ID   ZG66_XENLA              Reviewed;         606 AA.
AC   P18733; Q6LDC3;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Gastrula zinc finger protein XlCGF66.1;
DE   Flags: Fragment;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-132.
RX   PubMed=8464056; DOI=10.1006/jmbi.1993.1158;
RA   Nietfeld W., Conrad S., van Wijk I., Giltay R., Bouwmeester T., Knochel W.,
RA   Pieler T.;
RT   "Evidence for a clustered genomic organization of FAX-zinc finger protein
RT   encoding transcription units in Xenopus laevis.";
RL   J. Mol. Biol. 230:400-412(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-295.
RX   PubMed=2503827; DOI=10.1073/pnas.86.16.6097;
RA   Knoechel W., Poeting A., Koester M., el Baradi T., Nietfeld W.,
RA   Bouwmeester T., Pieler T.;
RT   "Evolutionary conserved modules associated with zinc fingers in Xenopus
RT   laevis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:6097-6100(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 240-606.
RX   PubMed=2509712; DOI=10.1016/0022-2836(89)90155-1;
RA   Nietfeld W., El-Baradi T., Mentzel H., Pieler T., Koester M., Poeting A.,
RA   Knoechel W.;
RT   "Second-order repeats in Xenopus laevis finger proteins.";
RL   J. Mol. Biol. 208:639-659(1989).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; S57882; AAB26030.1; -; Genomic_DNA.
DR   EMBL; M25873; AAA50020.1; -; mRNA.
DR   PIR; H33282; H33282.
DR   PIR; S06582; S06582.
DR   AlphaFoldDB; P18733; -.
DR   SMR; P18733; -.
DR   PRIDE; P18733; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 10.
DR   SMART; SM00355; ZnF_C2H2; 11.
DR   SUPFAM; SSF57667; SSF57667; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..>606
FT                   /note="Gastrula zinc finger protein XlCGF66.1"
FT                   /id="PRO_0000047805"
FT   ZN_FING         273..295
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         300..322
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         328..350
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         384..407
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         413..435
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         441..464
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         470..492
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         498..521
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         527..549
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         555..578
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         584..606
FT                   /note="C2H2-type 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         606
SQ   SEQUENCE   606 AA;  69087 MW;  5187755B9F1DC2FD CRC64;
     MGMWEEASDT GMKGKKKKKD KNEEEEERGK KERMVNLTLE MIYLLTGEHY IPRKKSDDGG
     ALHAPGSVIQ KENNKNDKKI LELMSNIIQL LTGEVAIRTH HVSIYFSLDE WDYIKGNKDL
     YEDGMKEEPQ QLHPLAVCEY KDESNVTAHM ESTLGCNNDG NLTKMSPVEQ PPPANGIKEE
     VASCEEINQS DCSINPFTEQ IQGTDTPTPI MGCSHFKTKV NKYDINSYWS PDESGITKST
     LHSKDSCNEG HKHLSHKSDY NKHQNPHKRQ KSFSCSKCGK CFSNLTSLHC HQKTHKGKKL
     LCLKCGKCFA TSSKLIIHRQ THMDKKHFSC SECRICFSKQ SSLARHQITH TEEKPLASSE
     CGKCFASLSE LTVHQRTNTG EKHDFCSECG KCFATSSQLI AHQQQVHIEV KPFSCTKCGK
     CFSYRSRLVR HQRTHTGVKP YSCSECGKCF ASSSHLIGHR QQVHMEGKTF FCSECGKYFL
     YQSQLVRHQR THTGEKPYSC SECGKCFATS SQLMAHQQQV HIEVKPFSCS ECGKYFLYRA
     HLVRHQRTHT GEKPDFCFEC GKCFATSLQL IAHQQQVHME VKQFSCSECG KSFLYRSHLA
     RHHRTH