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Database: UniProt
Entry: A0A0L6V6V4_9BASI
LinkDB: A0A0L6V6V4_9BASI
Original site: A0A0L6V6V4_9BASI 
ID   A0A0L6V6V4_9BASI        Unreviewed;       554 AA.
AC   A0A0L6V6V4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=VP01_2390g4 {ECO:0000313|EMBL:KNZ56493.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ56493.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ56493.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ56493.1,
RC   ECO:0000313|Proteomes:UP000037035};
RA   Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA   Sacco F.;
RT   "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT   Schw, the Causal Agent of Maize Common Rust.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:KNZ56493.1}.
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DR   EMBL; LAVV01007270; KNZ56493.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6V6V4; -.
DR   STRING; 27349.A0A0L6V6V4; -.
DR   VEuPathDB; FungiDB:VP01_2390g4; -.
DR   OrthoDB; 3084186at2759; -.
DR   Proteomes; UP000037035; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR   CDD; cd20356; Rcat_RBR_HHARI-like; 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; IPR048962; ARIH1-like_UBL.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685:SF212; E3 UBIQUITIN-PROTEIN LIGASE ARIH1; 1.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF21235; ARI1_UBAl; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51873; TRIAD; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037035};
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}.
FT   DOMAIN          141..387
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..33
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   554 AA;  63877 MW;  73B9C037795342D6 CRC64;
     MSSDTSDIEL EYDSTEGYED DEDAIDLDSN DPSSDDGDGS SFNMVPMATQ PTKPLYQVEY
     SVLQESELTQ RQIREIEHVA GIIGIASKDA ALVLRYFGWN KDLLMEKYMD SPEKVFRDVG
     IRTDLGLNKP SSSRRRTRST PKFVCQICFN DEPNQETVYL PSCPPLPKDS DPRSRSASSY
     QSVKHEFCRD CYTYYVEAKI KEGESRTIEC MESECKQIVD ENTIVNLLTV RDANLPESEK
     LMGRFQTLLN RTFVDDNPAL KFCPAPNCIY TIECHVSKKS LDTVVPSVTC HCGQRYTSFC
     FGCSLADHQP CICPIVKLWL QKCEDDSETA NWISANTKEC TKCHSTIEKN GGCNHMTCKK
     CKHEFCWVCT GVWADHGMAW YSCNRYEERD EHGKDQQSKS RASLERYLHY YNRFANHEQS
     LRLDKELHAK TEKKMEEIQH ASNLSWIEVQ FLNKAVETLS VCRTTLKWTY AMAFYLEKNN
     FTALFEDNQR DLEQAVEDLS GLLESPIEAD TIADLRQKVT DKTVYVHKRN EIMLEETARD
     YQDGRVFWNT HFKL
//
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