR1 isoform X2 [Macaca mulatta]

Protein Classification

ZPR1-type zinc finger protein( domain architecture ID 10505857)

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

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 ...
 199-358 2.43e-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: 228.69  E-value: 2.43e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761  199 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIP 278
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761  279 ELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPCQKEGLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQN 358
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAIQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 1-148 1.41e-73

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: 226.62  E-value: 1.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761   1 MTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRVQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEIPAFS 80
Cdd:pfam03367  11 LTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIPELDLEIPPGT 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622866761  81 QKGALTTVEGLITRAISGLE------QDQPARranKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVE 148
Cdd:pfam03367  91 LGGRITTVEGLLTRIIDDLEtaddfeGDQPER---EDEVKEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSFIQ 161
 
Name Accession Description Interval E-value
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 199-358 2.43e-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: 228.69  E-value: 2.43e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761  199 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIP 278
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761  279 ELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPCQKEGLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQN 358
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAIQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 199-357 2.55e-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: 228.55  E-value: 2.55e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 199 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIP 278
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 279 ELEFELGMAVLGGKFTTLEGLLKDIRE-LVTKNPFtLGDSSNPCQ--KEGLQEFSQKMDQIIEGNMKAHFIMDDPAGNSY 355
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDdLETADDF-EGDQPEREDevKEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSF 159


                  ..
gi 1622866761 356 LQ 357
Cdd:pfam03367 160 IQ 161
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 1-148 1.41e-73

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: 226.62  E-value: 1.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761   1 MTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRVQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEIPAFS 80
Cdd:pfam03367  11 LTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIPELDLEIPPGT 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622866761  81 QKGALTTVEGLITRAISGLE------QDQPARranKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVE 148
Cdd:pfam03367  91 LGGRITTVEGLLTRIIDDLEtaddfeGDQPER---EDEVKEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSFIQ 161
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 2-149 1.19e-71

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: 221.76  E-value: 1.19e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761    2 TRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRVQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEIPAFSQ 81
Cdd:smart00709  12 TRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIPELDLEIPPGPL 91

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622866761   82 KGALTTVEGLITRAISGLEQD-QPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVEN 149
Cdd:smart00709  92 GGFITTVEGLLSRVREVLSQAiQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 201-391 6.25e-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: 153.82  E-value: 6.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 201 CPECNAPAQTNMKLVQ-IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDPSDMTRDLLKSETCSVEIPE 279
Cdd:TIGR00310   3 CPSCGGECETVMKTVNdIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 280 L--EFELGMAvLGGKFTTLEGLLKDIRELVTKNPFTlgDSSNPCQKEGLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQ 357
Cdd:TIGR00310  81 LglDIEPGPT-SGGFITNLEGVLRRVEEELETAIRW--QSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQ 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622866761 358 NVYAPEDDP-EMKVERYKRTFDQNEELGLNDMKTE 391
Cdd:TIGR00310 158 NVYAPKEILsEEEIEDLKTGKEINEDLGLSDEEVE 192
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
9-152 4.29e-30

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 114.63  E-value: 4.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761   9 IPFFREIIVSSFSCEHCGWNNTEIQSAgrvqDQG--VRYTLTVRAPEDMNREVVKTDSATTRIPELDFEI---PAfSQkG 83
Cdd:COG1779    29 IPYFGEVLIITGRCSSCGYRFSDVMIL----EQKepVRYTLKVEKEEDLNARVVRSSSGTIRIPELGLEIepgPA-SE-G 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761  84 ALTTVEGLITRAISGLEQdqpARRANKD-ATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHA 152
Cdd:COG1779   103 FITNVEGVLNRFEEVVET---ACKWAEDeEEKEKALEILEKIEEAKDGKRPFTLIIEDPLGNSAIISDKA 169
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 8-176 1.89e-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: 112.98  E-value: 1.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761   8 KIPFFREIIVSSFSCEHCGWNNTEIQSAGRVQDqgVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEI-PAFSQKGALT 86
Cdd:TIGR00310  19 DIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPELGLDIePGPTSGGFIT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761  87 TVEGLITRaISGLEQDQPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDS-LVITHYN 165
Cdd:TIGR00310  97 NLEGVLRR-VEEELETAIRWQSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQNVYAPKEILSeEEIEDLK 175

