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Conserved domains on  [gi|1370456617|ref|XP_024303636|]
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zinc finger protein 438 isoform X2 [Homo sapiens]

Protein Classification

zf-C2H2 and zf-C2H2_4 domain-containing protein( domain architecture ID 10443155)

zf-C2H2 and zf-C2H2_4 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 98-364 1.88e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617   98 PHVASAQPIQKPRmslpeNLKLPiPRYQPPRNSKASRKKPILIFPKSGCSKAPAQTQMCPQMSPSPPHHPELLYKPSPFE 177
Cdd:PHA03247  2641 HPPPTVPPPERPR-----DDPAP-GRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA 2714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617  178 EVPS------------------LEQAPASISTAALTNGSDHGDLRPPVTNTHGSLNPPATPASSTPEE-PAKQDLTALSG 238
Cdd:PHA03247  2715 LVSAtplppgpaaarqaspalpAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRlTRPAVASLSES 2794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617  239 KAHFVSKITSSKPSAVASEKFKEQVDLAKTMTNLSPTIlgNAVQLISSVPKGklPIPPYSRMKtmevykiKSDANIAGFS 318
Cdd:PHA03247  2795 RESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT--SAQPTAPPPPPG--PPPPSLPLG-------GSVAPGGDVR 2863

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1370456617  319 LPGPKADCDKIPSTTegfnaATKVASRLPVPQVSQQSacESAFCPP 364
Cdd:PHA03247  2864 RRPPSRSPAAKPAAP-----ARPPVRRLARPAVSRST--ESFALPP 2902
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 535-558 3.78e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


:

Pssm-ID: 464025  Cd Length: 24  Bit Score: 35.31  E-value: 3.78e-03
                          10        20
                  ....*....|....*....|....
gi 1370456617 535 YSCRICRKSYVRPGSLSTHMKLHH 558
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTHH 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 507-529 8.72e-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: 34.58  E-value: 8.72e-03
                          10        20
                  ....*....|....*....|...
gi 1370456617 507 HRCHVCNHHFQFKQHLRDHMNTH 529
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PHA03247 PHA03247
large tegument protein UL36; Provisional
 98-364 1.88e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617   98 PHVASAQPIQKPRmslpeNLKLPiPRYQPPRNSKASRKKPILIFPKSGCSKAPAQTQMCPQMSPSPPHHPELLYKPSPFE 177
Cdd:PHA03247  2641 HPPPTVPPPERPR-----DDPAP-GRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA 2714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617  178 EVPS------------------LEQAPASISTAALTNGSDHGDLRPPVTNTHGSLNPPATPASSTPEE-PAKQDLTALSG 238
Cdd:PHA03247  2715 LVSAtplppgpaaarqaspalpAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRlTRPAVASLSES 2794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617  239 KAHFVSKITSSKPSAVASEKFKEQVDLAKTMTNLSPTIlgNAVQLISSVPKGklPIPPYSRMKtmevykiKSDANIAGFS 318
Cdd:PHA03247  2795 RESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT--SAQPTAPPPPPG--PPPPSLPLG-------GSVAPGGDVR 2863

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1370456617  319 LPGPKADCDKIPSTTegfnaATKVASRLPVPQVSQQSacESAFCPP 364
Cdd:PHA03247  2864 RRPPSRSPAAKPAAP-----ARPPVRRLARPAVSRST--ESFALPP 2902
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 90-233 1.41e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.53  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617  90 GTFSLVALPHVASAQPIQKPRMSL-PENLKLPIPRYQPPRnskasrkKPILIFPKSGCSKAPAQTQMCPQMSPSPPHHPE 168
Cdd:pfam03154 202 SAPSVPPQGSPATSQPPNQTQSTAaPHTLIQQTPTLHPQR-------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQ 274

