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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//