                         170
                  ....*....|.
gi 1622866761 166 RTQHQKEMLGL 176
Cdd:TIGR00310 176 TGKEINEDLGL 186
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
198-354 3.14e-22

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 93.06  E-value: 3.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 198 NTNCPECNapaQTNMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDPSDMTRDLLKSETC 273
Cdd:COG1779     9 EVKCPVCG---GKTLKVIWqtynIPYFGEVLIITGRCSSCGYRFSDVMILEQKEP--VRYTLKVEKEEDLNARVVRSSSG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 274 SVEIPELEFEL--GMAVLGgkF-TTLEGLLKDIRELVTknpFTLGDSSNPCQKEGLQEFSQKMDQIIEGNMKAHFIMDDP 350
Cdd:COG1779    84 TIRIPELGLEIepGPASEG--FiTNVEGVLNRFEEVVE---TACKWAEDEEEKEKALEILEKIEEAKDGKRPFTLIIEDP 158


                  ....
gi 1622866761 351 AGNS 354
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 ...
 199-358 2.43e-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: 228.69  E-value: 2.43e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761  199 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIP 278
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761  279 ELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPCQKEGLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQN 358
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAIQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 199-357 2.55e-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: 228.55  E-value: 2.55e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 199 TNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIP 278
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 279 ELEFELGMAVLGGKFTTLEGLLKDIRE-LVTKNPFtLGDSSNPCQ--KEGLQEFSQKMDQIIEGNMKAHFIMDDPAGNSY 355
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDdLETADDF-EGDQPEREDevKEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSF 159


                  ..
gi 1622866761 356 LQ 357
Cdd:pfam03367 160 IQ 161
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 1-148 1.41e-73

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: 226.62  E-value: 1.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761   1 MTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRVQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEIPAFS 80
Cdd:pfam03367  11 LTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIPELDLEIPPGT 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622866761  81 QKGALTTVEGLITRAISGLE------QDQPARranKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVE 148
Cdd:pfam03367  91 LGGRITTVEGLLTRIIDDLEtaddfeGDQPER---EDEVKEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSFIQ 161
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 2-149 1.19e-71

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: 221.76  E-value: 1.19e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761    2 TRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRVQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEIPAFSQ 81
Cdd:smart00709  12 TRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIPELDLEIPPGPL 91

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622866761   82 KGALTTVEGLITRAISGLEQD-QPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVEN 149
Cdd:smart00709  92 GGFITTVEGLLSRVREVLSQAiQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 201-391 6.25e-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: 153.82  E-value: 6.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 201 CPECNAPAQTNMKLVQ-IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDPSDMTRDLLKSETCSVEIPE 279
Cdd:TIGR00310   3 CPSCGGECETVMKTVNdIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 280 L--EFELGMAvLGGKFTTLEGLLKDIRELVTKNPFTlgDSSNPCQKEGLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQ 357
Cdd:TIGR00310  81 LglDIEPGPT-SGGFITNLEGVLRRVEEELETAIRW--QSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQ 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622866761 358 NVYAPEDDP-EMKVERYKRTFDQNEELGLNDMKTE 391
Cdd:TIGR00310 158 NVYAPKEILsEEEIEDLKTGKEINEDLGLSDEEVE 192
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
9-152 4.29e-30

