ID A0A1P8B4V7_ARATH Unreviewed; 425 AA.
AC A0A1P8B4V7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=E3 ubiquitin-protein ligase ORTHRUS {ECO:0000256|RuleBase:RU369101};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369101};
DE AltName: Full=Protein VARIANT IN METHYLATION {ECO:0000256|RuleBase:RU369101};
DE AltName: Full=RING-type E3 ubiquitin transferase ORTHRUS {ECO:0000256|RuleBase:RU369101};
GN Name=ORTHL {ECO:0000313|EMBL:ANM66610.1, ECO:0000313|TAIR:AT4G08590};
GN Synonyms=15935 {ECO:0000313|EMBL:ANM66610.1}, ORL1
GN {ECO:0000313|EMBL:ANM66610.1}, ORTH-LIKE 1
GN {ECO:0000313|EMBL:ANM66610.1}, ORTHRUS-like
GN {ECO:0000313|EMBL:ANM66610.1}, ORTHRUS-LIKE 1
GN {ECO:0000313|EMBL:ANM66610.1}, VARIANT IN METHYLATION 6
GN {ECO:0000313|EMBL:ANM66610.1}, VIM6 {ECO:0000313|EMBL:ANM66610.1};
GN OrderedLocusNames=At4g08590 {ECO:0000313|Araport:AT4G08590,
GN ECO:0000313|EMBL:ANM66610.1};
GN ORFNames=T3F12.10 {ECO:0000313|EMBL:ANM66610.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:ANM66610.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:ANM66610.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=10617198; DOI=10.1038/47134;
RG EU;
RG CSHL and WU Arabidopsis Sequencing Project;
RA Mayer K., Schuller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Dusterhoft A., Stiekema W., Entian K.D., Terryn N., Harris B., Ansorge W.,
RA Brandt P., Grivell L., Rieger M., Weichselgartner M., de Simone V.,
RA Obermaier B., Mache R., Muller M., Kreis M., Delseny M., Puigdomenech P.,
RA Watson M., Schmidtheini T., Reichert B., Portatelle D., Perez-Alonso M.,
RA Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H.,
RA Ridley P., Langham S.A., McCullagh B., Bilham L., Robben J.,
RA Van der Schueren J., Grymonprez B., Chuang Y.J., Vandenbussche F.,
RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E.,
RA Brandt A., Peters S., van Staveren M., Dirske W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Kotter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., Van Montagu M., Rogers J.,
RA Cronin A., Quail M., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M.,
RA Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M.,
RA Benes V., Rechmann S., Borkova D., Blocker H., Scharfe M., Grimm M.,
RA Lohnert T.H., Dose S., de Haan M., Maarse A., Schafer M., Muller-Auer S.,
RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O.,
RA Quigley F., Clabauld G., Mundlein A., Felber R., Schnabl S., Hiller R.,
RA Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C.,
RA Montfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sehkon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L., Nelson J.,
RA Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J.,
RA Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffmann J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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 RING fingers are required for ubiquitin ligase activity.
CC {ECO:0000256|RuleBase:RU369101}.
CC -!- DOMAIN: The YDG domain mediates the interaction with histone H3.
CC {ECO:0000256|RuleBase:RU369101}.
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DR EMBL; CP002687; ANM66610.1; -; Genomic_DNA.
DR RefSeq; NP_001328495.1; NM_001340600.1.
DR AlphaFoldDB; A0A1P8B4V7; -.
DR SMR; A0A1P8B4V7; -.
DR ProteomicsDB; 207866; -.
DR EnsemblPlants; AT4G08590.6; AT4G08590.6; AT4G08590.
DR GeneID; 826420; -.
DR Gramene; AT4G08590.6; AT4G08590.6; AT4G08590.
DR Araport; AT4G08590; -.
DR TAIR; AT4G08590; ORTHL.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; A0A1P8B4V7; baseline and differential.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd23138; RING-HC_ORTHRUS_rpt1; 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; IPR047498; RING-HC_ORTHRUS_rpt1.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR InterPro; IPR045134; UHRF1/2-like.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14140:SF46; E3 UBIQUITIN-PROTEIN LIGASE ORTHRUS 1-RELATED; 1.
DR PANTHER; PTHR14140; E3 UBIQUITIN-PROTEIN LIGASE UHRF-RELATED; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00466; SRA; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51015; YDG; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU369101};
KW Metal-binding {ECO:0000256|RuleBase:RU369101};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00358};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1P8B4V7};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW Transferase {ECO:0000256|RuleBase:RU369101};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU369101};
KW Zinc {ECO:0000256|RuleBase:RU369101};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175,
KW ECO:0000256|RuleBase:RU369101}.
FT DOMAIN 109..148
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 233..374
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT REGION 31..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 47483 MW; A04C9D77D6DBD49E CRC64;
MTRVNQLPCD CVSTAEESLT SGTCITPTHV TSLSSPLDRS GDVDPLPVSD ESGGSKADES
MTDADETKKR KRILSGDCEA DENNKSDGEI ASLNDGVDAF TAICEDLNCS LCNQLPDRPV
TILCGHNFCL KCFDKWIDQG NQICATCRST IPDKMAANPR VNSSLVSVIR YVKVAKTAGV
GTANFFPFTS NQDGPENAFR TKRAKIGEEN AARIYVTVPF DHFGPIPAEH DPVRNQGVLV
GESWENRVEC RQWGVHLPHV SCIAGQEDYG AQSVVISGGY KDDEDHGEWF LYTGRSRGRH
FANEDQEFED LNEALRVSCE MGYPVRVVRS YKDRYSAYAP KEGVRYDGVY RIEKCWRKAR
FPDSFKVCRY LFVRCDNEPA PWNSDESGDR PRPLPNIPEL ETASDLFERK ESPSWDFDVS
SNYNS
//
