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Conserved domains on  [gi|18858239|ref|NP_572532|]
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Zpr1 [Drosophila melanogaster]

Protein Classification

Zpr1 domain-containing protein( domain architecture ID 10653829)

Zpr1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 41-199 5.23e-76

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


:

Pssm-ID: 128949  Cd Length: 160  Bit Score: 234.47  E-value: 5.23e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239     41 SACMNCFETGVTRLLPTKIPFFREVVLMSFKCDHCGHINNEMQSASEIQKSGIRIELRVQSVADLNRRVVRSDNSSISIP 120
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    121 EIELEIPVQSQKGEVTTVEGIIERTIAGLSQD-QEKRRIDHPETAASIEKYIERLHRLKEVTTPFQVLLEDISGNSFIEN 199
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAiQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 259-416 3.79e-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: 229.85  E-value: 3.79e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    259 TNCPSCQAPCETNMKLTNIPHFKEVVIMATVCGACGHKTNEVKSGGGVEAQGVRFRVQIASREDLTRDVLKSETCSMSIP 338
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    339 ELDLEVGPHALCGRFTTVEGLLVAMRDQLDG--TLFHDSADDATKQQMQRFLDTFEDVMNLKRVITLVLEDPAGNTYVQS 416
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQaiQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
 
Name Accession Description Interval E-value
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 41-199 5.23e-76

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


Pssm-ID: 128949  Cd Length: 160  Bit Score: 234.47  E-value: 5.23e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239     41 SACMNCFETGVTRLLPTKIPFFREVVLMSFKCDHCGHINNEMQSASEIQKSGIRIELRVQSVADLNRRVVRSDNSSISIP 120
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    121 EIELEIPVQSQKGEVTTVEGIIERTIAGLSQD-QEKRRIDHPETAASIEKYIERLHRLKEVTTPFQVLLEDISGNSFIEN 199
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAiQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 259-416 3.79e-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: 229.85  E-value: 3.79e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    259 TNCPSCQAPCETNMKLTNIPHFKEVVIMATVCGACGHKTNEVKSGGGVEAQGVRFRVQIASREDLTRDVLKSETCSMSIP 338
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    339 ELDLEVGPHALCGRFTTVEGLLVAMRDQLDG--TLFHDSADDATKQQMQRFLDTFEDVMNLKRVITLVLEDPAGNTYVQS 416
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQaiQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 259-415 5.45e-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: 227.01  E-value: 5.45e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   259 TNCPSCQAPCETNMKLTNIPHFKEVVIMATVCGACGHKTNEVKSGGGVEAQGVRFRVQIASREDLTRDVLKSETCSMSIP 338
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   339 ELDLEVGPHALCGRFTTVEGLLVAMRDQLDGTLF--HDSAD--DATKQQMQRFLDTFEDVMNLKRVITLVLEDPAGNTYV 414
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDDLETADDfeGDQPEreDEVKEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSFI 160


                  .
gi 18858239   415 Q 415
Cdd:pfam03367 161 Q 161
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 41-198 8.72e-69

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: 216.22  E-value: 8.72e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    41 SACMNCFETGVTRLLPTKIPFFREVVLMSFKCDHCGHINNEMQSASEIQKSGIRIELRVQSVADLNRRVVRSDNSSISIP 120
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   121 EIELEIPVQSQKGEVTTVEGIIERTIAGL------SQDQEKRridHPETAASIEKYIERLHRLKEVTTPFQVLLEDISGN 194
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDDLetaddfEGDQPER---EDEVKEKIEEFIEKLDKAIEGKEPFTLILDDPSGN 157


                  ....
gi 18858239   195 SFIE 198
Cdd:pfam03367 158 SFIQ 161
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 261-451 1.15e-39

