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