ID A0A3Q0D986_MESAU Unreviewed; 777 AA.
AC A0A3Q0D986;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=E3 ubiquitin-protein ligase UHRF {ECO:0000256|RuleBase:RU369101};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369101};
DE AltName: Full=RING-type E3 ubiquitin transferase UHRF {ECO:0000256|RuleBase:RU369101};
DE AltName: Full=Ubiquitin-like PHD and RING finger domain-containing protein {ECO:0000256|RuleBase:RU369101};
DE AltName: Full=Ubiquitin-like-containing PHD and RING finger domains protein {ECO:0000256|RuleBase:RU369101};
GN Name=Uhrf1 {ECO:0000313|RefSeq:XP_021089361.1,
GN ECO:0000313|RefSeq:XP_021089362.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021089361.1};
RN [1] {ECO:0000313|RefSeq:XP_021089361.1, ECO:0000313|RefSeq:XP_021089362.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Multi domain E3 ubiquitin ligase that also plays a role in
CC DNA methylation and histone modifications.
CC {ECO:0000256|RuleBase:RU369101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU369101};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369101}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00358,
CC ECO:0000256|RuleBase:RU369101}.
CC -!- DOMAIN: The YDG domain mediates the interaction with histone H3.
CC {ECO:0000256|RuleBase:RU369101}.
CC -!- DOMAIN: The tudor-like regions specifically recognize and bind histone
CC H3 unmethylated at 'Arg-2' (H3R2me0), while the PHD-type zinc finger
CC specifically recognizes and binds histone H3 trimethylated at 'Lys-9'
CC (H3K9me3). {ECO:0000256|RuleBase:RU369101}.
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DR RefSeq; XP_021089361.1; XM_021233702.1.
DR RefSeq; XP_021089362.1; XM_021233703.1.
DR KEGG; maua:101830093; -.
DR OrthoDB; 5481936at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd15525; PHD_UHRF1_2; 1.
DR CDD; cd20388; Tudor_UHRF_rpt2; 1.
DR CDD; cd17122; Ubl_UHRF1; 1.
DR Gene3D; 2.30.30.1150; -; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.280.10; SRA-YDG; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR InterPro; IPR021991; TTD_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR047406; Ubl_UHRF1.
DR InterPro; IPR045134; UHRF1/2-like.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14140; E3 UBIQUITIN-PROTEIN LIGASE UHRF-RELATED; 1.
DR PANTHER; PTHR14140:SF2; E3 UBIQUITIN-PROTEIN LIGASE UHRF1; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF12148; TTD; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00466; SRA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS51015; YDG; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU369101};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369101};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00358}; Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369101};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU369101};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369101};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..78
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT DOMAIN 300..367
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 420..582
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT DOMAIN 708..747
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 80..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 87704 MW; 5AAEDA750F85B75B CRC64;
MWIQVRTMDG KETHTVDSLS RLTKVQELRK KIAELFHVEP QLQRLFYRGK QMEDGHTLFD
YDVRLNDTIQ LLVRQSLALP PSTKERDSEL SDSDSGYGVC QSESDKSSTH GEGDDKAVWE
DTELGLYKVN EYVDVRDNTL GAWFEAQVVQ VQKRAPSQEE PCSSSASMTL EDDIMYHIKY
DDYPESGVEV VKAKDVRARA RTVIPWEDLE VGQVVMVNYN VDYPRKRGFW YDVEICRKRR
TRTARELYGN VMLLNDSQLD NCRIMFVDEV FKIELPNERN PLIGGPSQPP LPLRKTGKSG
PSCQYCKDDE NKPCRKCACH VCGGREAPEK QVLCDECDMA FHLYCLQPQL TCVPPEPEWY
CPSCRTDSSE VVQAGEKLKQ SKKKAKMASA TSSSRRDWGK GMACVGRTKE CTIVPANHFG
PIPGVPVGTM WRFRVQVSES GVHRPHVAGI HGRSNDGAYS LVLAGGYEDD VDNGNFFTYT
GSGGRDLSGN KRTAGQSSDQ KLTNTNRALA LNCNSKISEN GAEAKDWRQG KPVRVVRNMK
GGKHSKYAPA EGNRYDGIYK VVKYWPEKGK SGFLVWRYLL RRDDTEPGPW TREGKDRMRQ
LGLTMQYPEG YLEALASKEK SRKRPARALE QEPTTSKTTT SKRKTTGVAT NTHVSKKSKL
EPYTLPVQQA TLIKEDKSNA KLWDDVLSSL QGGPYQVFLS KVEEAFQCIC CQELVFRPVT
TVCQHNVCKD CLDRSFRAEV FSCPACRCDL DHSSPTRVNQ PLQTILNQLF PGYGSGR
//