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 114.63  E-value: 4.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761   9 IPFFREIIVSSFSCEHCGWNNTEIQSAgrvqDQG--VRYTLTVRAPEDMNREVVKTDSATTRIPELDFEI---PAfSQkG 83
Cdd:COG1779    29 IPYFGEVLIITGRCSSCGYRFSDVMIL----EQKepVRYTLKVEKEEDLNARVVRSSSGTIRIPELGLEIepgPA-SE-G 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761  84 ALTTVEGLITRAISGLEQdqpARRANKD-ATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHA 152
Cdd:COG1779   103 FITNVEGVLNRFEEVVET---ACKWAEDeEEKEKALEILEKIEEAKDGKRPFTLIIEDPLGNSAIISDKA 169
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 8-176 1.89e-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: 112.98  E-value: 1.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761   8 KIPFFREIIVSSFSCEHCGWNNTEIQSAGRVQDqgVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEI-PAFSQKGALT 86
Cdd:TIGR00310  19 DIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPELGLDIePGPTSGGFIT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761  87 TVEGLITRaISGLEQDQPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDS-LVITHYN 165
Cdd:TIGR00310  97 NLEGVLRR-VEEELETAIRWQSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQNVYAPKEILSeEEIEDLK 175

                         170
                  ....*....|.
gi 1622866761 166 RTQHQKEMLGL 176
Cdd:TIGR00310 176 TGKEINEDLGL 186
zpr1_rel TIGR00340
ZPR1-related zinc finger protein; This model describes a strictly archaeal family homologous ...
 6-152 3.67e-27

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: 105.65  E-value: 3.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761   6 LTKIPFFREIIVSSFSCEHCGWNNTEIQSAGrvQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEI-PAFSQKGA 84
Cdd:TIGR00340  15 DYDIPYFGKIMLSTYICEKCGYRSTDVYQLE--EKEPVRYIIKIENEDDLFTLVYRSRSATIRIPELGIKIePGPASQGY 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622866761  85 LTTVEGLITRAisgLEQDQPARRANKDATA-ERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHA 152
Cdd:TIGR00340  93 ISNIEGVLERI---EEVLDTASDDDEDDEAvKKCEEILKRIREVIEGKFKFTLIIEDPFGNSFIESEKA 158
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
198-354 3.14e-22

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 93.06  E-value: 3.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 198 NTNCPECNapaQTNMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDPSDMTRDLLKSETC 273
Cdd:COG1779     9 EVKCPVCG---GKTLKVIWqtynIPYFGEVLIITGRCSSCGYRFSDVMILEQKEP--VRYTLKVEKEEDLNARVVRSSSG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 274 SVEIPELEFEL--GMAVLGgkF-TTLEGLLKDIRELVTknpFTLGDSSNPCQKEGLQEFSQKMDQIIEGNMKAHFIMDDP 350
Cdd:COG1779    84 TIRIPELGLEIepGPASEG--FiTNVEGVLNRFEEVVE---TACKWAEDEEEKEKALEILEKIEEAKDGKRPFTLIIEDP 158


                  ....
gi 1622866761 351 AGNS 354
Cdd:COG1779   159 LGNS 162
zpr1_rel TIGR00340
ZPR1-related zinc finger protein; This model describes a strictly archaeal family homologous ...
 201-356 2.13e-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: 73.30  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 201 CPECNAPAqtnMKLVQ----IPHFKEVIIMATNCENCGHRTNEVKSGGAVEPlgTRITLHITDPSDMTRDLLKSETCSVE 276
Cdd:TIGR00340   1 CPVCGSRT---LKAVTydydIPYFGKIMLSTYICEKCGYRSTDVYQLEEKEP--VRYIIKIENEDDLFTLVYRSRSATIR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622866761 277 IPELEFEL---GMAvlGGKFTTLEGLLKDIRELVTKnpfTLGDSSNPCQKEGLQEFSQKMDQIIEGNMKAHFIMDDPAGN 353
Cdd:TIGR00340  76 IPELGIKIepgPAS--QGYISNIEGVLERIEEVLDT---ASDDDEDDEAVKKCEEILKRIREVIEGKFKFTLIIEDPFGN 150


                  ...
gi 1622866761 354 SYL 356
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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