ID A0A2K6RR11_RHIRO Unreviewed; 622 AA.
AC A0A2K6RR11;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Zinc finger protein 274 {ECO:0000313|Ensembl:ENSRROP00000043479.1};
GN Name=ZNF274 {ECO:0000313|Ensembl:ENSRROP00000043479.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000043479.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000043479.1}
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}.
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 AlphaFoldDB; A0A2K6RR11; -.
DR Ensembl; ENSRROT00000067990.1; ENSRROP00000043479.1; ENSRROG00000044784.1.
DR GeneTree; ENSGT00940000162111; -.
DR OMA; VEDVTWM; -.
DR Proteomes; UP000233200; 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; 2.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 6.10.140.140; -; 2.
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:SF117; KRAB DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01352; KRAB; 2.
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; 3.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 2.
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:UP000233200};
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 14..101
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 129..207
FT /note="SCAN box"
FT /evidence="ECO:0000259|PROSITE:PS50804"
FT DOMAIN 184..492
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT DOMAIN 256..329
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 476..503
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 504..531
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 532..559
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 560..587
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 588..615
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 105..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..622
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 70547 MW; 18849A80F5EC5546 CRC64;
MASRLPTAWS CEPVIFEDVT LGFTPEEWGL LDLKQKSLYR EVMLENYRNL VSVEYPELQL
DPKLDPLPAE SPLMNIEVVE VLTLNQEVAG PRNAQIQALY AEDGSLSPDA PSEQVQQQGK
HPGDPEAARQ RFRKFRYKDM TGPREALDQL RELCHQWLQP EARSKEQILE LLVLEQFLGA
LPVKLRTWVE SQHPENCQEV VALVEGVTWI SEEEVLPAGQ PAEGTTCCLE VTAQQEEKQK
EDAAICPVTV LPEEPVTFQD VAVDFSREEW GLLGPTQRTE YRDVMLETFG HLVSVGWETT
LENKELAPNS DIPEEEPAPS LKVQESSRDC ALSSTLEDTL QGGVQEVQET VLKQVESTRE
KDLPQKKHFD NHESQANSGT LDTNQVSLQK IDSVESQANN GALNTNQVLL QKIPPRKQLR
KCDSQAKSMK HSSRVKIHQK SYERQKAKEG NGCRKTFSRS AKQITFIRIH KGSQVCRCSE
CGKIFRNPRY FSVHKKIHTG ERPYVCQACG KGFVQSSSLT QHQRVHSGER PFECQECGRT
FNDRSAISQH LRTHTGAKPY KCQDCGKAFR QSSHLIRHQR THTGERPYAC NKCGKAFTQS
SHLIGHQRTH NRTKRKKKQP TS
//
