ID A0A8H3XCT9_GIGMA Unreviewed; 223 AA.
AC A0A8H3XCT9;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 02-APR-2025, entry version 14.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=F8M41_004046 {ECO:0000313|EMBL:KAF0440413.1};
OS Gigaspora margarita.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=4874 {ECO:0000313|EMBL:KAF0440413.1, ECO:0000313|Proteomes:UP000439903};
RN [1] {ECO:0000313|EMBL:KAF0440413.1, ECO:0000313|Proteomes:UP000439903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEG34 {ECO:0000313|EMBL:KAF0440413.1,
RC ECO:0000313|Proteomes:UP000439903};
RX PubMed=31621176;
RA Venice F., Ghignone S., Salvioli di Fossalunga A., Amselem J., Novero M.,
RA Xianan X., Sedzielewska Toro K., Morin E., Lipzen A., Grigoriev I.V.,
RA Henrissat B., Martin F.M., Bonfante P.;
RT "At the nexus of three kingdoms: the genome of the mycorrhizal fungus
RT Gigaspora margarita provides insights into plant, endobacterial and fungal
RT interactions.";
RL Environ. Microbiol. 0:0-0(2019).
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}.
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:KAF0440413.1}.
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DR EMBL; WTPW01001365; KAF0440413.1; -; Genomic_DNA.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000439903; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
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; IPR054694; Parkin-like_IBR.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22605; IBR_2; 1.
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:UP000439903};
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 5..223
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 9..58
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 223 AA; 25726 MW; C0C9BBD593A6B72D CRC64;
MGNNICKECN ICVEKKSPTL FLAVTTKCKH DKNICSNCVE RHIDANLNGK GDVFIQCPFE
GCKKVIEHND VKRIANQELF ERFDTISLRH ALRTMPDFRW CKNSRCGSGQ IHYERDDAPI
MTCRSCGEKS CYTHDVPWHE NMSCAQYEEK SKESEAATNH YLMKHTKPCP KCGTHIEKNG
GCNHMTCKIR SCSYEFCWLC LADYNEIRKH GNKKHKKTCS LYA
//
