位置:首页 > 蛋白库 > RAD18_CANAL
RAD18_CANAL
ID   RAD18_CANAL             Reviewed;         378 AA.
AC   Q5A4N5; A0A1D8PPP7; O94001;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Postreplication repair E3 ubiquitin-protein ligase RAD18;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase RAD18 {ECO:0000305};
GN   Name=RAD18; OrderedLocusNames=CAALFM_C601770WA;
GN   ORFNames=Ca20C1.14c, CaO19.10910, CaO19.3407;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1161;
RA   Oliver K., Harris D., Barrell B.G., Rajandream M.A.;
RT   "Candida albicans strain 1161 genome pilot sequencing project.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: E3 RING-finger protein, member of the UBC2/RAD6 epistasis
CC       group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to
CC       form the UBC2-RAD18 ubiquitin ligase complex involved in
CC       postreplicative repair (PRR) of damaged DNA. {ECO:0000250}.
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with E2 UBC2, forming a complex with ubiquitin
CC       ligase activity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RAD18 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL033391; CAA21935.1; -; Genomic_DNA.
DR   EMBL; CP017628; AOW30114.1; -; Genomic_DNA.
DR   RefSeq; XP_716717.2; XM_711624.2.
DR   AlphaFoldDB; Q5A4N5; -.
DR   SMR; Q5A4N5; -.
DR   BioGRID; 1224731; 1.
DR   STRING; 237561.Q5A4N5; -.
DR   PRIDE; Q5A4N5; -.
DR   GeneID; 3641637; -.
DR   KEGG; cal:CAALFM_C601770WA; -.
DR   CGD; CAL0000182971; RAD18.
DR   VEuPathDB; FungiDB:C6_01770W_A; -.
DR   HOGENOM; CLU_028491_2_0_1; -.
DR   InParanoid; Q5A4N5; -.
DR   OrthoDB; 1013108at2759; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q5A4N5; -.
DR   Proteomes; UP000000559; Chromosome 6.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0097505; C:Rad6-Rad18 complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR   GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR039577; Rad18.
DR   InterPro; IPR004580; Rad18_fungi.
DR   InterPro; IPR006642; Rad18_UBZ4.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR14134; PTHR14134; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00513; SAP; 1.
DR   SMART; SM00734; ZnF_Rad18; 1.
DR   TIGRFAMs; TIGR00599; rad18; 1.
DR   PROSITE; PS50800; SAP; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS51908; ZF_UBZ4; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..378
FT                   /note="Postreplication repair E3 ubiquitin-protein ligase
FT                   RAD18"
FT                   /id="PRO_0000056153"
FT   DOMAIN          287..321
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT   ZN_FING         29..67
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         181..209
FT                   /note="UBZ4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   REGION          109..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          233..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   BINDING         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   BINDING         204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   CONFLICT        86
FT                   /note="I -> V (in Ref. 1; CAA21935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="V -> A (in Ref. 1; CAA21935)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        266
FT                   /note="S -> A (in Ref. 1; CAA21935)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   378 AA;  42482 MW;  E9A4E8D1607A8909 CRC64;
     MNLKDITDPS DFKTTKLPAL AELDILKRCY ICKDLLNAPV RTQCDHTYCS QCIREFLLRD
     NRCPLCKTEV FESGLKRDPL LEEIVISYAS LRPHLLRLLE IEKVESKQEV DREKSANESA
     SNGNRNVNND VDETVRVKDQ SNADELGEEK GQAQHGEQVN EQTTEVISLL SDDEENGSDS
     LVKCPICFER MELDVLQGKH IDDCLSGKST KRTPTDILSP KAKRPKQITS FFKPTIDTKT
     PSPPTSKAST TPTATPTTTL LKANVSSPSP VAQSTVHKGK PLPKLDFSSL STQKIKAKLS
     DLKLPTTGSR NEMEARYLHY YVIYNANLDS NHPVKESILR QQLKQWEMVQ HQPSFGDAEW
     KGAETGNWKE LIARARSN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024