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Database: UniProt
Entry: A0A835BSJ9_9POAL
LinkDB: A0A835BSJ9_9POAL
Original site: A0A835BSJ9_9POAL 
ID   A0A835BSJ9_9POAL        Unreviewed;       635 AA.
AC   A0A835BSJ9;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   02-APR-2025, entry version 17.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=HU200_033051 {ECO:0000313|EMBL:KAF8702283.1};
OS   Digitaria exilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Panicodae; Paniceae; Anthephorinae; Digitaria.
OX   NCBI_TaxID=1010633 {ECO:0000313|EMBL:KAF8702283.1, ECO:0000313|Proteomes:UP000636709};
RN   [1] {ECO:0000313|EMBL:KAF8702283.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF8702283.1};
RA   Bennetzen J.L., Chen S., Ma X., Wang X., Yssel A.E.J., Chaluvadi S.R.,
RA   Johnson M., Gangashetty P., Hamidou F., Sanogo M.D., Zwaenepoel A.,
RA   Wallace J., Van De Peer Y., Van Deynze A.;
RT   "Genome sequence and genetic diversity analysis of an under-domesticated
RT   orphan crop, white fonio (Digitaria exilis).";
RL   Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SIMILARITY: Belongs to the RBR family. RNF14 subfamily.
CC       {ECO:0000256|ARBA:ARBA00044508}.
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:KAF8702283.1}.
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DR   EMBL; JACEFO010001787; KAF8702283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A835BSJ9; -.
DR   OrthoDB; 1431934at2759; -.
DR   Proteomes; UP000636709; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20341; BRcat_RBR_RNF14; 1.
DR   CDD; cd20354; Rcat_RBR_RNF14; 1.
DR   CDD; cd23820; RWD_RNF14; 1.
DR   FunFam; 1.20.120.1750:FF:000029; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.10.110.10:FF:000083; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000358; RBR-type E3 ubiquitin transferase; 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; IPR047548; Rcat_RBR_RNF14.
DR   InterPro; IPR006575; RWD_dom.
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   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   Pfam; PF05773; RWD; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 3.
DR   SMART; SM00591; RWD; 1.
DR   SUPFAM; SSF57850; RING/U-box; 4.
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:UP000636709};
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          138..275
FT                   /note="RWD"
FT                   /evidence="ECO:0000259|PROSITE:PS50908"
FT   DOMAIN          326..546
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          330..378
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..87
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..101
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   635 AA;  71010 MW;  98A4EE7DB3F1F7B7 CRC64;
     MPRKSSRPRG AAAQGPVGPT AVPRPPFKGA APNPSPAAEP PQAAAPAVDE ALERLHLDTV
     SDGDPPAPAP PEPEPEPEAP APSPPAPVEA SSSGRSAAGG SLEEEEALRK LHELAEAGGE
     EVALTDDEVG ANDQRQEDEI CALESIFGDA VVIFNRKGGQ RCFQVHVHIE IPEAIDVSTR
     FNYGDGTLKY GEASDADDLV YKFRVEHLPP ILLTCLLPAS YPSHRPPLFT ISSYWLDKGM
     ISSLCHMLDM LWEEQQGMEV TYQWVQWLQS SSLSHLGFDN EIVLSKNDVA CEADKRACLD
     NASPDVIIPR MMRYNENRHH EAFVNAIHDC MICFSECPGV DFVKLPCHHF FCWKCMQTYC
     KMNVKEGNVV KLLCPDTKCE GAVPPNILKR LLGEDEFERW EGLLLQRTLD AMADVVYCPR
     CQTACLEDVG NEAVCSSCLF SFCTLCRNRR HIGEQCMSPA ERLLILEKRQ QSGHVQADQM
     RILEELRSLK EIMKDSKQCP KCNMAISKTE GCNKMECWNC KEYFCYQCNR AITGYDHFRG
     SCVLFPQEEL DRWEMQMNQR VQRQVVAQVH AEMHLQHGPA HPCPTCRQPS PKIGNNNHLF
     CWACQKHFCA LCHKSVPKPA QHYGPKGCKQ HTADT
//
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