ID   RAD16_SCHPO             Reviewed;         877 AA.
AC   P36617;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 2.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=DNA repair protein rad16;
DE            EC=3.1.-.-;
GN   Name=rad16; Synonyms=rad10, rad20, swi9; ORFNames=SPCC970.01;
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], AND MUTAGENESIS OF GLU-659.
RX   PubMed=8114734; DOI=10.1128/mcb.14.3.2029-2040.1994;
RA   Carr A.M., Schmidt H., Kirchoff S., Muriel W.J., Sheldrick K.S.,
RA   Griffiths D.J., Basmacioglu C.N., Subramani S., Clegg M., Nasim A.,
RA   Lehmann A.R.;
RT   "The rad16 gene of Schizosaccharomyces pombe: a homolog of the RAD1 gene of
RT   Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 14:2029-2040(1994).
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [4]
RP   FUNCTION.
RX   PubMed=166019; DOI=10.1093/genetics/79.4.573;
RA   Nasim A., Smith B.P.;
RT   "Genetic control of radiation sensitivity in Schizosaccharomyces pombe.";
RL   Genetics 79:573-582(1975).
RN   [5]
RP   FUNCTION.
RX   PubMed=10080187; DOI=10.1038/6838;
RA   Fleck O., Lehmann E., Schaer P., Kohli J.;
RT   "Involvement of nucleotide-excision repair in msh2 pms1-independent
RT   mismatch repair.";
RL   Nat. Genet. 21:314-317(1999).
RN   [6]
RP   FUNCTION.
RX   PubMed=12628934; DOI=10.1093/emboj/cdg119;
RA   Prudden J., Evans J.S., Hussey S.P., Deans B., O'Neill P., Thacker J.,
RA   Humphrey T.;
RT   "Pathway utilization in response to a site-specific DNA double-strand break
RT   in fission yeast.";
RL   EMBO J. 22:1419-1430(2003).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Endonuclease that specifically degrades single-stranded DNA
CC       and which is involved in nucleotide excision repair of DNA damaged with
CC       UV light, bulky adducts, or cross-linking agents. Required for double
CC       strand break-induced interchromosomal gene conversion.
CC       {ECO:0000269|PubMed:10080187, ECO:0000269|PubMed:12628934,
CC       ECO:0000269|PubMed:166019}.
CC   -!- SUBUNIT: Heterodimer composed of rad16 and swi10.
CC   -!- INTERACTION:
CC       P36617; O94542: SPCC1322.02; NbExp=5; IntAct=EBI-16120215, EBI-16120253;
CC       P36617; Q06182: swi10; NbExp=2; IntAct=EBI-16120215, EBI-16120325;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, spindle pole body
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA50599.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; X71595; CAA50599.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU329672; CAA20694.2; -; Genomic_DNA.
DR   PIR; A56213; A56213.
DR   RefSeq; NP_587855.2; NM_001022848.2.
DR   AlphaFoldDB; P36617; -.
DR   SMR; P36617; -.
DR   BioGRID; 275343; 32.
DR   DIP; DIP-61015N; -.
DR   IntAct; P36617; 4.
DR   STRING; 4896.SPCC970.01.1; -.
DR   MaxQB; P36617; -.
DR   PaxDb; P36617; -.
DR   EnsemblFungi; SPCC970.01.1; SPCC970.01.1:pep; SPCC970.01.
DR   GeneID; 2538760; -.
DR   KEGG; spo:SPCC970.01; -.
DR   PomBase; SPCC970.01; rad16.
DR   VEuPathDB; FungiDB:SPCC970.01; -.
DR   eggNOG; KOG0442; Eukaryota.
DR   HOGENOM; CLU_002265_2_0_1; -.
DR   InParanoid; P36617; -.
DR   OMA; FHKILQA; -.
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:P36617; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IPI:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:1990599; F:3' overhang single-stranded DNA endodeoxyribonuclease activity; IDA:PomBase.
DR   GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IBA:GO_Central.
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; IMP:PomBase.
DR   GO; GO:0000736; P:double-strand break repair via single-strand annealing, removal of nonhomologous ends; 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:0006289; P:nucleotide-excision repair; IGI:PomBase.
DR   GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IMP:PomBase.
DR   GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR   GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR   InterPro; IPR006166; ERCC4_domain.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR006167; XPF.
DR   Pfam; PF02732; ERCC4; 1.
DR   SMART; SM00891; ERCC4; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR00596; rad1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; DNA damage; DNA repair; DNA-binding; Endonuclease;
KW   Hydrolase; Nuclease; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..877
FT                   /note="DNA repair protein rad16"
FT                   /id="PRO_0000198856"
FT   DOMAIN          652..732
FT                   /note="ERCC4"
FT   REGION          440..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..457
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         71
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         659
FT                   /note="E->K: In swi9."
FT                   /evidence="ECO:0000269|PubMed:8114734"
SQ   SEQUENCE   877 AA;  100264 MW;  B08764366A445CF6 CRC64;
     METKVHLPLA YQQQVFNELI EEDGLCVIAP GLSLLQIAAN VLSYFAVPGS LLLLVGANVD
     DIELIQHEME SHLEKKLITV NTETMSVDKR EKSYLEGGIF AITSRILVMD LLTKIIPTEK
     ITGIVLLHAD RVVSTGTVAF IMRLYRETNK TGFIKAFSDD PEQFLMGINA LSHCLRCLFL
     RHVFIYPRFH VVVAESLEKS PANVVELNVN LSDSQKTIQS CLLTCIESTM RELRRLNSAY
     LDMEDWNIES ALHRSFDVIV RRQLDSVWHR VSPKTKQLVG DLSTLKFLLS ALVCYDCVSF
     LKLLDTLVLS VNVSSYPSNA QPSPWLMLDA ANKMIRVARD RVYKESEGPN MDAIPILEEQ
     PKWSVLQDVL NEVCHETMLA DTDAETSNNS IMIMCADERT CLQLRDYLST VTYDNKDSLK
     NMNSKLVDYF QWREQYRKMS KSIKKPEPSK EREASNTTSR KGVPPSKRRR VRGGNNATSR
     TTSDNTDAND SFSRDLRLEK ILLSHLSKRY EPEVGNDAFE VIDDFNSIYI YSYNGERDEL
     VLNNLRPRYV IMFDSDPNFI RRVEVYKATY PKRSLRVYFM YYGGSIEEQK YLFSVRREKD
     SFSRLIKERS NMAIVLTADS ERFESQESKF LRNVNTRIAG GGQLSITNEK PRVIVDLREF
     RSSLPSILHG NNFSVIPCQL LVGDYILSPK ICVERKSIRD LIQSLSNGRL YSQCEAMTEY
     YEIPVLLIEF EQHQSFTSPP FSDLSSEIGK NDVQSKLVLL TLSFPNLRIV WSSSAYVTSI
     IFQDLKAMEQ EPDPASAASI GLEAGQDSTN TYNQAPLDLL MGLPYITMKN YRNVFYGGVK
     DIQEASETSE RKWSELIGPE AGRRLYSFFR KQLKDYE