GenomeNet

Database: UniProt
Entry: P36607
LinkDB: P36607
Original site: P36607 
ID   RAD5_SCHPO              Reviewed;        1133 AA.
AC   P36607;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   16-OCT-2019, entry version 162.
DE   RecName: Full=DNA repair protein rad8 {ECO:0000305|PubMed:8290359};
DE            EC=3.6.4.-;
DE   AltName: Full=DNA repair protein RAD5 homolog {ECO:0000303|PubMed:8290359};
GN   Name=rad8 {ECO:0000303|PubMed:8290359};
GN   ORFNames=SPAC13G6.01c {ECO:0000312|PomBase:SPAC13G6.01c},
GN   SPAC5H10.14c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=8290359; DOI=10.1093/nar/21.25.5964;
RA   Doe C.L., Murray J.M., Shayeghi M., Hoskins M., Lehmann A.R.,
RA   Carrs A.M., Watts F.Z.;
RT   "Cloning and characterisation of the Schizosaccharomyces pombe rad8
RT   gene, a member of the SNF2 helicase family.";
RL   Nucleic Acids Res. 21:5964-5971(1993).
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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   FUNCTION.
RX   PubMed=14871939; DOI=10.1128/ec.3.1.82-90.2004;
RA   Malik M., Nitiss J.L.;
RT   "DNA repair functions that control sensitivity to topoisomerase-
RT   targeting drugs.";
RL   Eukaryot. Cell 3:82-90(2004).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the
RT   fission yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Probable helicase, member of the UBC2/RAD6 epistasis
CC       group. Functions with DNA repair protein rad18 in error-free
CC       postreplication DNA repair. Involved in the maintenance of wild-
CC       type rates of instability of simple repetitive sequences such as
CC       poly(GT) repeats (By similarity). Plays a role in surviving
CC       topoisomerase-mediated DNA damage (PubMed:14871939).
CC       {ECO:0000250|UniProtKB:P32849, ECO:0000269|PubMed:14871939,
CC       ECO:0000269|PubMed:8290359}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32849}.
CC       Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
DR   EMBL; X74615; CAA52686.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA89964.1; -; Genomic_DNA.
DR   PIR; S41478; S41478.
DR   RefSeq; XP_001713034.1; XM_001712982.2.
DR   BioGrid; 280467; 58.
DR   STRING; 4896.SPAC13G6.01c.1; -.
DR   iPTMnet; P36607; -.
DR   MaxQB; P36607; -.
DR   PaxDb; P36607; -.
DR   PRIDE; P36607; -.
DR   EnsemblFungi; SPAC13G6.01c.1; SPAC13G6.01c.1:pep; SPAC13G6.01c.
DR   EuPathDB; FungiDB:SPAC13G6.01c; -.
DR   PomBase; SPAC13G6.01c; rad8.
DR   HOGENOM; HOG000040492; -.
DR   InParanoid; P36607; -.
DR   OMA; RVFMMDP; -.
DR   PhylomeDB; P36607; -.
DR   PRO; PR:P36607; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; ISO:PomBase.
DR   GO; GO:0003678; F:DNA helicase activity; ISM:PomBase.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:PomBase.
DR   GO; GO:0006301; P:postreplication repair; ISO:PomBase.
DR   GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014905; HIRAN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00910; HIRAN; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1133       DNA repair protein rad8.
FT                                /FTId=PRO_0000056127.
FT   DOMAIN      516    705       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      971   1125       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     529    536       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   ZN_FING     877    923       RING-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00175}.
FT   MOTIF       656    659       DEGH box.
FT   MOD_RES      18     18       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
SQ   SEQUENCE   1133 AA;  128610 MW;  5A70C93D9933BF63 CRC64;
     MKRKVQKIID EAPLEENSPP RFFDSDVEAD SKPNDLTAAN SIVDLKTNSQ HENANAAGKE
     YGDSGVSESW VLDFLSVTGE KTISEFLAQK IWKTSNGDLN VAVDMYFDES FNIKNSNPDS
     ESQKDTDASL TQMDQLSNTV SVKDLSINRN TNKKALNAVS PSLNLSSNSS VQDVSIDKEE
     MMKKQSRNAL TPLDFIMKKN ELMKYIGCFG VEAYSTASGT RTLQAGERIY LERQKLSIKS
     QSRNSRKKSK LLSINSSCYS NIVRFCNSDH HEIGKLPTEV ASVISTLMEQ GFWSFEAICI
     YSDNIIRFGS NVTLQVYCFI NVNHPSLNRS PFTLATNSMQ EEEEHLKASF AQNKRDHLLR
     LFTWIALEPD LEDCNTKESI HIDDILKTSS LPEARDESNS DLTPSSTEDE EDVVSDQLAI
     LYDKVKTSGA ELPSAPKPST FALDLREYQK QALYWMCCKE EGVQSDGSAP KLHPLWSRFR
     FPKDSEFPEF FKCSSDDDNT HFYVNLYTGE TTMLFPNSMP YHRGGILADE MGLGKTIEVL
     SLIHSRPCFS TDEIPEAFRH SKPSLPVASR TTLVVAPMSL LDQWHSEACK VSQGTKFRSM
     IYYGSEKPLD LKSCVIDTST APLIIITSYG VLLSEFSQQS HSSGLFSVHW FRVVLDEGHN
     IRNRESKTAK ACHSISSQNR WVITGTPIVN KLDDLYSLIK FMRYEPWCNY TYWQTFVSLP
     YQSKDVLKAL NVVQSILEFL VLRRTKETKD RNGNSIVTLP PKTVKIEYLD FSDSERKIYD
     SLYTKAKSTV NANIVAGTLF RNYTTILGLL LRLRQACCDP VLLSNMTINS ETFDDFEFSV
     EQFNSLINQF VVTGKPIPSD ILKIDTLKSF EALITECPIC CNEPIQNPLL LNCKHACCGD
     CLSEHIQYQK RRNIIPPLCH TCRQPFNEQD VYKPFFVKNN GTQSTLLVGE EVKWKYWNRL
     QSVKLNGLLG QLRQLTHSSE PEKVVIFSQF TTFLDIIADV LESEKMGYAR FDGTMSQQMR
     STALETFRND PDVNVLIISL KAGGVGLNLT CANHVFIMDP WWSWSVEAQA IDRIHRLGQE
     KPVFVTRYIV RDTVEERMLK IQERKNFITG TLGMSEGKQQ VQSIEDIKML FEY
//
DBGET integrated database retrieval system