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: 141.10  E-value: 1.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   261 CPSCQAPCETNMKLTN-IPHFKEVVIMATVCGACGHKTNEVKSGGGVEAqgVRFRVQIASREDLTRDVLKSETCSMSIPE 339
Cdd:TIGR00310   3 CPSCGGECETVMKTVNdIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   340 LDLEVGP-HALCGRFTTVEGLLVAMRDQLDGTLFHDSADDATKQQMQRFLDTFEDVMNLKRVITLVLEDPAGNTYVQSLS 418
Cdd:TIGR00310  81 LGLDIEPgPTSGGFITNLEGVLRRVEEELETAIRWQSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQNVY 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 18858239   419 DDDSEPdDKLTVERYDRSYEDNEDLGLNDMKTE 451
Cdd:TIGR00310 161 APKEIL-SEEEIEDLKTGKEINEDLGLSDEEVE 192
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 43-232 1.55e-25

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: 102.97  E-value: 1.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    43 CMNCFETGVTRLLP-TKIPFFREVVLMSFKCDHCGHINNEMQSASEIQKSgiRIELRVQSVADLNRRVVRSDNSSISIPE 121
Cdd:TIGR00310   3 CPSCGGECETVMKTvNDIPYFGEVLETSTICEHCGYRSNDVKTLGAKEPK--RYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   122 IELEI-PVQSQKGEVTTVEGIIERTIAGLsQDQEKRRIDHPETAASIEKYIERLHRLKEVTTPFQVLLEDISGNSFIENP 200
Cdd:TIGR00310  81 LGLDIePGPTSGGFITNLEGVLRRVEEEL-ETAIRWQSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQNV 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 18858239   201 LAPAADPQLKT-SYFTRSQQQNEQLGLYEQNHE 232
Cdd:TIGR00310 160 YAPKEILSEEEiEDLKTGKEINEDLGLSDEEVE 192
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
59-197 1.07e-23

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 97.68  E-value: 1.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239  59 IPFFREVVLMSFKCDHCGHINNEMQSASeiQKSGIRIELRVQSVADLNRRVVRSDNSSISIPEIELEI---PVqSQkGEV 135
Cdd:COG1779  29 IPYFGEVLIITGRCSSCGYRFSDVMILE--QKEPVRYTLKVEKEEDLNARVVRSSSGTIRIPELGLEIepgPA-SE-GFI 104

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18858239 136 TTVEGIIER------TIAGLSQDQEKRRIdhpetaasIEKYIERLHRLKEVTTPFQVLLEDISGNSFI 197
Cdd:COG1779 105 TNVEGVLNRfeevveTACKWAEDEEEKEK--------ALEILEKIEEAKDGKRPFTLIIEDPLGNSAI 164
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
258-444 1.07e-22

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 94.99  E-value: 1.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239 258 PTNCPSCQapcETNMKLT----NIPHFKEVVIMATVCGACGHKTNEVKSGGGVEAqgVRFRVQIASREDLTRDVLKSETC 333
Cdd:COG1779   9 EVKCPVCG---GKTLKVIwqtyNIPYFGEVLIITGRCSSCGYRFSDVMILEQKEP--VRYTLKVEKEEDLNARVVRSSSG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239 334 SMSIPELDLEVGPHALC-GRFTTVEGLLVAMRDQLDgTLFHDSADDATKQQMQRFLDTFEDVMNLKRVITLVLEDPAGNT 412
Cdd:COG1779  84 TIRIPELGLEIEPGPASeGFITNVEGVLNRFEEVVE-TACKWAEDEEEKEKALEILEKIEEAKDGKRPFTLIIEDPLGNS 162

                       170       180       190
                ....*....|....*....|....*....|..
gi 18858239 413 YVQSlsdddsepdDKLTVERYDRsyEDNEDLG 444
Cdd:COG1779 163 AIIS---------DKAKKEKLTE--EEAEKLK 183
 
Name Accession Description Interval E-value
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 41-199 5.23e-76

