NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|154090939|ref|NP_064683|]
View 

insulinoma-associated protein 2 [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10442881)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
354-376 3.98e-05

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: 40.36  E-value: 3.98e-05
                          10        20
                  ....*....|....*....|...
gi 154090939  354 FVCPYCHKKFRRQAYLRKHLGTH 376
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 super family cl33720
large tegument protein UL36; Provisional
2-343 2.64e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939    2 PRGFLVKRTKRSGSSYRA-----RPVEPLFPPP-GPLAAQSSPEEPGR-------GLLGSPCLAPPQDDAEWGAGGGDGP 68
Cdd:PHA03247 2659 GRVSRPRRARRLGRAAQAssppqRPRRRAARPTvGSLTSLADPPPPPPtpepaphALVSATPLPPGPAAARQASPALPAA 2738
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939   69 GPSPARPAGPELRRAFLERCLRSPVSAESFPSATAFCSAAPAAVTSGEELVPPQVPVSVPIPVPGPAPHGLQRRGKGAPV 148
Cdd:PHA03247 2739 PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAAL 2818
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939  149 CASAPAAVRKPKavrrlsfadevTTSPVLGLKIKEEEPGAPARALGGVRTPLGEFICQLCKHQ-YADPFALAQHRCSRIV 227
Cdd:PHA03247 2819 PPAASPAGPLPP-----------PTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSpAAKPAAPARPPVRRLA 2887
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939  228 RVEyrCPECDKVFSCPANlashrrwhKPRPTPACAASKPPHAPLTPPDPSLATGKENGRvPRTDDQHPQAPDSSGDGQHR 307
Cdd:PHA03247 2888 RPA--VSRSTESFALPPD--------QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP-PRPQPPLAPTTDPAGAGEPS 2956
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 154090939  308 DSAARPGLQALVYPEAARPQAPYPEVILGRHGPGSS 343
Cdd:PHA03247 2957 GAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASS 2992
 
Name Accession Description Interval E-value
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
354-376 3.98e-05

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: 40.36  E-value: 3.98e-05
                          10        20
                  ....*....|....*....|...
gi 154090939  354 FVCPYCHKKFRRQAYLRKHLGTH 376
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
2-343 2.64e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939    2 PRGFLVKRTKRSGSSYRA-----RPVEPLFPPP-GPLAAQSSPEEPGR-------GLLGSPCLAPPQDDAEWGAGGGDGP 68
Cdd:PHA03247 2659 GRVSRPRRARRLGRAAQAssppqRPRRRAARPTvGSLTSLADPPPPPPtpepaphALVSATPLPPGPAAARQASPALPAA 2738
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939   69 GPSPARPAGPELRRAFLERCLRSPVSAESFPSATAFCSAAPAAVTSGEELVPPQVPVSVPIPVPGPAPHGLQRRGKGAPV 148
Cdd:PHA03247 2739 PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAAL 2818
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939  149 CASAPAAVRKPKavrrlsfadevTTSPVLGLKIKEEEPGAPARALGGVRTPLGEFICQLCKHQ-YADPFALAQHRCSRIV 227
Cdd:PHA03247 2819 PPAASPAGPLPP-----------PTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSpAAKPAAPARPPVRRLA 2887
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939  228 RVEyrCPECDKVFSCPANlashrrwhKPRPTPACAASKPPHAPLTPPDPSLATGKENGRvPRTDDQHPQAPDSSGDGQHR 307
Cdd:PHA03247 2888 RPA--VSRSTESFALPPD--------QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP-PRPQPPLAPTTDPAGAGEPS 2956
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 154090939  308 DSAARPGLQALVYPEAARPQAPYPEVILGRHGPGSS 343
Cdd:PHA03247 2957 GAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASS 2992
ZnF_C2H2 smart00355
zinc finger;
354-376 2.78e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 2.78e-03
                           10        20
                   ....*....|....*....|...
gi 154090939   354 FVCPYCHKKFRRQAYLRKHLGTH 376
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
231-253 3.65e-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: 3.65e-03
                          10        20
                  ....*....|....*....|...
gi 154090939  231 YRCPECDKVFSCPANLASHRRWH 253
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
354-376 3.98e-05

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: 40.36  E-value: 3.98e-05
                          10        20
                  ....*....|....*....|...
gi 154090939  354 FVCPYCHKKFRRQAYLRKHLGTH 376
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
PHA03247 PHA03247
large tegument protein UL36; Provisional
2-343 2.64e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939    2 PRGFLVKRTKRSGSSYRA-----RPVEPLFPPP-GPLAAQSSPEEPGR-------GLLGSPCLAPPQDDAEWGAGGGDGP 68
Cdd:PHA03247 2659 GRVSRPRRARRLGRAAQAssppqRPRRRAARPTvGSLTSLADPPPPPPtpepaphALVSATPLPPGPAAARQASPALPAA 2738
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939   69 GPSPARPAGPELRRAFLERCLRSPVSAESFPSATAFCSAAPAAVTSGEELVPPQVPVSVPIPVPGPAPHGLQRRGKGAPV 148
Cdd:PHA03247 2739 PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAAL 2818
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939  149 CASAPAAVRKPKavrrlsfadevTTSPVLGLKIKEEEPGAPARALGGVRTPLGEFICQLCKHQ-YADPFALAQHRCSRIV 227
Cdd:PHA03247 2819 PPAASPAGPLPP-----------PTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSpAAKPAAPARPPVRRLA 2887
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154090939  228 RVEyrCPECDKVFSCPANlashrrwhKPRPTPACAASKPPHAPLTPPDPSLATGKENGRvPRTDDQHPQAPDSSGDGQHR 307
Cdd:PHA03247 2888 RPA--VSRSTESFALPPD--------QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP-PRPQPPLAPTTDPAGAGEPS 2956
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 154090939  308 DSAARPGLQALVYPEAARPQAPYPEVILGRHGPGSS 343
Cdd:PHA03247 2957 GAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASS 2992
ZnF_C2H2 smart00355
zinc finger;
354-376 2.78e-03

zinc finger;


Pssm-ID: 197676  Cd Length: 23  Bit Score: 35.13  E-value: 2.78e-03
                           10        20
                   ....*....|....*....|...
gi 154090939   354 FVCPYCHKKFRRQAYLRKHLGTH 376
Cdd:smart00355   1 YRCPECGKVFKSKSALREHMRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
231-253 3.65e-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: 3.65e-03
                          10        20
                  ....*....|....*....|...
gi 154090939  231 YRCPECDKVFSCPANLASHRRWH 253
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH