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Database: UniProt
Entry: A0A1W2TVY4_ROSNE
LinkDB: A0A1W2TVY4_ROSNE
Original site: A0A1W2TVY4_ROSNE 
ID   A0A1W2TVY4_ROSNE        Unreviewed;       868 AA.
AC   A0A1W2TVY4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   02-APR-2025, entry version 25.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=SAMD00023353_9500190 {ECO:0000313|EMBL:GAP92810.2};
OS   Rosellinia necatrix (White root-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX   NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP92810.2};
RN   [1] {ECO:0000313|EMBL:GAP92810.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W97 {ECO:0000313|EMBL:GAP92810.2};
RA   Kanematsu S.;
RT   "Draft genome sequence of Rosellinia necatrix.";
RL   Submitted (MAR-2016) 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};
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DR   EMBL; DF977540; GAP92810.2; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2TVY4; -.
DR   STRING; 77044.A0A1W2TVY4; -.
DR   OMA; PWFNYET; -.
DR   OrthoDB; 9977870at2759; -.
DR   Proteomes; UP000054516; 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; cd20335; BRcat_RBR; 1.
DR   CDD; cd22584; Rcat_RBR_unk; 1.
DR   Gene3D; 1.20.120.1750; -; 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; IPR044066; TRIAD_supradom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; 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:UP000054516};
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          381..581
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   REGION          1..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..87
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..106
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..131
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..185
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..291
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..362
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..698
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   868 AA;  97319 MW;  3CDF80F753D63C75 CRC64;
     MADSQYVAGK RRYGRGRQTA ASENHDWEPR RGESRHSLPY RIRQPEIQRP DRRNPKYSSR
     PSRTSEDLAH TGAMPAPMRM LPRPATPKSR GRRQYDEDED DDDDDSERER LRGRLRSRSR
     APSGPASRPA SKSAWGGKSR ATSGVASRAP SGVTSRAKSG AKSRPVSRDS QSTDSSPFPT
     PTRSSFVQLH PAPSAPSPGA STESSSEDSD DESSGSTQDY RMHTRTLKER MNMTPDSEPA
     PNPAARSRSR HKSRERIVPE IESPTEDSDD QARRPRLILK KRSLSRPRLA HQSRSPSRAP
     RHRRQTDRHG EERPSLSPKR GSKKYHHSDF AQPRETPFSR SRATSASRVK SAQSAGSSSK
     PSLGNFFPTS GPSQPYDQGS KSHTCVACKD RLPAEDLAKL KCGHRWCEDC LKRRFELSIE
     DVQNMPPRCC TSDIIPIKYV TDLFGDDFKK TWNEKFAKFS ARGRIYCPRP KCREPIRPTD
     YRHHSNGRTS ATCRKCEAKI CGLCYNKWHE SKRCPGDADT AQFLKVAKEA GWKRCFNCQA
     MVELKEGCNH MTCRCGAQFC MICGLKWKGC ECPWFSYDLE EEDEFGHVQI PIPMVSRERL
     GGAGGVPRGL RPDLGYAPEP RHHRGHRDDD RTRRLQHVEI DVDDDEEDDD HDDYIDGMGG
     VVGAGDTGGH FMGDSYRRRS HSTAVPQAPS APLAAPSVAH ERTKSGTNYV SGVNKARGVR
     GSSMERRLAD RFEQRQSFNP HHRSFGQPGP PLTAPPLTAP PLGMAPLPHQ PPMVPSPISR
     RHTIDNDMYD IPFDPRYASH AIPRRSTSHA YVDDFAVHAP LGRRRYRQME PPRPSELAGL
     TGPGGGMNRV FEWANHVETF PPDNQTVA
//
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