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
//