RAD5_SCHPO
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 03-AUG-2022, entry version 175.
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}, SPAC5H10.14c;
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], 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., Carrs A.M.,
RA Watts F.Z.;
RT "Cloning and characterisation of the Schizosaccharomyces pombe rad8 gene, a
RT 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., 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).
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-targeting
RT 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 fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP 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 group.
CC Functions with DNA repair protein rad18 in error-free postreplication
CC DNA repair. Involved in the maintenance of wild-type rates of
CC instability of simple repetitive sequences such as poly(GT) repeats (By
CC similarity). Plays a role in surviving topoisomerase-mediated DNA
CC damage (PubMed:14871939). {ECO:0000250|UniProtKB:P32849,
CC ECO:0000269|PubMed:14871939, ECO:0000269|PubMed:8290359}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32849}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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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 AlphaFoldDB; P36607; -.
DR SMR; P36607; -.
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 PomBase; SPAC13G6.01c; rad8.
DR VEuPathDB; FungiDB:SPAC13G6.01c; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR InParanoid; P36607; -.
DR OMA; WSNFSFW; -.
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:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; NAS:PomBase.
DR GO; GO:0003677; F:DNA binding; ISO:PomBase.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IC:PomBase.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
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 Gene3D; 3.40.50.300; -; 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-rel_dom; 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; Cytoplasm; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1133
FT /note="DNA repair protein rad8"
FT /id="PRO_0000056127"
FT DOMAIN 516..705
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 971..1125
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 877..923
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 656..659
FT /note="DEGH box"
FT BINDING 529..536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="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
