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Database: UniProt
Entry: A0A2K5K8Z7_COLAP
LinkDB: A0A2K5K8Z7_COLAP
Original site: A0A2K5K8Z7_COLAP 
ID   A0A2K5K8Z7_COLAP        Unreviewed;       610 AA.
AC   A0A2K5K8Z7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Zinc finger protein 274 {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:ENSCANP00000037564.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000037564.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000256|ARBA:ARBA00006991}.
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DR   RefSeq; XP_011814487.1; XM_011959097.1.
DR   AlphaFoldDB; A0A2K5K8Z7; -.
DR   Ensembl; ENSCANT00000060816.1; ENSCANP00000037564.1; ENSCANG00000042458.1.
DR   GeneID; 105524016; -.
DR   CTD; 10782; -.
DR   OMA; VEDVTWM; -.
DR   OrthoDB; 5261021at2759; -.
DR   Proteomes; UP000233080; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd07765; KRAB_A-box; 1.
DR   CDD; cd07936; SCAN; 1.
DR   Gene3D; 6.10.140.140; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR   Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 1.
DR   InterPro; IPR002016; Haem_peroxidase.
DR   InterPro; IPR001909; KRAB.
DR   InterPro; IPR036051; KRAB_dom_sf.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR23232; KRAB DOMAIN C2H2 ZINC FINGER; 1.
DR   PANTHER; PTHR23232:SF90; KRAB DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00349; KRAB; 2.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   PROSITE; PS50805; KRAB; 2.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          1..43
FT                   /note="KRAB"
FT                   /evidence="ECO:0000259|PROSITE:PS50805"
FT   DOMAIN          119..197
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000259|PROSITE:PS50804"
FT   DOMAIN          174..480
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
FT   DOMAIN          248..321
FT                   /note="KRAB"
FT                   /evidence="ECO:0000259|PROSITE:PS50805"
FT   DOMAIN          464..491
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          492..519
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          520..547
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          548..575
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          576..603
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          94..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          348..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..442
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..610
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   610 AA;  69217 MW;  06066E92299F4816 CRC64;
     MLENYRNLVS VEHQLSKPDV VSQLEEAEDF WPVERGIPQD TIPEYPELQP DPKLDPLPAE
     SPLMNIEVVE VLTLNQEVAG PRNAQIQALY AEDGSLSPDA PSEQVQQQGK HPGDPEAARQ
     RFRKFRYKDM TGPREALDQL RELCHQWLQP EARSKEQILE LLVLEQFLGA LPVKLRTWVE
     SQHPENCQEV VALVEGVTWI SEEEVLPAGQ PAEGTTCCLE VTAQQEEKEK EKEDAAICPV
     TVLPEEPVTF QDVAVDFSRE EWGLLGPTQR TEYRDVMLET FGHLVSVGWE TTLENKELAP
     NSDIPEEEPA PSLKVQESSR DCALSSTLED TLQGGVQEVQ ETVLKQVESA QEKEKHFDNH
     ESQANSGTLD TNQVSLQKMD SVESQANNGA LNTNQVLLQK IPHRKQLRKC DSQVKSMKQN
     SRVKIHQKSY ERQKAKEGNG CRKTFSRSAK QITFIRIHKG SQVCRCSECG KIFRNPRYFS
     VHKKIHTGER PYVCQACGKG FVQSSSLTQH QRVHSGERPF ECQECGRTFN DRSAISQHLR
     THTGAKPYKC QDCGKAFRQS SHLIRHQRTH TGERPYACNK CGKAFTQSSH LIGHQRTHNR
     TKRKKKQPTS
//
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