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Database: UniProt
Entry: B8A106_MAIZE
LinkDB: B8A106_MAIZE
Original site: B8A106_MAIZE 
ID   B8A106_MAIZE            Unreviewed;       534 AA.
AC   B8A106;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   18-JUN-2025, entry version 96.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   Name=LOC100279995 {ECO:0000313|EnsemblPlants:Zm00001eb218920_P001};
GN   ORFNames=ZEAMMB73_Zm00001d013716 {ECO:0000313|EMBL:AQK64214.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ACL53855.1};
RN   [1] {ECO:0000313|EMBL:ACL53855.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACL53855.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [2] {ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|Proteomes:UP000007305};
RX   PubMed=19965430; DOI=10.1126/science.1178534;
RA   Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA   Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA   Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA   Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA   Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA   Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA   Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA   Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA   Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA   Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA   Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA   Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA   Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA   Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA   Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA   Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA   Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA   Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA   Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA   Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA   SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA   Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA   Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA   Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA   Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA   Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT   "The B73 maize genome: complexity, diversity, and dynamics.";
RL   Science 326:1112-1115(2009).
RN   [3] {ECO:0000313|EMBL:AQK64214.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK64214.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EnsemblPlants:Zm00001eb218920_P001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb218920_P001};
RA   Seetharam A., Woodhouse M., Cannon E.;
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EnsemblPlants:Zm00001eb218920_P001}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb218920_P001};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) to UniProtKB.
CC   -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC       complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC       enzymes and then transfers it to substrates.
CC       {ECO:0000256|ARBA:ARBA00003976}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
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DR   EMBL; BT055248; ACL53855.1; -; mRNA.
DR   EMBL; BT055305; ACL53912.1; -; mRNA.
DR   EMBL; CM000781; AQK64214.1; -; Genomic_DNA.
DR   RefSeq; NP_001146415.1; NM_001152943.1.
DR   SMR; B8A106; -.
DR   FunCoup; B8A106; 1308.
DR   STRING; 4577.B8A106; -.
DR   PaxDb; 4577-GRMZM2G110423_P01; -.
DR   EnsemblPlants; Zm00001eb218920_T001; Zm00001eb218920_P001; Zm00001eb218920.
DR   GeneID; 100279995; -.
DR   Gramene; Zm00001eb218920_T001; Zm00001eb218920_P001; Zm00001eb218920.
DR   KEGG; zma:100279995; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   HOGENOM; CLU_009823_2_1_1; -.
DR   OMA; CKLLMED; -.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000007305; Chromosome 5.
DR   ExpressionAtlas; B8A106; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR   CDD; cd22586; Rcat_RBR_ARI1-like; 1.
DR   CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR   FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045840; Ariadne.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Ligase {ECO:0000313|EMBL:AQK64214.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:B8A106};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          121..334
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          125..168
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  60605 MW;  1BB77FBF3906DE7E CRC64;
     MTSDDEEACD YFYDDDDDAE EDAAAGLEED SSLPTPEGRA DYWAITQDTV FAAQKQDLST
     VMNLLNINQH QARALLIHHR WSMDGIYDSL DMGRERMLRN SGIVLQEVNS IAAAGSMTPW
     RTVTCKVCFE DFSMDAVSTM DCGHCFCNDC WTEYFHAAVE SGKKQIRCME VKCSAFCDED
     LVRFLLVQKY PDMAKNFNRF LLGSYLEDNA SVKWCPSTPN CGHAIRVGTD ERCCEVECPC
     GLSFCFNCMG HAHSPCPCTI WEKWNASRSE GENIKWILAN TKSCPKCFKA IEKNGGCNLV
     RCKCGQCMCW LCGGGTGQDH TWNSITGHSC NRYEEEICVE TVHTGRQQMQ RYKHYHDRFK
     IHGDSSYGVE KQKLGAAIEE RVRLLESDRE RPLAIRDGDW LTRAHRRLLV SRQVLSRSYV
     FAYYMFGGHE LRTRPAERAN LGVARNLFEH QQEQLERHVE HLSRSLAESA DLAGAPDAEI
     VKQKQTAITL TKTVERLCGE MYKCIQDELL TLLVEPMSIA AYRPDGPDRA KPAI
//
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