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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2074815990 361 QPIKRELICKWLDPEELAGPpapadsgaKPCSKTFGTMHELVNHVTVEHVGGP 413
Cdd:pfam18366   1 QPIKQELSCKWIDPEQPAPK--------KPCNKTFSTMHEIVTHLTVEHVGGP 45

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2074815990 361 QPIKRELICKWLDPEELAGPpapadsgaKPCSKTFGTMHELVNHVTVEHVGGP 413
Cdd:pfam18366   1 QPIKQELSCKWIDPEQPAPK--------KPCNKTFSTMHEIVTHLTVEHVGGP 45

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*...
gi 2074815990 467 NLKIHKRTHTGEKPFKCEFdgCDRKFAN 494
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPE--CGKSFKS 26

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2074815990 361 QPIKRELICKWLDPEELAGPpapadsgaKPCSKTFGTMHELVNHVTVEHVGGP 413
Cdd:pfam18366   1 QPIKQELSCKWIDPEQPAPK--------KPCNKTFSTMHEIVTHLTVEHVGGP 45

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074815990 438 LINHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFDGCDRKFANSSDrKKHSHVHTSDKPYYCKIRG 517
Cdd:COG5048    49 LTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSS-SLSSSSSNSNDNNLLSSHS 127

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2074815990 518 CDKSYTHPS--SLRKHMKIHCKSPPPSPGALGYSSVGT---PVGDTLSPVLDPTRSRSSTLSPQVTN 579
Cdd:COG5048   128 LPPSSRDPQlpDLLSISNLRNNPLPGNNSSSVNTPQSNslhPPLPANSLSKDPSSNLSLLISSNVST 194

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074815990 447 GEKPFPCPFPGCGKVFARSENLKIHKRT-HtgekpfkcefdgCDRKFANSSDRKKHSHVHTSDKPYYCKIrgCDKSYTHP 525
Cdd:COG5189   346 DGKPYKCPVEGCNKKYKNQNGLKYHMLHgH------------QNQKLHENPSPEKMNIFSAKDKPYRCEV--CDKRYKNL 411

                  ....*...
gi 2074815990 526 SSLRKHMK 533
Cdd:COG5189   412 NGLKYHRK 419

Zinc-finger double domain;

                          10        20
                  ....*....|....*....|....*..
gi 2074815990 438 LINHIRVHTGEKPFPCPFpgCGKVFAR 464
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPE--CGKSFKS 26

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.

                          10        20
                  ....*....|....*....|....*
gi 2074815990 511 YYCKIrgCDKSYTHPSSLRKHMKIH 535
Cdd:pfam00096   1 YKCPD--CGKSFSRKSNLKRHLRTH 23

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

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2074815990 430 KPFKAKYKLINHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEfdgCDRKFANSSDRKKHS 502
Cdd:COG5048   396 RNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCS---ILKSFRRDLDLSNHG 465