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Database: UniProt
Entry: A0A1Z5TIH6_HORWE
LinkDB: A0A1Z5TIH6_HORWE
Original site: A0A1Z5TIH6_HORWE 
ID   A0A1Z5TIH6_HORWE        Unreviewed;       516 AA.
AC   A0A1Z5TIH6;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=BTJ68_03962 {ECO:0000313|EMBL:OTA35852.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA35852.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA35852.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA35852.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) 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:OTA35852.1}.
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DR   EMBL; MUNK01000039; OTA35852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5TIH6; -.
DR   STRING; 1157616.A0A1Z5TIH6; -.
DR   VEuPathDB; FungiDB:BTJ68_03962; -.
DR   InParanoid; A0A1Z5TIH6; -.
DR   OrthoDB; 3084186at2759; -.
DR   Proteomes; UP000194280; 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; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194280};
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          137..351
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          141..189
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..40
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  59563 MW;  63C69C671BD8BE16 CRC64;
     MDSDDDFNSV MSSEELGEDM DSSVDLGADS DVELEDVEDE SAFDAHPKDL KPAKKAYEVD
     FNVYSPEDIQ AQQDRQVAEV ATLLEQPTEQ TAILLRFMRW NKERLIEQYM DNQEEVLDKA
     GLGADMSSNP PRLEAIDGFM CDICCEDEPG LQSFAMNCGH RFCVDCYRQY LAQKIKEEGE
     AARIKCPGDG CNKIIDARSL DLLVTSDLTD RYHELLMRTY VDDKENLKWC PAPNCVFAVE
     CGVKRRDLNK IVPTVHCQCK HAFCFGCTLV DHQPCPCSLV RKWLKKCEDD SETANWISAN
     TKECPKCQST IEKNGGCNHM TCRKCRHEFC WMCMGLWSEH GTSWYNCNRF EEKSGTDARD
     AQALSRKSLE RYLHYYNRYA NHEQSAKLDK DIFHKTEKKM QLLQSSSGMS WIEVQFLEAA
     SHALQQCRQT LKWTYAFAYY LARNNQTEIF EDNQKDLEMA VENLSEMFEK NTDQLSGLKV
     DMMDKTSYCM RRRVILLDDT AQRLRDGGWE FNVDLD
//
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