ID   A0A3B3R306_9TELE        Unreviewed;      1088 AA.
AC   A0A3B3R306;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS50157};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000012066.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000012066.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   AlphaFoldDB; A0A3B3R306; -.
DR   STRING; 1676925.ENSPKIP00000012066; -.
DR   Ensembl; ENSPKIT00000036449.1; ENSPKIP00000012066.1; ENSPKIG00000025685.1.
DR   GeneTree; ENSGT00940000155341; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24403:SF102; RE1-SILENCING TRANSCRIPTION FACTOR; 1.
DR   PANTHER; PTHR24403; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   Pfam; PF13909; zf-H2C2_5; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          219..246
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          279..306
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          307..334
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          335..363
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          100..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          916..1048
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..582
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..744
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1012
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1088 AA;  123097 MW;  6B7D211A795049EC CRC64;
     MAAQPVYPIG VGMFTPVVSV PMAGEGQGVT DMAAPQLVML ANVALTSEGT NCESLTEEKQ
     MVELKTVGSG SYSDSEDEAL TRFSGFDGQA EAPLVVYDEA QPDPPCQTAA EPEPEPEETR
     NDQEGVAEPP EQDQSPAGVG KRKRIQRPVE PPKKKKPFHC KPCQYQAECE EDFVHHIRRH
     SAKKLIVVNG AEAEAEGAAK DSASSAEGGD GLVYTKGVIR CERCGYNTNR YDHYVAHLKH
     HTKEGDSQRV YKCTICTYTT ISQYHWKKHL RNHFPSKLYT CAQCCYFSDR KNNYVQHIRT
     HTGERPFRCP YCKYSSSQKT HLTRHMRTHS GERPFKCETC SYLAANQHEV TRHARQVHNG
     PKPLSCPHCQ YKTADRSNYK KHVELHINPR QFLCPVCSYA ASKKCNLQYH IKSRHPDCSE
     ITMDVSKVKL RVKKPDSNST YYNVDGNTQY VLTGIKERKG QPEKRSVKQG NATADEQQNL
     TPMNLSMRKS NRPASAPAAE KERKDKTSKK GEQNSEKAGT GKAEKGLAEE KGTEKQKEKC
     ERRERSGGRT TRMEKADCDG KQAESGLEKV EKKKEAKKTT KASRLSDGTV VKTPNRRGRK
     SAKMTTGSEE KDKMEKVEKK KEKAEKERME KERTEKARVE KERVEKKRLE KERVEKERLE
     KERVEQEKVE KERVEQEKAE RERVEKERLE KEKAERDRVE KERAEKERVE REKLEKEQAE
     RERVEKERTE REKAESKNKK TVKSDRSACQ SSPKVMKDVE DKDQGRDFEC WELPRKCESR
     EVANTYGKRK AEELEQSSHC QGTSEPSVSR KSRRKKAEDM PLQASSILRS KRKVLQTCQA
     TRGKDKPAKG LGLPVVVQLQ TKTKKVQSKK KQSLSLLEPS MVDENIVEQV LEGENPTVET
     DASAMEAEHQ VLIQTPQETT ANKDQHNVEA HLGLLRNPVD GVNEEERTEM EHGPVNSAPN
     EVPEARGKAL EPQKGEQGQP SSTLELPRTG HKPAETEEDE GIHSHDGSDI SDNVSEGSDD
     SGLSGSGKLA GPETPTEEVP PVPTATALPS HTCIFCDRTF PMEVEYRRHL NRHLVNVYYL
     ESAASEEQ
//