ID A0A8H4TC19_9HYPO Unreviewed; 347 AA.
AC A0A8H4TC19;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 02-APR-2025, entry version 12.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=FSARC_11945 {ECO:0000313|EMBL:KAF4955119.1};
OS Fusarium sarcochroum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium lateritium species complex.
OX NCBI_TaxID=1208366 {ECO:0000313|EMBL:KAF4955119.1, ECO:0000313|Proteomes:UP000622797};
RN [1] {ECO:0000313|EMBL:KAF4955119.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 20472 {ECO:0000313|EMBL:KAF4955119.1};
RX PubMed=33059601;
RA Kim H.S., Lohmar J.M., Busman M., Brown D.W., Naumann T.A., Divon H.H.,
RA Lysoe E., Uhlig S., Proctor R.H.;
RT "Correction to: Identification and distribution of gene clusters required
RT for synthesis of sphingolipid metabolism inhibitors in diverse species of
RT the filamentous fungus Fusarium.";
RL BMC Genomics 21:712-710(2020).
RN [2] {ECO:0000313|EMBL:KAF4955119.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 20472 {ECO:0000313|EMBL:KAF4955119.1};
RA Kim H.-S., Proctor R.H., Brown D.W.;
RL Submitted (MAY-2020) 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:KAF4955119.1}.
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DR EMBL; JABEXW010000791; KAF4955119.1; -; Genomic_DNA.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000622797; 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; 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 SMART; SM00647; IBR; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000622797};
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 49..330
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 53..107
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT COILED 230..261
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 347 AA; 39366 MW; 39DA5DFDA3E0ACBE CRC64;
MTTAYLRRLE QSGNEAADDF RFGQRYQKAS DSSDVIITHQ RTPRSTVVGD LECVVCADTK
DADAFPRFSV TATCTHPPNT CLDCVQLSIE SDLSSKLWTE IRCPECRELL EYADIQRYAN
KQTFTRYETL ALRAAMSEAE NFIWCTSGCG SGQIHESGSA QPIVTCLHCN HRSCFHHNVA
WHETLSCEEY DQLLADPDNF RSRLELENER WSEAQQAQLE ADRAIAQGLL AEDRAELKLR
EERARQEREQ AQKAAKLARQ IAARRKKEED RSKATVNRTA KPCAGCGWAI EKNRGCSHMT
LSPDAVYFMS GLDRPPYAAL THWWFDLETV DLTLYAEKIG TSGPIHY
//
