ID B6JWP1_SCHJY Unreviewed; 426 AA.
AC B6JWP1;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Postreplication repair E3 ubiquitin-protein ligase RAD18 {ECO:0000256|ARBA:ARBA00015551};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING-type E3 ubiquitin transferase RAD18 {ECO:0000256|ARBA:ARBA00031783};
GN Name=rhp18 {ECO:0000313|JaponicusDB:SJAG_00819};
GN ORFNames=SJAG_00819 {ECO:0000313|EMBL:EEB05792.1};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB05792.1, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB05792.1, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RAD18 family.
CC {ECO:0000256|ARBA:ARBA00009506}.
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DR EMBL; KE651166; EEB05792.1; -; Genomic_DNA.
DR RefSeq; XP_002172085.1; XM_002172049.1.
DR AlphaFoldDB; B6JWP1; -.
DR STRING; 402676.B6JWP1; -.
DR EnsemblFungi; EEB05792; EEB05792; SJAG_00819.
DR GeneID; 7048893; -.
DR JaponicusDB; SJAG_00819; rhp18.
DR VEuPathDB; FungiDB:SJAG_00819; -.
DR eggNOG; KOG0287; Eukaryota.
DR HOGENOM; CLU_028491_2_0_1; -.
DR OMA; IPNTGPR; -.
DR OrthoDB; 6177at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
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:0036297; P:interstrand cross-link repair; IEA:EnsemblFungi.
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; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039577; Rad18.
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; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR PANTHER; PTHR14134:SF2; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF57850; RING/U-box; 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 {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PROSITE-
KW ProRule:PRU01256};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PROSITE-
KW ProRule:PRU01256}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 28..66
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 167..194
FT /note="UBZ4-type"
FT /evidence="ECO:0000259|PROSITE:PS51908"
FT DOMAIN 293..327
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 136..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 47529 MW; A92AA78487302878 CRC64;
MQADTTDSSD WQNTRLPSLT SFESLLRCPI CHDFFSGPLI TSCCHSFCSY CIRCYLKDHS
ICPICRSEQQ ESRLRKNLVV EELVEGFNKL RSSLLEQLAP VPEPIPESES KSICLPEPIV
EDELVYVDEV SNSPSMTIKN SPSPVVSIPS RSSRASTGKK RKVAPATVPC PICDDQISED
QIQSHVNACI DKQEKAASLQ HEIQELESSL NSLADSNASR SKTNALKRTL LSKRNTLQRL
RTPQSILPSS SSSSSTSLAT TNSGLSVSVT STVSRNHREM PIEERVRLPK ITYAILSESK
MRSKLSELGL PTDGNKQTLQ RRHSQWVTMY NANLDRTHPV TRAVLLRELR DWEYAQSRKP
IVKRDKIGGP DWEKLYADDF ERLVGNARNN MKRNSTAKKP GESKNNISAG ASSDAAREPT
SHESEV
//
