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Database: UniProt
Entry: A0A1B6PMS5_SORBI
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Original site: A0A1B6PMS5_SORBI 
ID   A0A1B6PMS5_SORBI        Unreviewed;       574 AA.
AC   A0A1B6PMS5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 2.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SORBI_3006G199500 {ECO:0000313|EMBL:KXG26966.2};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG26966.2, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:KXG26966.2, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
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DR   EMBL; CM000765; KXG26966.2; -; Genomic_DNA.
DR   RefSeq; XP_002448438.1; XM_002448393.1.
DR   AlphaFoldDB; A0A1B6PMS5; -.
DR   EnsemblPlants; KXG26966; KXG26966; SORBI_3006G199500.
DR   GeneID; 8071093; -.
DR   Gramene; KXG26966; KXG26966; SORBI_3006G199500.
DR   KEGG; sbi:8071093; -.
DR   eggNOG; KOG1814; Eukaryota.
DR   InParanoid; A0A1B6PMS5; -.
DR   OMA; CRQFGGE; -.
DR   OrthoDB; 4338126at2759; -.
DR   Proteomes; UP000000768; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
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:InterPro.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd20341; BRcat_RBR_RNF14; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR11685:SF297; RBR-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF01485; IBR; 2.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 2.
DR   SMART; SM00591; RWD; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50908; RWD; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000768};
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          90..233
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          284..500
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          288..336
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   574 AA;  64759 MW;  3CA94A41D8B78304 CRC64;
     MAALASGSTS GRFSDKASSS DGAGSSAVAA EGGYEAEEGV LDLDSPWVAA TEAESRLEAA
     GTAAGVGLSL LAGEELEEYE IRDNQQRQED ELTALEAIYG DDLIVFENKG GLRSFQIYIH
     YHLPDGIEVC AKLSAPNASP RDVGWCDYKH DDGPDEFSYT CNFEYLPPLI LTCLLPRSYP
     SKDPPSFTVT AKWMDGPYVS QLCQMLDTIW AGLPGQEVVY QWVEWLHNSS MSYLWIDGNM
     TLGPDIVNHN ADHRAISRTN SLESVIPLML SYSSKKRYQA FLEAIHMCMI CLNQTKGSNF
     IRLPCQHLFC VKCMETLCRL HVKEGSVFQL ICPDSKCKDS IPPYVLKRLL TEAEYERWDR
     LLLQKTLDSM SNVVYCPNCV IGCMEDEDNN AQCPKCSFVF CSFCKGPCHP GKKCLTPEEQ
     IQLRKVSGRM TEKEMAQELF NIRQLYKDVR LCPRCRMAIA KTEGCNKMVC GNCGQFFCFA
     CGKAISGYQH FRDQDCKLFA ARDIAAWERQ MAEIQPERLM RNAARPIGST VRCPKCRAQN
     FKDDEKYIFC WACMTDYCMF CRRKIQNRKG HSCI
//
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