ID G0VDF8_NAUCC Unreviewed; 674 AA.
AC G0VDF8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 08-NOV-2023, entry version 56.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=NCAS0C05300 {ECO:0000313|EMBL:CCC69520.1};
GN OrderedLocusNames=NCAS_0C05300 {ECO:0000313|EMBL:CCC69520.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC69520.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC69520.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the ZNF598/HEL2 family.
CC {ECO:0000256|ARBA:ARBA00035113}.
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DR EMBL; HE576754; CCC69520.1; -; Genomic_DNA.
DR RefSeq; XP_003675884.1; XM_003675836.1.
DR AlphaFoldDB; G0VDF8; -.
DR STRING; 1064592.G0VDF8; -.
DR GeneID; 11526330; -.
DR KEGG; ncs:NCAS_0C05300; -.
DR eggNOG; KOG2231; Eukaryota.
DR HOGENOM; CLU_008515_2_0_1; -.
DR InParanoid; G0VDF8; -.
DR OMA; HTTCHKC; -.
DR OrthoDB; 3059402at2759; -.
DR Proteomes; UP000001640; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:InterPro.
DR CDD; cd16615; RING-HC_ZNF598; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041888; RING-HC_ZNF598/Hel2.
DR InterPro; IPR044288; ZNF598/Hel2.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22938:SF0; E3 UBIQUITIN-PROTEIN LIGASE ZNF598; 1.
DR PANTHER; PTHR22938; ZINC FINGER PROTEIN 598; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 72..112
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 75797 MW; B30829ECB13B92CA CRC64;
MTDQQPTPSK ALKTADKTQK KSTSKANTKA KNDTAKANKK GKSRISKPIE EIARTTRNLD
INSGDDDDDD LCLICASKLV YASLSPCNHT TCHKCSFKQR SLYNKKACLI CRTENDKLIF
TENINANYTD SNLGHYQFNE KYGIVFTSEE VATATLNLLK YTCSVCPANK DGIEREDFGS
YKKYNEHLRS KHNKCLCTIC AQNNHIFPSE LPVYTQNQLR NHQSKGNSEG FKGHPLCAFC
SGQRFYGDDE LYVHMRNKHE KCHICDKIDH NSPQYFKDYD QLFDHFKNFH YICTVQTCLD
NKFIVFKDEL ELQAHILKEH GDLIRGKPKL FQSELSTFMS GPSRVVRDRD AMNYDMDSRP
SLFSSSPSSS ATPLGTDGND DNSDNDIPEL RQLRLEERAK YYLENSQELY DKFIKCNDEY
DKGYLTGLGL LDSYKEIFTT PQSNVYLLIN NVAKLYPKNS PKFKELNAIY EAQEQKLYLQ
NGLPSLSGSS ASISSATRSW NNSGSVAMNR NIRDLPTLEA KSKSFDPFAT TVKKTPALRT
MKKTVVKKVS PSPIAYTPLG GSSLSSLSTV PRLPTTNVSN TVRMGSSTNG KNKKLADLNL
PQLPTPKPKV YIPPLRKTTI PDPKQWGGGG QNVPSTDNLP SLPIHHSNGS SQSNQQKGKR
GKQKQKQLLF HIGI
//
