RAD22_SCHPO
ID RAD22_SCHPO Reviewed; 469 AA.
AC P36592;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=DNA repair and recombination protein rad22;
GN Name=rad22; ORFNames=SPAC30D11.10;
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].
RC STRAIN=972 / ATCC 24843;
RX PubMed=8290356; DOI=10.1093/nar/21.25.5940;
RA Ostermann K., Lorentz A., Schmidt H.;
RT "The fission yeast rad22 gene, having a function in mating-type switching
RT and repair of DNA damages, encodes a protein homolog to Rad52 of
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 21:5940-5944(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 INTERACTION WITH RHP51.
RX PubMed=14551247; DOI=10.1091/mbc.e03-05-0288;
RA Catlett M.G., Forsburg S.L.;
RT "Schizosaccharomyces pombe Rdh54 (TID1) acts with Rhp54 (RAD54) to repair
RT meiotic double-strand breaks.";
RL Mol. Biol. Cell 14:4707-4720(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-319, AND
RP IDENTIFICATION 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: Active in the repair of DNA damage and in mating-type
CC switching. Probably involved in the repair of DNA double-strands
CC breaks. Has a role in promoting S phase completion.
CC -!- SUBUNIT: Interacts with rhp51. {ECO:0000269|PubMed:14551247}.
CC -!- INTERACTION:
CC P36592; O13351: pmt3; NbExp=4; IntAct=EBI-966242, EBI-966336;
CC P36592; P36592: rad22; NbExp=3; IntAct=EBI-966242, EBI-966242;
CC P36592; P36601: rhp51; NbExp=5; IntAct=EBI-966242, EBI-926960;
CC P36592; Q92372: ssb1; NbExp=2; IntAct=EBI-966242, EBI-966394;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RAD52 family. {ECO:0000305}.
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DR EMBL; X72220; CAA51021.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA91896.1; -; Genomic_DNA.
DR PIR; S41496; S41496.
DR RefSeq; NP_593207.1; NM_001018603.2.
DR AlphaFoldDB; P36592; -.
DR SMR; P36592; -.
DR BioGRID; 279519; 63.
DR IntAct; P36592; 7.
DR MINT; P36592; -.
DR STRING; 4896.SPAC30D11.10.1; -.
DR iPTMnet; P36592; -.
DR MaxQB; P36592; -.
DR PaxDb; P36592; -.
DR PRIDE; P36592; -.
DR EnsemblFungi; SPAC30D11.10.1; SPAC30D11.10.1:pep; SPAC30D11.10.
DR GeneID; 2543086; -.
DR KEGG; spo:SPAC30D11.10; -.
DR PomBase; SPAC30D11.10; -.
DR VEuPathDB; FungiDB:SPAC30D11.10; -.
DR eggNOG; KOG4141; Eukaryota.
DR HOGENOM; CLU_011431_3_2_1; -.
DR InParanoid; P36592; -.
DR OMA; VSYIESW; -.
DR PhylomeDB; P36592; -.
DR Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-SPO-5685938; HDR through Single Strand Annealing (SSA).
DR PRO; PR:P36592; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0003684; F:damaged DNA binding; TAS:PomBase.
DR GO; GO:0045027; F:DNA end binding; IDA:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:PomBase.
DR GO; GO:0000730; P:DNA recombinase assembly; NAS:PomBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:PomBase.
DR GO; GO:0045002; P:double-strand break repair via single-strand annealing; IBA:GO_Central.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IMP:PomBase.
DR GO; GO:0007533; P:mating type switching; IMP:PomBase.
DR GO; GO:0006312; P:mitotic recombination; IMP:PomBase.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR GO; GO:0110027; P:negative regulation of DNA strand resection involved in replication fork processing; EXP:PomBase.
DR GO; GO:0010947; P:negative regulation of meiotic joint molecule formation; IDA:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IGI:PomBase.
DR GO; GO:0000722; P:telomere maintenance via recombination; IGI:PomBase.
DR Gene3D; 3.30.390.80; -; 1.
DR InterPro; IPR004585; DNA_recomb/repair_Rad52.
DR InterPro; IPR041247; Rad52_fam.
DR InterPro; IPR007232; Rad52_Rad59_Rad22.
DR InterPro; IPR042525; Rad52_Rad59_Rad22_sf.
DR PANTHER; PTHR12132; PTHR12132; 1.
DR Pfam; PF04098; Rad52_Rad22; 1.
DR TIGRFAMs; TIGR00607; rad52; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..469
FT /note="DNA repair and recombination protein rad22"
FT /id="PRO_0000173891"
FT REGION 265..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 34
FT /note="T -> S (in Ref. 1; CAA51021)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="D -> E (in Ref. 1; CAA51021)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 51961 MW; E6B8B538D28B899D CRC64;
MSFEQKQHVA SEDQGHFNTA YSHEEFNFLQ SSLTRKLGPE YVSRRSGPGG FSVSYIESWK
AIELANEIFG FNGWSSSIRS INVDFMDENK ENGRISLGLS VIVRVTIKDG AYHEDIGYGS
IDNCRGKASA FEKCKKEGTT DALKRALRNF GNSLGNCMYD KYYLREVGKM KPPTYHFDSG
DLFRKTDPAA RESFIKKQKT LNSTRTVNNQ PLVNKGEQLA PRRAAELNDE QTREIEMYAD
EELDNIFVED DIIAHLAVAE DTAHPAANNH HSEKAGTQIN NKDKGSHNSA KPVQRSHTYP
VAVPQNTSDS VGNAVTDTSP KTLFDPLKPN TGTPSPKFIS ARAAAAAEGV VSAPFTNNFN
PRLDSPSIRK TSIIDHSKSL PVQRASVLPI IKQSSQTSPV SNNSMIRDSE SIINERKENI
GLIGVKRSLH DSTTSHNKSD LMRTNSDPQS AMRSRENYDA TVDKKAKKG
