ID A0A8H7QBC8_9FUNG Unreviewed; 479 AA.
AC A0A8H7QBC8;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 02-APR-2025, entry version 16.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=INT44_003873 {ECO:0000313|EMBL:KAG2188734.1};
OS Umbelopsis vinacea.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Umbelopsidomycetes; Umbelopsidales; Umbelopsidaceae; Umbelopsis.
OX NCBI_TaxID=44442 {ECO:0000313|EMBL:KAG2188734.1, ECO:0000313|Proteomes:UP000612746};
RN [1] {ECO:0000313|EMBL:KAG2188734.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WA0000051536 {ECO:0000313|EMBL:KAG2188734.1};
RA Muszewska A., Okrasinska A., Steczkiewicz K., Drgas O., Orlowska M.,
RA Perlinska-Lenart U., Aleksandrzak-Piekarczyk T., Szatraj K.,
RA Zielenkiewicz U., Pilsyk S., Malc E., Mieczkowski P., Kruszewska J.S.,
RA Biernat P., Pawlowska J.;
RT "Metabolic potential, ecology and presence of endohyphal bacteria is
RT reflected in genomic diversity of Mucoromycotina.";
RL Submitted (DEC-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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF14 subfamily.
CC {ECO:0000256|ARBA:ARBA00044508}.
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:KAG2188734.1}.
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DR EMBL; JAEPRA010000001; KAG2188734.1; -; Genomic_DNA.
DR OrthoDB; 1431934at2759; -.
DR Proteomes; UP000612746; 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; cd20341; BRcat_RBR_RNF14; 1.
DR CDD; cd20354; Rcat_RBR_RNF14; 1.
DR CDD; cd23820; RWD_RNF14; 1.
DR FunFam; 3.30.40.10:FF:000416; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 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; IPR047548; Rcat_RBR_RNF14.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF05773; RWD; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000612746};
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 21..147
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 205..451
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 209..255
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 479 AA; 55350 MW; 7F118E676312AA31 CRC64;
MASSLVVEED DNPLNDELQK EELVALSSIF GQNFMYNSHR STSGAEVISG TFSVRVEIPN
DTVEVILDQE KIHLHYLPPI IIEFTMTPRY PLQDVCKFSI QNVWLTKDQL NVLKTRLHDI
WESEKNVVGV MNQYFCIKFD QHAKPKHRCQ ILYNFADFLQ HDSLSCLGVS FPLELKNVTC
SGGVSLKKIL EQHEKSCLQE TFVHTSYTCS ICMEEKKGES CTQLSRCGHV FCKICLTGYF
AMLIREGMIH QVRCPDLECG AKKEDDNEPP SQEELILIVG EDLADRYDRL QLQLKLQADP
SITFCPRLQC QQPVRKDDNY DKLCLCSECG YAFCLICQKT WHGKQVHCQF KDTPAILQQY
LDCEDDPEEL KKLEAKYGKK NLEKLVNDYK IEMETEKWKR ENTVECPTCH IPVEKTFGCN
HMTCQICQTH FCFLCGSWVD PSHPYKHFNM QGNLCYMRLF EGAGDVYNID EMDLLEVQI
//
