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SRS2_SCHPO
ID   SRS2_SCHPO              Reviewed;         887 AA.
AC   Q10213;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=ATP-dependent DNA helicase srs2;
DE            EC=3.6.4.12;
GN   Name=srs2; ORFNames=SPAC4H3.05;
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 [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   [2]
RP   FUNCTION.
RX   PubMed=14993467; DOI=10.1093/nar/gkh317;
RA   Doe C.L., Whitby M.C.;
RT   "The involvement of Srs2 in post-replication repair and homologous
RT   recombination in fission yeast.";
RL   Nucleic Acids Res. 32:1480-1491(2004).
CC   -!- FUNCTION: ATP-dependent DNA helicase involved in DNA repair at least
CC       for UV-induced lesions. Also aids the recombinational repair of
CC       camptothecin-induced collapsed replication forks.
CC       {ECO:0000269|PubMed:14993467}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- INTERACTION:
CC       Q10213; O13600: sws1; NbExp=2; IntAct=EBI-8527058, EBI-8527040;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAA93344.1; -; Genomic_DNA.
DR   PIR; T38885; T38885.
DR   RefSeq; NP_594341.1; NM_001019762.2.
DR   AlphaFoldDB; Q10213; -.
DR   SMR; Q10213; -.
DR   BioGRID; 279992; 70.
DR   IntAct; Q10213; 1.
DR   MINT; Q10213; -.
DR   STRING; 4896.SPAC4H3.05.1; -.
DR   iPTMnet; Q10213; -.
DR   MaxQB; Q10213; -.
DR   PaxDb; Q10213; -.
DR   PRIDE; Q10213; -.
DR   EnsemblFungi; SPAC4H3.05.1; SPAC4H3.05.1:pep; SPAC4H3.05.
DR   GeneID; 2543577; -.
DR   KEGG; spo:SPAC4H3.05; -.
DR   PomBase; SPAC4H3.05; srs2.
DR   VEuPathDB; FungiDB:SPAC4H3.05; -.
DR   eggNOG; KOG2108; Eukaryota.
DR   HOGENOM; CLU_004585_4_2_1; -.
DR   InParanoid; Q10213; -.
DR   OMA; HCANILI; -.
DR   PhylomeDB; Q10213; -.
DR   PRO; PR:Q10213; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR   GO; GO:0006301; P:postreplication repair; IGI:PomBase.
DR   GO; GO:0000725; P:recombinational repair; IMP:PomBase.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..887
FT                   /note="ATP-dependent DNA helicase srs2"
FT                   /id="PRO_0000102083"
FT   DOMAIN          9..304
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   DOMAIN          305..597
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT   BINDING         33..38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   BINDING         302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   887 AA;  101124 MW;  39830861766783F1 CRC64;
     METKSSYLKF LNEEQRISVQ SPHKYTQILA GPGSGKTRVL TARVAYLLQK NHIAAEDLII
     ATFTNKAANE IKLRIEAILG NSEASKLISG TFHSIAYKYL VKYGKHIGLS SNWLIADRND
     TQAIMKRLLD SLKKAKNPIA SGIRGQELTP QNALNRITKL KSNGLLVKPG MDQLSLINGL
     EEPPKELQSH QSVELYRLYQ TSLWKNNLAD FDDLLLNFIL LLQKQPDCVR NIKHILIDEF
     QDTSKIQYFL VKLLALQNSD ITIVGDPDQS IYGFRSAEIR NLNQMSEDFE GTQVLHLERN
     YRSAKPILEL ALSIISQDKS RPKKGLKSNH ISSLKPHYRL FETNNKESYW IAREIKRIVG
     SCPELIFYND IAILVRSSSL TRSLEHALSE LGVPYRMVGV NKFFDREEIR DLIAYLRVLA
     NKDSTSLIRV INVPPRNIGK TKIDRIIFES ERRGLTFWQT LNEVKNENIL LSQRNDKSFL
     KSLKSFLCSI SKLENRYLSN GHSATLSDLL LGILSEIKYY EYLVRKNKET VEEKWENVME
     LVQQSDNISC IFYELDYKIS TIVLLQNFLT QIALVNEEQK EGESQKVTIS TLHAAKGLEW
     PVVFLPCLCE NIIPHSRSDD LDEERRLLYV GATRAQALLY LSSFKSVTGM FADMQNSDNV
     QDVSPFLKGE EMKRWVMESE IVFNEKIASE IGTILGRKSY GKITNLSGIG SNANHNGTKF
     ENLGFQCCRV LAEAELKKRE RVKSVNDYNK DETNFRKHNA KRSKTDIRSW FEKKQPIDSD
     VEISEPSRSA SIMVANKDLN DRSFETVNRI VSTRASTTNA SFMSSVRQNL GRGPSTKDQV
     INRTLREGHQ DVVQHTDLNQ SNTKVASARP AGSRKRLGVR LRVSRML
 
 
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