SWI10_SCHPO
ID SWI10_SCHPO Reviewed; 252 AA.
AC Q06182;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Mating-type switching protein swi10;
GN Name=swi10; ORFNames=SPBC4F6.15c;
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].
RX PubMed=1475195; DOI=10.1093/nar/20.23.6347;
RA Roedel C., Kirchhoff S., Schmidt H.;
RT "The protein sequence and some intron positions are conserved between the
RT switching gene swi10 of Schizosaccharomyces pombe and the human excision
RT repair gene ERCC1.";
RL Nucleic Acids Res. 20:6347-6353(1992).
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).
CC -!- FUNCTION: Involved in termination of copy-synthesis during mating-type
CC switching. Involved in nucleotide excision repair of DNA damaged with
CC UV light, bulky adducts, or cross-linking agents. Along with RAD16
CC forms an endonuclease that specifically degrades single-stranded DNA.
CC -!- SUBUNIT: Heterodimer composed of rad16 and swi10.
CC -!- INTERACTION:
CC Q06182; P36617: rad16; NbExp=2; IntAct=EBI-16120325, EBI-16120215;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the ERCC1/RAD10/SWI10 family. {ECO:0000305}.
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DR EMBL; X61926; CAA43928.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA20735.1; -; Genomic_DNA.
DR PIR; S30292; S30292.
DR RefSeq; NP_596115.1; NM_001022032.2.
DR AlphaFoldDB; Q06182; -.
DR SMR; Q06182; -.
DR BioGRID; 277404; 54.
DR DIP; DIP-61016N; -.
DR IntAct; Q06182; 3.
DR STRING; 4896.SPBC4F6.15c.1; -.
DR iPTMnet; Q06182; -.
DR MaxQB; Q06182; -.
DR PaxDb; Q06182; -.
DR EnsemblFungi; SPBC4F6.15c.1; SPBC4F6.15c.1:pep; SPBC4F6.15c.
DR GeneID; 2540887; -.
DR KEGG; spo:SPBC4F6.15c; -.
DR PomBase; SPBC4F6.15c; swi10.
DR VEuPathDB; FungiDB:SPBC4F6.15c; -.
DR eggNOG; KOG2841; Eukaryota.
DR HOGENOM; CLU_041616_3_0_1; -.
DR InParanoid; Q06182; -.
DR OMA; LNPDYIC; -.
DR PhylomeDB; Q06182; -.
DR Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR PRO; PR:Q06182; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0070522; C:ERCC4-ERCC1 complex; IBA:GO_Central.
DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IPI:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:PomBase.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0000736; P:double-strand break repair via single-strand annealing, removal of nonhomologous ends; IMP:PomBase.
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:0000710; P:meiotic mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
DR GO; GO:0070914; P:UV-damage excision repair; IBA:GO_Central.
DR InterPro; IPR004579; ERCC1/RAD10/SWI10.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR12749; PTHR12749; 1.
DR Pfam; PF03834; Rad10; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00597; rad10; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW Nucleus; Reference proteome.
FT CHAIN 1..252
FT /note="Mating-type switching protein swi10"
FT /id="PRO_0000072347"
FT DNA_BIND 76..98
FT /evidence="ECO:0000255"
SQ SEQUENCE 252 AA; 28638 MW; C08FC0DA01F04EA7 CRC64;
MSDIDDEEFE QLAVSALEEV EKKAGFAQQP TPQKVSRVTA HSILVNPRQK GNPLLPHVRN
VPWEYTDIVP DFVMGTGICS LFLSLKYHHL HPEYIYSRIS KLGKSYNLRI LLILVDVENH
QASIQELVKT SIVNQYTLIL AWSSEEAARY LETYKAYENM SPALIMEKPS TDYLSQVQSF
LTSIRGINKS DSLSLLSKFG SLERALVASR DELEQLEGWG PTKVNRFLEA VQQPFMSHST
IKRPEAINLK QT
