RAD60_SCHPO
ID RAD60_SCHPO Reviewed; 406 AA.
AC Q9USX3;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=DNA repair protein rad60;
GN Name=rad60; ORFNames=SPBC1921.02;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11971984; DOI=10.1128/mcb.22.10.3537-3548.2002;
RA Morishita T., Tsutsui Y., Iwasaki H., Shinagawa H.;
RT "The Schizosaccharomyces pombe rad60 gene is essential for repairing
RT double-strand DNA breaks spontaneously occurring during replication and
RT induced by DNA damaging agents.";
RL Mol. Cell. Biol. 22:3537-3548(2002).
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, INTERACTION WITH SMC5, AND PHOSPHORYLATION BY CDS1.
RX PubMed=12897162; DOI=10.1128/mcb.23.16.5939-5946.2003;
RA Boddy M.N., Shanahan P., McDonald W.H., Lopez-Girona A., Noguchi E.,
RA Yates J.R. III, Russell P.;
RT "Replication checkpoint kinase Cds1 regulates recombinational repair
RT protein Rad60.";
RL Mol. Cell. Biol. 23:5939-5946(2003).
RN [4]
RP INTERACTION WITH RFP1.
RX PubMed=17502373; DOI=10.1074/jbc.m702652200;
RA Kosoy A., Calonge T.M., Outwin E.A., O'Connell M.J.;
RT "Fission yeast Rnf4 homologs are required for DNA repair.";
RL J. Biol. Chem. 282:20388-20394(2007).
CC -!- FUNCTION: Required for repair of DNA double strand breaks which occur
CC during replication, or induced by UV or gamma radiation, via
CC recombination between sister chromatids. This has a subsequent role in
CC the maintenance of chromosome structure. May work in conjunction with
CC the Smc5-Smc6 complex. {ECO:0000269|PubMed:11971984,
CC ECO:0000269|PubMed:12897162}.
CC -!- SUBUNIT: Interacts with rfp1 and smc5. {ECO:0000269|PubMed:12897162,
CC ECO:0000269|PubMed:17502373}.
CC -!- INTERACTION:
CC Q9USX3; P40984: hus5; NbExp=2; IntAct=EBI-3650521, EBI-966468;
CC Q9USX3; O13710: smc5; NbExp=2; IntAct=EBI-3650521, EBI-603756;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11971984}.
CC -!- PTM: Phosphorylated by cds1. {ECO:0000269|PubMed:12897162}.
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DR EMBL; CU329671; CAB58968.1; -; Genomic_DNA.
DR EMBL; AB089814; BAC07534.1; -; Genomic_DNA.
DR PIR; T39786; T39786.
DR RefSeq; NP_595995.1; NM_001021903.2.
DR PDB; 3GOE; X-ray; 0.97 A; A=332-406.
DR PDB; 3RCZ; X-ray; 1.90 A; A=332-406.
DR PDBsum; 3GOE; -.
DR PDBsum; 3RCZ; -.
DR AlphaFoldDB; Q9USX3; -.
DR SMR; Q9USX3; -.
DR BioGRID; 277321; 22.
DR DIP; DIP-44205N; -.
DR IntAct; Q9USX3; 8.
DR MINT; Q9USX3; -.
DR STRING; 4896.SPBC1921.02.1; -.
DR iPTMnet; Q9USX3; -.
DR MaxQB; Q9USX3; -.
DR PaxDb; Q9USX3; -.
DR PRIDE; Q9USX3; -.
DR EnsemblFungi; SPBC1921.02.1; SPBC1921.02.1:pep; SPBC1921.02.
DR GeneID; 2540802; -.
DR KEGG; spo:SPBC1921.02; -.
DR PomBase; SPBC1921.02; rad60.
DR VEuPathDB; FungiDB:SPBC1921.02; -.
DR eggNOG; ENOG502SBJ2; Eukaryota.
DR HOGENOM; CLU_685422_0_0_1; -.
DR InParanoid; Q9USX3; -.
DR OMA; FKVKSNQ; -.
DR EvolutionaryTrace; Q9USX3; -.
DR PRO; PR:Q9USX3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..406
FT /note="DNA repair protein rad60"
FT /id="PRO_0000097154"
FT STRAND 333..343
FT /evidence="ECO:0007829|PDB:3GOE"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:3GOE"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:3GOE"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:3GOE"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:3GOE"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:3GOE"
SQ SEQUENCE 406 AA; 46077 MW; 5FF406D9FC791983 CRC64;
MDNLDEDDLA FFSKPIKKPP LNYAKQLIAS SSDSEEESEL DTNKQALEHI NAQKNITHNE
NKSAEPLSRQ STILDADEGN QDVSDTTPNA CLNEGRHSPK SAISCVTQPV SPVYNTRAAA
NLRNNSINSE AALSTTSSLL DDDFARRLEE IDRQVQEFEK SSSDMDVQIH THKREIEEDD
DNTSADVPLL KHSKSDHSTL YHSKSEFSTN EPVISVVLQL AVIGQRIPNS NISLPRDWEA
PLFFKVKSNQ QFRRVRIAYS ERKKVDNVVL VFQNQRLWDY GTPKGAGMLK VDTRLVVHAY
CHSDFISLKR IKELEVEKLS SVTEDSTAQT CKLITLLLRS SKSEDLRLSI PVDFTVKDLI
KRYCTEVKIS FHERIRLEFE GEWLDPNDQV QSTELEDEDQ VSVVLD
