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Conserved domains on  [gi|270265864|ref|NP_001161851|]
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zinc finger protein ZIC 4 isoform 2 [Homo sapiens]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 16062894)

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

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  22803940|11361095|11179890|12665246|10940247
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf_ZIC pfam18366
Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family ...
 160-204 1.44e-22

Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family proteins found in Eukaryotes. In humans, there are five members of the Zic family that are involved in human congenital anomalies. One of them, ZIC3, causes X-linked heterotaxy (HTX1), which is a left-right axis disturbance that manifests as variable combinations of heart malformation, altered lung lobation, splenic abnormality and gastrointestinal malrotation. Zic faily proteins contain multiple zinc finger domains (ZFD), which are generally composed of five tandemly repeated C2H2 zinc finger (ZF) motifs. Sequence comparison analysis reveal that this N-terminal ZF (ZF1) domain of the Zic zinc finger domains is unique in that it possesses more amino acid residues (6-38 amino acids) between the two cysteine residues of the C2H2 motif compared to Gli and Glis ZF1s or any of the other ZFs (ZF2-5) in the Gli/Glis/Zic superfamily of proteins. Mutations in cysteine 253 (C253S) or histidine 286 (H286R) in ZIC3 ZF1, which are found in heterotaxy patients, result in extranuclear localization of the mutant ZIC3 protein. Furthermore, mutations in the evolutionarily conserved amino acid residues (C253, W255, C268, H281 and H286) of ZF1 generally impair nuclear localization.


:

Pssm-ID: 436441  Cd Length: 45  Bit Score: 89.37  E-value: 1.44e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 270265864  160 QPIKQELICKWLAADGTATPSLCSKTFSTMHELVTHVTVEHVGGP 204
Cdd:pfam18366   1 QPIKQELSCKWIDPEQPAPKKPCNKTFSTMHEIVTHLTVEHVGGP 45
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
180-326 1.40e-09

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265864 180 SLCSKTFSTMHELVTHVTVEHVGGPEQANHICFWEECPrqgKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENL 259
Cdd:COG5048  293 KQCNISFSRSSPLTRHLRSVNHSGESLKPFSCPYSLCG---KLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNN 369

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 270265864 260 KIHKRTH-----TGEKPFRCEFEGCERRFANSSDRKKHSHVHTSDKPYTCKVRGCDKCYTHPSSLRKHMKVH 326
Cdd:COG5048  370 EPPQSLQqykdlKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIH 441
 
Name Accession Description Interval E-value
zf_ZIC pfam18366
Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family ...
 160-204 1.44e-22

Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family proteins found in Eukaryotes. In humans, there are five members of the Zic family that are involved in human congenital anomalies. One of them, ZIC3, causes X-linked heterotaxy (HTX1), which is a left-right axis disturbance that manifests as variable combinations of heart malformation, altered lung lobation, splenic abnormality and gastrointestinal malrotation. Zic faily proteins contain multiple zinc finger domains (ZFD), which are generally composed of five tandemly repeated C2H2 zinc finger (ZF) motifs. Sequence comparison analysis reveal that this N-terminal ZF (ZF1) domain of the Zic zinc finger domains is unique in that it possesses more amino acid residues (6-38 amino acids) between the two cysteine residues of the C2H2 motif compared to Gli and Glis ZF1s or any of the other ZFs (ZF2-5) in the Gli/Glis/Zic superfamily of proteins. Mutations in cysteine 253 (C253S) or histidine 286 (H286R) in ZIC3 ZF1, which are found in heterotaxy patients, result in extranuclear localization of the mutant ZIC3 protein. Furthermore, mutations in the evolutionarily conserved amino acid residues (C253, W255, C268, H281 and H286) of ZF1 generally impair nuclear localization.


Pssm-ID: 436441  Cd Length: 45  Bit Score: 89.37  E-value: 1.44e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 270265864  160 QPIKQELICKWLAADGTATPSLCSKTFSTMHELVTHVTVEHVGGP 204
Cdd:pfam18366   1 QPIKQELSCKWIDPEQPAPKKPCNKTFSTMHEIVTHLTVEHVGGP 45
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
180-326 1.40e-09

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265864 180 SLCSKTFSTMHELVTHVTVEHVGGPEQANHICFWEECPrqgKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENL 259
Cdd:COG5048  293 KQCNISFSRSSPLTRHLRSVNHSGESLKPFSCPYSLCG---KLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNN 369

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 270265864 260 KIHKRTH-----TGEKPFRCEFEGCERRFANSSDRKKHSHVHTSDKPYTCKVRGCDKCYTHPSSLRKHMKVH 326
Cdd:COG5048  370 EPPQSLQqykdlKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
258-285 5.00e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 5.00e-04
                          10        20
                  ....*....|....*....|....*...
gi 270265864  258 NLKIHKRTHTGEKPFRCEFegCERRFAN 285
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPE--CGKSFKS 26
 
Name Accession Description Interval E-value
zf_ZIC pfam18366
Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family ...
 160-204 1.44e-22

Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family proteins found in Eukaryotes. In humans, there are five members of the Zic family that are involved in human congenital anomalies. One of them, ZIC3, causes X-linked heterotaxy (HTX1), which is a left-right axis disturbance that manifests as variable combinations of heart malformation, altered lung lobation, splenic abnormality and gastrointestinal malrotation. Zic faily proteins contain multiple zinc finger domains (ZFD), which are generally composed of five tandemly repeated C2H2 zinc finger (ZF) motifs. Sequence comparison analysis reveal that this N-terminal ZF (ZF1) domain of the Zic zinc finger domains is unique in that it possesses more amino acid residues (6-38 amino acids) between the two cysteine residues of the C2H2 motif compared to Gli and Glis ZF1s or any of the other ZFs (ZF2-5) in the Gli/Glis/Zic superfamily of proteins. Mutations in cysteine 253 (C253S) or histidine 286 (H286R) in ZIC3 ZF1, which are found in heterotaxy patients, result in extranuclear localization of the mutant ZIC3 protein. Furthermore, mutations in the evolutionarily conserved amino acid residues (C253, W255, C268, H281 and H286) of ZF1 generally impair nuclear localization.


Pssm-ID: 436441  Cd Length: 45  Bit Score: 89.37  E-value: 1.44e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 270265864  160 QPIKQELICKWLAADGTATPSLCSKTFSTMHELVTHVTVEHVGGP 204
Cdd:pfam18366   1 QPIKQELSCKWIDPEQPAPKKPCNKTFSTMHEIVTHLTVEHVGGP 45
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
180-326 1.40e-09

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 59.32  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265864 180 SLCSKTFSTMHELVTHVTVEHVGGPEQANHICFWEECPrqgKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENL 259
Cdd:COG5048  293 KQCNISFSRSSPLTRHLRSVNHSGESLKPFSCPYSLCG---KLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNN 369

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 270265864 260 KIHKRTH-----TGEKPFRCEFEGCERRFANSSDRKKHSHVHTSDKPYTCKVRGCDKCYTHPSSLRKHMKVH 326
Cdd:COG5048  370 EPPQSLQqykdlKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIH 441
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 238-324 2.17e-07

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 52.41  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265864 238 GEKPFPCPFPGCGKVFARSENLKIHKRthtgekpfrcefEG-CERRFANSSDRKKHSHVHTSDKPYTCKVrgCDKCYTHP 316
Cdd:COG5189  346 DGKPYKCPVEGCNKKYKNQNGLKYHML------------HGhQNQKLHENPSPEKMNIFSAKDKPYRCEV--CDKRYKNL 411


                 ....*...
gi 270265864 317 SSLRKHMK 324
Cdd:COG5189  412 NGLKYHRK 419
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
229-299 3.49e-05

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 45.46  E-value: 3.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 270265864 229 LVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFRCEFEGCERRFANSSDRKKHSHVHTSD 299
Cdd:COG5048   49 LTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSND 119
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
239-338 1.71e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 43.53  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265864 239 EKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFRCEFEGCERRFANSSDRKKHSHVHTSDKPYTCKVRGCDKCYTHPSS 318
Cdd:COG5048   29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSS 108

                         90       100
                 ....*....|....*....|
gi 270265864 319 LRKHMKVHGRSPPPSSGYDS 338
Cdd:COG5048  109 SLSSSSSNSNDNNLLSSHSL 128
zf-H2C2_2 pfam13465
Zinc-finger double domain;
258-285 5.00e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.97  E-value: 5.00e-04
                          10        20
                  ....*....|....*....|....*...
gi 270265864  258 NLKIHKRTHTGEKPFRCEFegCERRFAN 285
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPE--CGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
221-293 1.13e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.83  E-value: 1.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 270265864 221 KPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFRCEfegCERRFANSSDRKKHS 293
Cdd:COG5048  396 RNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCS---ILKSFRRDLDLSNHG 465
zf-H2C2_2 pfam13465
Zinc-finger double domain;
229-255 1.19e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.19e-03
                          10        20
                  ....*....|....*....|....*..
gi 270265864  229 LVNHIRVHTGEKPFPCPFpgCGKVFAR 255
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPE--CGKSFKS 26
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 243-332 2.14e-03

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 37.40  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270265864  243 PCPFPGCGKVFARSENLKIHKRTHTGE------KPFRCEFEGCERRFANSSDRKKHSHVHTSDKPYTcKVRGCDKCYTHP 316
Cdd:pfam15909   1 PCSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRYF-KCENCLLRFRTH 79

                          90
                  ....*....|....*....
gi 270265864  317 SSLRKHMKV---HGRSPPP 332
Cdd:pfam15909  80 RSLFKHLHVcaeHAQSPAP 98
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 302-326 4.20e-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: 34.20  E-value: 4.20e-03
                          10        20
                  ....*....|....*....|....*
gi 270265864  302 YTCKvrGCDKCYTHPSSLRKHMKVH 326
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 242-266 8.34e-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: 33.43  E-value: 8.34e-03
                          10        20
                  ....*....|....*....|....*
gi 270265864  242 FPCPfpGCGKVFARSENLKIHKRTH 266
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 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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