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Database: UniProt
Entry: S3BNH4_OPHP1
LinkDB: S3BNH4_OPHP1
Original site: S3BNH4_OPHP1 
ID   S3BNH4_OPHP1            Unreviewed;       540 AA.
AC   S3BNH4;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=F503_08502 {ECO:0000313|EMBL:EPE02739.1};
OS   Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX   NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE02739.1, ECO:0000313|Proteomes:UP000016923};
RN   [1] {ECO:0000313|EMBL:EPE02739.1, ECO:0000313|Proteomes:UP000016923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE02739.1,
RC   ECO:0000313|Proteomes:UP000016923};
RX   PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA   Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA   Robertson G., Birol I., Bohlmann J., Breuil C.;
RT   "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT   a comparison with the bark beetle-associated pine pathogen Grosmannia
RT   clavigera.";
RL   BMC Genomics 14:373-373(2013).
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; KE148174; EPE02739.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3BNH4; -.
DR   STRING; 1262450.S3BNH4; -.
DR   VEuPathDB; FungiDB:F503_08502; -.
DR   eggNOG; KOG1815; Eukaryota.
DR   HOGENOM; CLU_009823_4_1_1; -.
DR   OMA; HRFCMIC; -.
DR   OrthoDB; 3084186at2759; -.
DR   Proteomes; UP000016923; 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   CDD; cd16625; RING-HC_RBR_HEL2-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; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
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   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 3.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016923};
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          141..355
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          145..191
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..46
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  62092 MW;  8A4F666CF1D91325 CRC64;
     MDSEDDFMST LSSEDDVMQD DSDNGMMSDN EDFDDFDDDE PDDLDIGLDK DVVSDDKTKK
     RYDVDFKVIC PQDIQKQQEE LIEDVNMILE MRPEDAAILL RHFRWNRERL IEEYMDRPNK
     TLEAAGLGPN VVTLPKLEIL PGFVCDICCE DDDELQTFAL KCGHRYCVDC YRQYLTQKIR
     EEGEAARIQC PTADCGRIID AISLSVLVTP ELSGRYHELL NRTYVEDRES LKWCPAPNCE
     NAVDCRVKKK DLDRVVPTVE CLCGYRFCFG CTLKDHLPAP CRLVKLWLKK CADDSETANW
     ISANTKECPK CNSTIEKNGG CNHMTCRKCK YEFCWMCMGL WSEHGTSWYN CNRFEEKSGT
     DARDAQAKSR VSLERYLHYY NRYANHEQSA RLDKDSYTKT EVKMMQLQTA SGMSWIEVQY
     LQAASQALQT CRQTLKWTYA FAFYLARNNL TEMFEDNQKD LEMAVEALSE MFEKPLGELA
     DPKTKLDIID KTSYCNKRRV TLLEYTADNL AQGSWTFNSD QLPAATAAAA PAKPAPKARN
//
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