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370456617 169 LLYKPSPFEEVPSLEQAPASISTAALTNGSDHGDLRP------PVTNTHGSLNPPATPASSTPEEPAKQDL 233
Cdd:pfam03154 275 MPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPgpspaaPGQSQQRIHTPPSQSQLQSQQPPREQPL 345
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 535-558 3.78e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 35.31  E-value: 3.78e-03
                          10        20
                  ....*....|....*....|....
gi 1370456617 535 YSCRICRKSYVRPGSLSTHMKLHH 558
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTHH 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 507-529 8.72e-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: 34.58  E-value: 8.72e-03
                          10        20
                  ....*....|....*....|...
gi 1370456617 507 HRCHVCNHHFQFKQHLRDHMNTH 529
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
PHA03247 PHA03247
large tegument protein UL36; Provisional
 98-364 1.88e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617   98 PHVASAQPIQKPRmslpeNLKLPiPRYQPPRNSKASRKKPILIFPKSGCSKAPAQTQMCPQMSPSPPHHPELLYKPSPFE 177
Cdd:PHA03247  2641 HPPPTVPPPERPR-----DDPAP-GRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA 2714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617  178 EVPS------------------LEQAPASISTAALTNGSDHGDLRPPVTNTHGSLNPPATPASSTPEE-PAKQDLTALSG 238
Cdd:PHA03247  2715 LVSAtplppgpaaarqaspalpAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRlTRPAVASLSES 2794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617  239 KAHFVSKITSSKPSAVASEKFKEQVDLAKTMTNLSPTIlgNAVQLISSVPKGklPIPPYSRMKtmevykiKSDANIAGFS 318
Cdd:PHA03247  2795 RESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT--SAQPTAPPPPPG--PPPPSLPLG-------GSVAPGGDVR 2863

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1370456617  319 LPGPKADCDKIPSTTegfnaATKVASRLPVPQVSQQSacESAFCPP 364
Cdd:PHA03247  2864 RRPPSRSPAAKPAAP-----ARPPVRRLARPAVSRST--ESFALPP 2902
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
71-279 4.53e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 47.08  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617  71 KLLGMSTQNY------------ALMQVAgqegtfslvALPHVA-SAQPIQKPRMSLPENLKLPIPRYQPPRNSKASRKKP 137
Cdd:PRK14971  333 KLCNQCDLNYrasknkrllvelTLIQLA---------QLTQKGdDASGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPS 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617 138 ilifpKSGCSKAPAQTQMCPQMSPSPPHHPELlyKPSPFEEVPSLEQAPAsistaalTNGSDHGDLRPPVTNTHGSLNPP 217
Cdd:PRK14971  404 -----QSSAAAQPSAPQSATQPAGTPPTVSVD--PPAAVPVNPPSTAPQA-------VRPAQFKEEKKIPVSKVSSLGPS 469

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370456617 218 AtpasstpEEPAKQDLTALSGKAHFVskITSSKPSAV------------ASEKFKEQVDLAKTMTNLSPTILGN 279
Cdd:PRK14971  470 T-------LRPIQEKAEQATGNIKEA--PTGTQKEIFteedlqyywqefAGTRPQEEKALKETMINCRPKLLNG 534
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 90-233 1.41e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.53  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456617  90 GTFSLVALPHVASAQPIQKPRMSL-PENLKLPIPRYQPPRnskasrkKPILIFPKSGCSKAPAQTQMCPQMSPSPPHHPE 168
Cdd:pfam03154 202 SAPSVPPQGSPATSQPPNQTQSTAaPHTLIQQTPTLHPQR-------LPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQ 274

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370456617 169 LLYKPSPFEEVPSLEQAPASISTAALTNGSDHGDLRP------PVTNTHGSLNPPATPASSTPEEPAKQDL 233
Cdd:pfam03154 275 MPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPgpspaaPGQSQQRIHTPPSQSQLQSQQPPREQPL 345
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 535-558 3.78e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 35.31  E-value: 3.78e-03
                          10        20
                  ....*....|....*....|....
gi 1370456617 535 YSCRICRKSYVRPGSLSTHMKLHH 558
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKTHH 24
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 507-529 8.72e-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: 34.58  E-value: 8.72e-03
                          10        20
                  ....*....|....*....|...
gi 1370456617 507 HRCHVCNHHFQFKQHLRDHMNTH 529
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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