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


Pssm-ID: 128949  Cd Length: 160  Bit Score: 234.47  E-value: 5.23e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239     41 SACMNCFETGVTRLLPTKIPFFREVVLMSFKCDHCGHINNEMQSASEIQKSGIRIELRVQSVADLNRRVVRSDNSSISIP 120
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    121 EIELEIPVQSQKGEVTTVEGIIERTIAGLSQD-QEKRRIDHPETAASIEKYIERLHRLKEVTTPFQVLLEDISGNSFIEN 199
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQAiQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
Zpr1 smart00709
Duplicated domain in the epidermal growth factor- and elongation factor-1alpha-binding protein ...
 259-416 3.79e-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: 229.85  E-value: 3.79e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    259 TNCPSCQAPCETNMKLTNIPHFKEVVIMATVCGACGHKTNEVKSGGGVEAQGVRFRVQIASREDLTRDVLKSETCSMSIP 338
Cdd:smart00709   1 SDCPSCGGNGTTRMLLTSIPYFREVIIMSFECEHCGYRNNEVKSGGAIEPKGTRITLKVESPEDLNRDVVKSETATISIP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    339 ELDLEVGPHALCGRFTTVEGLLVAMRDQLDG--TLFHDSADDATKQQMQRFLDTFEDVMNLKRVITLVLEDPAGNTYVQS 416
Cdd:smart00709  81 ELDLEIPPGPLGGFITTVEGLLSRVREVLSQaiQETRDDSDPETKEKIDEFLEKLKELIEGKEPFTLILDDPAGNSYIQN 160
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 259-415 5.45e-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: 227.01  E-value: 5.45e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   259 TNCPSCQAPCETNMKLTNIPHFKEVVIMATVCGACGHKTNEVKSGGGVEAQGVRFRVQIASREDLTRDVLKSETCSMSIP 338
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   339 ELDLEVGPHALCGRFTTVEGLLVAMRDQLDGTLF--HDSAD--DATKQQMQRFLDTFEDVMNLKRVITLVLEDPAGNTYV 414
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDDLETADDfeGDQPEreDEVKEKIEEFIEKLDKAIEGKEPFTLILDDPSGNSFI 160


                  .
gi 18858239   415 Q 415
Cdd:pfam03367 161 Q 161
zf-ZPR1 pfam03367
ZPR1 zinc-finger domain; The zinc-finger protein ZPR1 is ubiquitous among eukaryotes. It is ...
 41-198 8.72e-69

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: 216.22  E-value: 8.72e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    41 SACMNCFETGVTRLLPTKIPFFREVVLMSFKCDHCGHINNEMQSASEIQKSGIRIELRVQSVADLNRRVVRSDNSSISIP 120
Cdd:pfam03367   1 SLCPNCGENGLTRMLLTNIPYFKEVIIMSFECEHCGYKNNEVKSGGEIQPKGVRITLKVESEEDLNRQVVKSDTATIRIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   121 EIELEIPVQSQKGEVTTVEGIIERTIAGL------SQDQEKRridHPETAASIEKYIERLHRLKEVTTPFQVLLEDISGN 194
Cdd:pfam03367  81 ELDLEIPPGTLGGRITTVEGLLTRIIDDLetaddfEGDQPER---EDEVKEKIEEFIEKLDKAIEGKEPFTLILDDPSGN 157


                  ....
gi 18858239   195 SFIE 198
Cdd:pfam03367 158 SFIQ 161
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 261-451 1.15e-39

