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Database: UniProt
Entry: A0A178ELX1_9PLEO
LinkDB: A0A178ELX1_9PLEO
Original site: A0A178ELX1_9PLEO 
ID   A0A178ELX1_9PLEO        Unreviewed;       733 AA.
AC   A0A178ELX1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=IQ07DRAFT_18408 {ECO:0000313|EMBL:OAL56794.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL56794.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL56794.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL56794.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; KV441636; OAL56794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178ELX1; -.
DR   STRING; 765867.A0A178ELX1; -.
DR   InParanoid; A0A178ELX1; -.
DR   OrthoDB; 1376344at2759; -.
DR   Proteomes; UP000077535; 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; cd20335; BRcat_RBR; 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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685:SF441; E3 UBIQUITIN-PROTEIN LIGASE PARKIN; 1.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077535};
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          489..729
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          493..541
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          65..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..439
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   733 AA;  83308 MW;  ED4C1D7DE14C06E8 CRC64;
     MSEFFPAQLP DRPQKASKFG LAKLLSSKFE RKKKVGDNYA TDAYVGNQSA VFTDLSTYPD
     EITQQKTHLD RPIYPKKSPL TRATTGGLLP KAKHAVSSLR HSKSARWDNS FPDQVLTSPY
     PYEEQDKPFR SMQSSRKKPQ LPDKKNLVKD WLNKESRTSG SYPTPRESPP PYRPEDNINY
     STQVPESSIT NHSLAQYPKT KPLFTVVPKR RPLNPYRHSS ISTEPTDLQH VPEVDESQNG
     TVVNSTPQER PYYIPTPLQP QYGHHDEDAR MPQYDYQGGS SFEVEPVYVQ PKLYPSEDTA
     RIEPVYEQPE VHPSNGTARI EPIYDQLEVY PLDVTTDITQ NEAIIQPKPH RASLASVQTP
     TTPAVQQTED WELAERLQQE EIEAYELGQE LLREELRSIT KQDRNKKSRS RKKTSLLGNL
     EQSRAAGGKR HRQSKSRPDT HDASTTYSPC QVQSPEFETL PQEPGAQKDK FTTPTWEELI
     SMGSPGPSPT RDCAVCGDSQ PISSLPSLAN CTHIPETCAD CYTEWITSQL TESSWREVKC
     PGSKCKIKLT YHEIQAYALP ENFQQYDTYI ARTAFNDDPN FRWCRSCDYG QIHLSGVEGN
     IFTCANCGHK VCVIHENTWH EGETCEEFDY RSSGRKERDQ KAQEKASLKA ISKLSKKCPG
     PGCVYNIEKN DGCDRKSNGL QIELLKLTIT TDMTCSKCRY EFCWVCLCDY DSIRTQGNSA
     HANSCKYHSR RLN
//
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