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Conserved domains on  [gi|1039777553|ref|XP_017177519|]
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paternally-expressed gene 3 protein isoform X2 [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 13618199)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA03169 super family cl27451
hypothetical protein; Provisional
 943-1151 4.47e-05

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PHA03169:

Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.66  E-value: 4.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777553  943 RSELIEHQKIHDRERPSGSRHyERSVIRSLAPS--DPQTSYAQERFIQEQVRKFRAFGQRSTTSNNLSVQKIYAQ----- 1015
Cdd:PHA03169    16 RSSCRGHCKRHGGTREQAGRR-RGTAARAAKPAppAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQggpsg 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777553 1016 ---ETFNAEEPHDKETHGQKIHDKEPYGKEPSGKE-PHGDEPQDKEPLDQEMRSE-EPHDDKPHGQEPHDDKPHGQEPHG 1090
Cdd:PHA03169    95 sgsESVGSPTPSPSGSAEELASGLSPENTSGSSPEsPASHSPPPSPPSHPGPHEPaPPESHNPSPNQQPSSFLQPSHEDS 174

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039777553 1091 DEPhGQEPHGDEPHDKEPIDQEMRSEEPHSEESHGDEPHGEESHGQEKVEDATIQASVSEE 1151
Cdd:PHA03169   175 PEE-PEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHE 234
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1218-1240 8.77e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 8.77e-04
                           10        20
                   ....*....|....*....|...
gi 1039777553 1218 YECPKCGESFIHSSLLFEHQRVH 1240
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 931-953 4.25e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 4.25e-03
                           10        20
                   ....*....|....*....|...
gi 1039777553  931 FECQECGEAFARRSELIEHQKIH 953
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 459-481 9.61e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 9.61e-03
                           10        20
                   ....*....|....*....|...
gi 1039777553  459 FECKECGETFSRSAALAEHRQIH 481
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PHA03169 PHA03169
hypothetical protein; Provisional
 943-1151 4.47e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.66  E-value: 4.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777553  943 RSELIEHQKIHDRERPSGSRHyERSVIRSLAPS--DPQTSYAQERFIQEQVRKFRAFGQRSTTSNNLSVQKIYAQ----- 1015
Cdd:PHA03169    16 RSSCRGHCKRHGGTREQAGRR-RGTAARAAKPAppAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQggpsg 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777553 1016 ---ETFNAEEPHDKETHGQKIHDKEPYGKEPSGKE-PHGDEPQDKEPLDQEMRSE-EPHDDKPHGQEPHDDKPHGQEPHG 1090
Cdd:PHA03169    95 sgsESVGSPTPSPSGSAEELASGLSPENTSGSSPEsPASHSPPPSPPSHPGPHEPaPPESHNPSPNQQPSSFLQPSHEDS 174

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039777553 1091 DEPhGQEPHGDEPHDKEPIDQEMRSEEPHSEESHGDEPHGEESHGQEKVEDATIQASVSEE 1151
Cdd:PHA03169   175 PEE-PEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHE 234
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1218-1240 8.77e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 8.77e-04
                           10        20
                   ....*....|....*....|...
gi 1039777553 1218 YECPKCGESFIHSSLLFEHQRVH 1240
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 931-953 4.25e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 4.25e-03
                           10        20
                   ....*....|....*....|...
gi 1039777553  931 FECQECGEAFARRSELIEHQKIH 953
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 459-481 9.61e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 9.61e-03
                           10        20
                   ....*....|....*....|...
gi 1039777553  459 FECKECGETFSRSAALAEHRQIH 481
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PHA03169 PHA03169
hypothetical protein; Provisional
 943-1151 4.47e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.66  E-value: 4.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777553  943 RSELIEHQKIHDRERPSGSRHyERSVIRSLAPS--DPQTSYAQERFIQEQVRKFRAFGQRSTTSNNLSVQKIYAQ----- 1015
Cdd:PHA03169    16 RSSCRGHCKRHGGTREQAGRR-RGTAARAAKPAppAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQggpsg 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777553 1016 ---ETFNAEEPHDKETHGQKIHDKEPYGKEPSGKE-PHGDEPQDKEPLDQEMRSE-EPHDDKPHGQEPHDDKPHGQEPHG 1090
Cdd:PHA03169    95 sgsESVGSPTPSPSGSAEELASGLSPENTSGSSPEsPASHSPPPSPPSHPGPHEPaPPESHNPSPNQQPSSFLQPSHEDS 174

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039777553 1091 DEPhGQEPHGDEPHDKEPIDQEMRSEEPHSEESHGDEPHGEESHGQEKVEDATIQASVSEE 1151
Cdd:PHA03169   175 PEE-PEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVEHE 234
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 1218-1240 8.77e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.05  E-value: 8.77e-04
                           10        20
                   ....*....|....*....|...
gi 1039777553 1218 YECPKCGESFIHSSLLFEHQRVH 1240
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 931-953 4.25e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 36.12  E-value: 4.25e-03
                           10        20
                   ....*....|....*....|...
gi 1039777553  931 FECQECGEAFARRSELIEHQKIH 953
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03169 PHA03169
hypothetical protein; Provisional
 1022-1134 4.55e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.49  E-value: 4.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777553 1022 EPHDKETHGQKIHDKEPYGKEPSgkepHGDEPQDKEPLDQEmrSEEPHDDKPHGQEPHDDKPHGQEPHGDEPHgQEPHGD 1101
Cdd:PHA03169   148 EPAPPESHNPSPNQQPSSFLQPS----HEDSPEEPEPPTSE--PEPDSPGPPQSETPTSSPPPQSPPDEPGEP-QSPTPQ 220

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1039777553 1102 EPHDKEPIDQEMRSEEPHSEESHGDEPHGEESH 1134
Cdd:PHA03169   221 QAPSPNTQQAVEHEDEPTEPEREGPPFPGHRSH 253
PRK09565 PRK09565
heme-binding protein;
1068-1194 5.96e-03

heme-binding protein;


Pssm-ID: 236571 [Multi-domain]  Cd Length: 533  Bit Score: 41.34  E-value: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777553 1068 PHDDKPHGQEPHDDKPHGQEPHGDEPHgqepHGDEPHDKEPIDQEMRSEEPHSEESHGDEPHGEESHGQEKVEDATIQAS 1147
Cdd:PRK09565   262 PTATPEDAADGGTGGTHDAEEFGEHGH----HGGHPGGEDGEHPHGHEDSGGHHGSGGDNFDHYDRHVATTVRADGGRED 337

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777553 1148 VSEE---------------HQKDDAGDAIYECQDCGLGFTDLNDLTS---HQDTHSRKALVDSRE 1194
Cdd:PRK09565   338 SDEEirgeladagvyagqpHGEDVYALVLYSEADPDELFEEVEGLREnfdHYDTHVKTAVYEAEE 402
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 459-481 9.61e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 34.97  E-value: 9.61e-03
                           10        20
                   ....*....|....*....|...
gi 1039777553  459 FECKECGETFSRSAALAEHRQIH 481
Cdd:pfam00096    1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
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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