ID A0A7K8EK80_LEURO Unreviewed; 745 AA.
AC A0A7K8EK80;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
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};
DE Flags: Fragment;
GN Name=Uhrf1 {ECO:0000313|EMBL:NXB51339.1};
GN ORFNames=LEUROT_R03795 {ECO:0000313|EMBL:NXB51339.1};
OS Leucopsar rothschildi (Bali myna) (Rothschild's mynah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sturnidae; Leucopsar.
OX NCBI_TaxID=127929 {ECO:0000313|EMBL:NXB51339.1, ECO:0000313|Proteomes:UP000522331};
RN [1] {ECO:0000313|EMBL:NXB51339.1, ECO:0000313|Proteomes:UP000522331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-02 {ECO:0000313|EMBL:NXB51339.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXB51339.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NXB51339.1}.
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DR EMBL; VZTC01007483; NXB51339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K8EK80; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000522331; Unassembled WGS sequence.
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:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044027; P:negative regulation of gene expression via chromosomal CpG island methylation; IEA:TreeGrafter.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd15616; PHD_UHRF1; 1.
DR CDD; cd16769; RING-HC_UHRF1; 1.
DR CDD; cd20455; Tudor_UHRF1_rpt1; 1.
DR CDD; cd20457; Tudor_UHRF1_rpt2; 1.
DR FunFam; 2.30.280.10:FF:000001; E3 ubiquitin-protein ligase UHRF1 isoform 1; 1.
DR FunFam; 2.30.30.140:FF:000068; E3 ubiquitin-protein ligase UHRF1 isoform 1; 1.
DR FunFam; 2.30.30.1150:FF:000001; E3 ubiquitin-protein ligase UHRF2 isoform X1; 1.
DR FunFam; 3.30.40.10:FF:000066; E3 ubiquitin-protein ligase UHRF2 isoform X1; 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; 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 SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SMART; SM00466; SRA; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 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; 2.
PE 4: Predicted;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU369101};
KW Ligase {ECO:0000313|EMBL:NXB51339.1};
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:UP000522331};
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 284..334
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 287..332
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 387..550
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT DOMAIN 676..715
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 40..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXB51339.1"
FT NON_TER 745
FT /evidence="ECO:0000313|EMBL:NXB51339.1"
SQ SEQUENCE 745 AA; 82604 MW; F173E5728597BF14 CRC64;
SDQMAPCFPP QMEDGHSLFD YSVGLNDIVQ LLVRQSPALL PAASKDKDSE LWDSDSGCGS
GPSESDKSSH NGEGALELEA QPSTAAEPHW TDPGFGLYKI NDLVDARDTD MGAWFEAQVV
NVTRKKPTSQ SAESCTDPEQ PTAVPEEDVI YHVKYDDYPE NGVVQMSSGN VRARARTILK
WHQLEVGQVV MVNYNPDEPK ERGFWYDAEI LQKRETKMTR ELNAKILLGE AGDSLNDCTI
ILVDEIYKIE EPGTASPISA GTPKRQSGPV CKACKDNPNK TCRVCACHIC GGKQDPDKQL
MCDECDMAFH IYCLNPPLSR IPDEDWYCPE CRNDASEVVL AGEKLKESKK KQKMASANSS
SRRDWGKGMA CVGRTKECTI VPSNHYGPIP GIPVGTMWKF RVQVSESGVH RPHVAGIHGR
SNDGAYSLVL AGGYEDDIDH GNSFTYTGSG GRDLSGNKRT AEQSCDQKLT NMNRALALNC
SAPINDKHGA EAKDWRAGKP VRVVRNVKGG KHSKYAPLEG NRYDGIYKVV KYWPETGKSG
FLVWRYLLRR DDEEPAPWTK EGKDRMKKLG LTMQYPEGYL EAVANKDKEK ENNGDDEFDT
PGKGKRKRKS AGGEENLISS PVGSPKKTKV EPYKLTSQQK SLIKSDEANE KLWNEVLEAL
KDGPKFLNKV EEAFLCICCQ EVVFRPVTTV CQHNVCKDCL DRSFKASVFS CPACRYELGR
SYSMEVNEAL QSVLAQLFPG YGSGR
//