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: 141.10  E-value: 1.15e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   261 CPSCQAPCETNMKLTN-IPHFKEVVIMATVCGACGHKTNEVKSGGGVEAqgVRFRVQIASREDLTRDVLKSETCSMSIPE 339
Cdd:TIGR00310   3 CPSCGGECETVMKTVNdIPYFGEVLETSTICEHCGYRSNDVKTLGAKEP--KRYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   340 LDLEVGP-HALCGRFTTVEGLLVAMRDQLDGTLFHDSADDATKQQMQRFLDTFEDVMNLKRVITLVLEDPAGNTYVQSLS 418
Cdd:TIGR00310  81 LGLDIEPgPTSGGFITNLEGVLRRVEEELETAIRWQSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQNVY 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 18858239   419 DDDSEPdDKLTVERYDRSYEDNEDLGLNDMKTE 451
Cdd:TIGR00310 161 APKEIL-SEEEIEDLKTGKEINEDLGLSDEEVE 192
ZPR1_znf TIGR00310
ZPR1 zinc finger domain; An orthologous protein found once in each of the completed archaeal ...
 43-232 1.55e-25

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: 102.97  E-value: 1.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239    43 CMNCFETGVTRLLP-TKIPFFREVVLMSFKCDHCGHINNEMQSASEIQKSgiRIELRVQSVADLNRRVVRSDNSSISIPE 121
Cdd:TIGR00310   3 CPSCGGECETVMKTvNDIPYFGEVLETSTICEHCGYRSNDVKTLGAKEPK--RYILKIDDEADLNRRVVKSESATIRIPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239   122 IELEI-PVQSQKGEVTTVEGIIERTIAGLsQDQEKRRIDHPETAASIEKYIERLHRLKEVTTPFQVLLEDISGNSFIENP 200
Cdd:TIGR00310  81 LGLDIePGPTSGGFITNLEGVLRRVEEEL-ETAIRWQSEDEETKKRAEEILERLKEAIEGKEKFTVILEDPLGGSYIQNV 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 18858239   201 LAPAADPQLKT-SYFTRSQQQNEQLGLYEQNHE 232
Cdd:TIGR00310 160 YAPKEILSEEEiEDLKTGKEINEDLGLSDEEVE 192
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
59-197 1.07e-23

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 97.68  E-value: 1.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239  59 IPFFREVVLMSFKCDHCGHINNEMQSASeiQKSGIRIELRVQSVADLNRRVVRSDNSSISIPEIELEI---PVqSQkGEV 135
Cdd:COG1779  29 IPYFGEVLIITGRCSSCGYRFSDVMILE--QKEPVRYTLKVEKEEDLNARVVRSSSGTIRIPELGLEIepgPA-SE-GFI 104

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18858239 136 TTVEGIIER------TIAGLSQDQEKRRIdhpetaasIEKYIERLHRLKEVTTPFQVLLEDISGNSFI 197
Cdd:COG1779 105 TNVEGVLNRfeevveTACKWAEDEEEKEK--------ALEILEKIEEAKDGKRPFTLIIEDPLGNSAI 164
Zpr1 COG1779
C4-type Zn-finger protein [General function prediction only];
258-444 1.07e-22

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


Pssm-ID: 441385  Cd Length: 191  Bit Score: 94.99  E-value: 1.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239 258 PTNCPSCQapcETNMKLT----NIPHFKEVVIMATVCGACGHKTNEVKSGGGVEAqgVRFRVQIASREDLTRDVLKSETC 333
Cdd:COG1779   9 EVKCPVCG---GKTLKVIwqtyNIPYFGEVLIITGRCSSCGYRFSDVMILEQKEP--VRYTLKVEKEEDLNARVVRSSSG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858239 334 SMSIPELDLEVGPHALC-GRFTTVEGLLVAMRDQLDgTLFHDSADDATKQQMQRFLDTFEDVMNLKRVITLVLEDPAGNT 412
Cdd:COG1779  84 TIRIPELGLEIEPGPASeGFITNVEGVLNRFEEVVE-TACKWAEDEEEKEKALEILEKIEEAKDGKRPFTLIIEDPLGNS 162

                       170       180       190
                ....*....|....*....|....*....|..
gi 18858239 413 YVQSlsdddsepdDKLTVERYDRsyEDNEDLG 444
Cdd:COG1779 163 AIIS---------DKAKKEKLTE--EEAEKLK 183
 
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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