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RAD31_SCHPO
ID   RAD31_SCHPO             Reviewed;         307 AA.
AC   P79064;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 143.
DE   RecName: Full=DNA damage tolerance protein rad31;
GN   Name=rad31; ORFNames=SPAC4C5.04;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=9092625; DOI=10.1093/nar/25.6.1162;
RA   Shayeghi M., Doe C.L., Tavassoli M., Watts F.Z.;
RT   "Characterisation of Schizosaccharomyces pombe rad31, a UBA-related gene
RT   required for DNA damage tolerance.";
RL   Nucleic Acids Res. 25:1162-1169(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Could be involved in a ubiquitin-related process important
CC       for DNA damage tolerance. Acts in a process which is defective in the
CC       checkpoint rad mutants and which involves hus5.
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DR   EMBL; Y08805; CAA70043.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB11175.1; -; Genomic_DNA.
DR   PIR; T45213; T45213.
DR   RefSeq; NP_593251.1; NM_001018648.2.
DR   AlphaFoldDB; P79064; -.
DR   SMR; P79064; -.
DR   BioGRID; 280021; 11.
DR   IntAct; P79064; 2.
DR   STRING; 4896.SPAC4C5.04.1; -.
DR   MaxQB; P79064; -.
DR   PaxDb; P79064; -.
DR   PRIDE; P79064; -.
DR   EnsemblFungi; SPAC4C5.04.1; SPAC4C5.04.1:pep; SPAC4C5.04.
DR   GeneID; 2543606; -.
DR   KEGG; spo:SPAC4C5.04; -.
DR   PomBase; SPAC4C5.04; rad31.
DR   VEuPathDB; FungiDB:SPAC4C5.04; -.
DR   eggNOG; KOG2014; Eukaryota.
DR   HOGENOM; CLU_002556_4_1_1; -.
DR   InParanoid; P79064; -.
DR   OMA; TDVWGTF; -.
DR   PhylomeDB; P79064; -.
DR   Reactome; R-SPO-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR   Reactome; R-SPO-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR   PRO; PR:P79064; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0031510; C:SUMO activating enzyme complex; IBA:GO_Central.
DR   GO; GO:0019948; F:SUMO activating enzyme activity; IDA:PomBase.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IGI:PomBase.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR   GO; GO:0016925; P:protein sumoylation; IDA:PomBase.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953; PTHR10953; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
PE   4: Predicted;
KW   DNA damage; Reference proteome.
FT   CHAIN           1..307
FT                   /note="DNA damage tolerance protein rad31"
FT                   /id="PRO_0000194974"
SQ   SEQUENCE   307 AA;  34703 MW;  FA4E72BFB6261B55 CRC64;
     MGNHNINAEE IALYDRQIRL WGFNAQQALK QSRVLLITAS PLANEIAKNL VLSGIGKLCV
     LDSMTVYEKD VEEQFFIEAS DIGQLRANVF KKKLHELNPL VEIDTDTSLI SEIDEGKISK
     FSMVIATQLD YEEFCRINEL TRICNASFYA TSCFGLYGFA FCDLINHNFA IDRVVDNTKV
     EEDMFIVQKP MKEAFQSILG ETLKPRLAKK IPTLYPAMLS LLKSKKSDPD SIRQVCIEQK
     LNEKTVLNGE FLSKFSSNIS FQWTPVMSVV GGVVSQDALN SISKKQFPID NFWIFDAESG
     LAPIYRL
 
 
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