ID   A0A3B3QBN6_9TELE        Unreviewed;       753 AA.
AC   A0A3B3QBN6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Transcriptional repressor CTCF-like {ECO:0000313|Ensembl:ENSPKIP00000003035.1};
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:ENSPKIP00000003035.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000003035.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A3B3QBN6; -.
DR   STRING; 1676925.ENSPKIP00000003035; -.
DR   Ensembl; ENSPKIT00000026992.1; ENSPKIP00000003035.1; ENSPKIG00000020697.1.
DR   GeneTree; ENSGT00940000156672; -.
DR   OrthoDB; 5398475at2759; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 9.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24379:SF81; CCCTC-BINDING FACTOR-LIKE; 1.
DR   PANTHER; PTHR24379; KRAB AND ZINC FINGER DOMAIN-CONTAINING; 1.
DR   Pfam; PF00096; zf-C2H2; 7.
DR   SMART; SM00355; ZnF_C2H2; 11.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          281..308
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          309..336
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          337..365
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          366..393
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          394..421
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          422..450
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          452..480
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          482..509
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          510..537
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          538..561
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          570..597
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          187..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..205
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..654
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..678
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  84672 MW;  A291742551D2D6EE CRC64;
     MEGNPADVVT DDCGDAFKAK DCKTYQRRRE GDEGEGLGAE LLQGVAQQVG VVGMNTGMEM
     MVVDSLVDQA LLQVKPPEGM EVGVAHSQVG VAMPTSATVD DTQIITLQVV NMEEQAGMGL
     GGLQLVQVPV GTVPVAGGPG VVDELQGTYV GTADTMAKDG EPIICHTLPL PEGFQVVKVG
     ANGEVETVEQ DELQPPDEPE PLEMQNEDPD YQPPTRKLKK AKKSRLRYNT EEGRDMDVSV
     YDFEEEQQEG MLSEVNAEKV VGNMKPPKPT KIKKKGVKKT FQCELCSYTC PRRSNLDRHM
     KSHTDERPHK CHLCGRAFRT VTLLRNHLNT HTGTRPHKCG DCDMAFVTSG ELVRHRRYKH
     THEKPFKCSM CDYSSVEVSK LKRHIRSHTG ERPFQCSLCS YASRDTYKLK RHMRTHSGEK
     PYECYICHAR FTQSGTMKMH ILQKHTENVA KFHCPHCDTV IARKSDLGVH LRKQHSYIES
     GRKCRYCDAV FHERYALIQH QKSHKNEKRF KCDQCEYACR QERHMVMHKR THTGEKPYAC
     SQCEKTFRQK QLLDMHFRRY HDPSFVPTSF VCSKCDKAFT RRNTMIRHTE NCTGVDSADA
     ENGAPPRRGR GGRKKKMRSR RDDDDDDDDD SEDHAEAELD DIDEDDDGLL PDVDMDMEME
     QAPPTIPIPA PVTPPVKRKR GRPPGRTNQP KPSPKAAIVQ VEDQNTVKER DPDGASTGVT
     TVEADAGAVH LPLVEAAPNG DLTPEMILSM MDR
//