ID A0A2K5JD09_COLAP Unreviewed; 657 AA.
AC A0A2K5JD09;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Zinc finger protein 630 {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000026706.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000026706.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000256|ARBA:ARBA00006991}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_011794117.1; XM_011938727.1.
DR RefSeq; XP_011794118.1; XM_011938728.1.
DR AlphaFoldDB; A0A2K5JD09; -.
DR STRING; 336983.ENSCANP00000026706; -.
DR Ensembl; ENSCANT00000049718.1; ENSCANP00000026706.1; ENSCANG00000036777.1.
DR GeneID; 105509485; -.
DR KEGG; cang:105509485; -.
DR CTD; 57232; -.
DR OMA; KIYTGMK; -.
DR OrthoDB; 5246932at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 1.
DR Gene3D; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 13.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24390; ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR24390:SF245; ZINC FINGER PROTEIN 383-RELATED; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 12.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 8.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
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 8..79
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 263..290
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 291..318
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 319..346
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 347..374
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 375..402
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 403..430
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 431..458
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 459..486
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 487..514
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 515..542
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 543..570
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 571..598
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 599..626
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 627..654
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
SQ SEQUENCE 657 AA; 75474 MW; 1EA9005DA0AA3EBF CRC64;
MIESQEPVTF EDVAVDFTKE EWQQLNPAQK TLHRDVMLET YSHLVSVGCS GIKPDVIFKL
EHGKDPWIIE SELSRWIYSD RVKGLESSQQ IISGELLFQR EILERAPKDN SLYSVLKIWH
IDNQIDRYQG NQDRVLRQVT VVSHETLTDE TGSKYSAFGK MFNQCTDLAP SSQKFHKLDS
CENSLKSSSD LLNYNRSYAR KNPIERFGCG RPPRYNASCS VPEKEGFIHT GIEPYGDSQS
EKVLSHKQAH VQYKKVQARE KPNVCSMCGK GFIKKSQLII HQRIHTGEKP YICGDCRKAF
SEKSHLIVHQ RIHTGEKPYE CTECGRAFSQ KSPFIVHQRV HTGEKPYECF ECPKAFSQKS
HLIIHQRVHT REKSFECSEC GKAFCAMSHL FIHRITHTGE KPYECTECGK TFPRKTQLII
HQRTHTGEKP YKCNECGKTF CQQSHLIGHQ RIHTGEKPYV CTDCGKAFSQ KSHLTGHQRL
HTGEKPYMCT ECGKSFSQKS PLIIHQRIHT GEKPYECGEC GKAFSQKSPL IIHQRVHTGK
KPYECTECGR AFSLKSHLIL HQRGHTVEKP YECSECGKAF CGKSPLIIHQ KTHPREKPPE
CAESGMTFSR KSQMITYQRR YTGEKPSRCS DCGKAFCQHV YFTGHQNPYS KDTMYMC
//
