ID A0A0Q3Q3P7_AMAAE Unreviewed; 1910 AA.
AC A0A0Q3Q3P7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 ORFNames=AAES_66535 {ECO:0000313|EMBL:KQK82828.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK82828.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK82828.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK82828.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00000040};
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 -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369101}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PROSITE-ProRule:PRU00358, 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 -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
CC -!- SIMILARITY: Belongs to the Polycomblike family.
CC {ECO:0000256|ARBA:ARBA00008084}.
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:KQK82828.1}.
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DR EMBL; LMAW01001703; KQK82828.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3Q3P7; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd15525; PHD_UHRF1_2; 1.
DR CDD; cd20464; Tudor_JMJD2B_rpt1; 1.
DR CDD; cd20455; Tudor_UHRF1_rpt1; 1.
DR CDD; cd20457; Tudor_UHRF1_rpt2; 1.
DR Gene3D; 2.30.30.1150; -; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 3.10.330.70; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 2.30.280.10; SRA-YDG; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR InterPro; IPR021991; TTD_dom.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047483; Tudor_KDM4B_rpt1.
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 PANTHER; PTHR14140; E3 UBIQUITIN-PROTEIN LIGASE UHRF-RELATED; 1.
DR PANTHER; PTHR14140:SF2; E3 UBIQUITIN-PROTEIN LIGASE UHRF1; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF12148; TTD; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 3.
DR SMART; SM00466; SRA; 1.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS51015; YDG; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
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}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
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 283..339
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 291..337
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 392..555
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT DOMAIN 820..862
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 953..1119
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 1595..1718
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 46..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1855..1886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1385
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1410
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1863..1877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1910 AA; 214830 MW; AA6D480415B253CF CRC64;
MFSSDAVTVI RNGMYMEDGH SLFDYSVGLN DIVQLLVRQS PXVLPTVSKE KDPELSDTDS
GCGSGQSESD KSSHNGEGAL ELEGQPGTAA QPDWTDPGFG LYKINDLVDA RDMNMGAWFE
AQVVNVSRKK PANASAESCS DPEQPRAIPE EDVIYHVKYE DYPENGVVQL GSNDVRARAR
TILKWHQLEV GQVVMVNYNP DEPKERGFWY DAEILQKREM KMIKEINAKI LLGDAGDSLN
DCRIILVDEI YKIEEPGSAC PLTAPPAKRR IGPVCKACKD NPNKTCRICA CHICGGKQDP
EKQLMCDECD MAFHIYCLNP PLSSIPEDED WYCPECRNDA SEVVLAGERL KDSKKKQKMA
SANSSSRRDW GKGMACVGRT KECTIVPSNH YGPIPGIPVG TMWKFRVQVS ESGVHRPHVA
GIHGRSNDGA YSLVLAGGYE DDIDHGNSFT YTGSGGRDLS GNKRTAEQSC DQKLTNMNRA
LALNCSAPIN DKNGAEAKDW RAGKPVRVVR NVKGGKHSKY APVEGNRYDG IYKVVKYWPE
TGKSGFLVWR YLLRRDDEEP APWTKEGKDR MKKLGLTMQX PEGYLEAVAN KDKEKENNGD
DEFDTPGKGK RKRKSXGGEE KLLSSPTGTP KKTKVEPYKL TAQQKSLIKN DEANEKLWNG
VLEALKDGPD CLDRSFKADV YSCPACRYDL GKSYSMHVNE TLQTILTQLF PGYGNGRINS
EERRFVQIVT IQPAARQSPS FLXSNADPET EQMVFCVARL EIPLGQGHPE GEXVGSGITF
RAVQGGQVEE YLKSSGDGPS RRTRKMGSEV PSPQNPGCKI MTFRPTLEEF RDFGKYVAYM
ESQGAHRAGL AKVIPPKEWK PRKTYDDIDD MIIPAPIQQV VTGQSGLFTQ YNIQKKPMTV
GEYRRLANSE KYVXVRYCTP RHQDFEDLER KYWKNLTFVS PIYGADISGS LYDADVEEWN
IGNLNTLLDM VEHECGIIIE GVNTPYLYFG MWKTTFAWHT EDMDLYSINY LHFGEPKSWY
AIPPEHGKRL ERLAKGFFPG SSQGCDAFLR HKMTLISPSI LKKYGIPFDR ITQEAGEFMI
TFPYGYHAGF NHGFNCAEST NFATLRWIDY GKMATQDKEL DDVPGASLRL SLQCTCRKDM
VKISMDVFVR VLQPERYDLW KQGKDITVLD HMKPTALTSP ELDAWNETKA ELKTKLLRRI
GDEEEDNKHR SQRKRSQPRR HKTEDQKSLG DVMAMETGLE DVKVKEELKR GADLEEEERS
KVIEGEVRLV HRPWTLWITL LKSRRLLTDD AISIHYAVFL ESGSQRKRSQ PRRHKTEDQK
SLGDVMAMET GLEDVKVKEE LKRGADLEEE ERSKVIEGEG DCKXKARPPK VKGERKRKHL
FHQHQHHLQA PPAPLQQQQP PLPPPPAAQQ PLAEGEASTA RPPVPPAVPI STAAGKSLSP
TPLNIIQPLE APVEEDDFKP RPIIPMLYVV PRTKKVVFDK EHMSCQQAXE QFATQKSPSW
QEQAVPMEIS GKEEENAEGE NREVSTEVSD LQSLQMDKEA VPVSVAETSS FVHLSKCGQK
TKPLIPEMCF TSSGENTEPL PSNSYIGEDG TSPLISCAKC CLQVHASECF LLHQSVLGIE
KQVSLWVHII CAIAVPEARF LNVIERHPVD ISAIPEQRWK LKCVYCRKRM KKVSGACIQC
SYEHCSTSFH VTCAHAAGVP MEPDDWPYVV SITCFKHKAA NQNIPFRREV TLGQTVITKN
RNGLYYRCKV IGMTTQTFYE VNFEDGSYSD NVYPESIISR DCVQLGPPPE GELVQLQWTD
GIVYKAKFIA AQISQIYQVE FEDGSQLMVK RGDIYTLEEE LPKRVKSRLS LSTGAPQEDV
FSGDELRAAK RPRLGSSRNP EEYGQNPDYL AFMESLLQTQ YQPGTQSNMF
//
