ID A0A8H5MR73_9HYPO Unreviewed; 707 AA.
AC A0A8H5MR73;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 02-APR-2025, entry version 11.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=FNAPI_11509 {ECO:0000313|EMBL:KAF5537130.1};
OS Fusarium napiforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=42672 {ECO:0000313|EMBL:KAF5537130.1, ECO:0000313|Proteomes:UP000574317};
RN [1] {ECO:0000313|EMBL:KAF5537130.1, ECO:0000313|Proteomes:UP000574317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 25196 {ECO:0000313|EMBL:KAF5537130.1,
RC ECO:0000313|Proteomes:UP000574317};
RA Kim H.-S., Busman M., Brown D.W., Divon H., Uhlig S., Proctor R.H.;
RT "Identification and distribution of gene clusters putatively required for
RT synthesis of sphingolipid metabolism inhibitors in phylogenetically diverse
RT species of the filamentous fungus Fusarium.";
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:KAF5537130.1}.
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DR EMBL; JAAOAO010000546; KAF5537130.1; -; Genomic_DNA.
DR Proteomes; UP000574317; 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 CDD; cd22584; Rcat_RBR_unk; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51873; TRIAD; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000574317};
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}.
FT DOMAIN 215..406
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 91..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 445..480
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 91..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 82407 MW; 7DEF705DB64A1FAB CRC64;
MPGAFGPEDY IDFYEGPFEV FNGSGTSREK QEQRASWAVK KLPDLDIVDL DWHKYSPPKA
LRKAPNITSQ VLLDVLQSSV ENVNARIIEE DRQKKENEEQ RKQEENEKGK SKEPYLPIII
PTEPPVEEKT NHAVPPPNIK KEILMTTSGP SVVAQADARA NKRRLFALRR FFQRSDERGE
SSATGAALGA LQERVAEAEH VNDSLGRLTK LNSVEEVECV SCLDDFHPKD VIKVPCHNYC
RDCFVRLVTA ACQNEQQWPP KCCLNEIPVK TVMRFIPSDL KKTFEDRSKE WELPVSDRVY
CSNANCNLWI KPKRIYPGKR QGICDRSHVT CTLCRGPAHA EEDCPQDVDM SLTNQLAEDE
GWKRCFNCNA LVEHREACQH MTCRCGTQFC YVCSRRWRTC TCTMEDLRAL KERVVSRRAE
RRAQELEEAE ELRHILLQIE EFEHEEALKA ELLRLEQERL EEERRQRELE ERVRQESIRR
RDIEVKYQEL RTVLGELHDL QQVLLDVDQE EEAENMIIDI RAAKQELEMK HETELSELKA
LALAKMTEKE NSLNNDFRVR AAKENELEEA YHERLKAYWE GKDNGEQEVE NSMLALRKRM
DQKHHAWQKW KADQLKVVEA KLEDNRTYRE ELMYSAKHRL DDSCKEKGAE MMRRMAAEKK
WLEAVILERE KLLNEREAQE VEVDADSMFA VESEDSGDGH YVIATTF
//