ID RAD13_SCHPO Reviewed; 1112 AA.
AC P28706; O59728;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 27-MAR-2024, entry version 164.
DE RecName: Full=DNA repair protein rad13;
DE EC=3.1.-.-;
GN Name=rad13; ORFNames=SPBC3E7.08c;
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 [MRNA].
RX PubMed=8464724; DOI=10.1093/nar/21.6.1345;
RA Carr A.M., Sheldrick K.S., Murray J.M., Al-Harithy R., Watts F.Z.,
RA Lehmann A.R.;
RT "Evolutionary conservation of excision repair in Schizosaccharomyces pombe:
RT evidence for a family of sequences related to the Saccharomyces cerevisiae
RT RAD2 gene.";
RL Nucleic Acids Res. 21:1345-1349(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).
CC -!- FUNCTION: Single-stranded DNA endonuclease involved in excision repair
CC of DNA damaged with UV light, bulky adducts, or cross-linking agents.
CC Essential for the incision step of excision-repair (Probable).
CC {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. They probably participate in
CC the reaction catalyzed by the enzyme. May bind an additional third
CC magnesium ion after substrate binding. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X66795; CAA47291.1; -; mRNA.
DR EMBL; CU329671; CAA19011.1; -; Genomic_DNA.
DR PIR; S30301; S30301.
DR PIR; T40382; T40382.
DR RefSeq; NP_596095.1; NM_001022011.2.
DR AlphaFoldDB; P28706; -.
DR SMR; P28706; -.
DR BioGRID; 277566; 74.
DR STRING; 284812.P28706; -.
DR iPTMnet; P28706; -.
DR MaxQB; P28706; -.
DR PaxDb; 4896-SPBC3E7-08c-1; -.
DR EnsemblFungi; SPBC3E7.08c.1; SPBC3E7.08c.1:pep; SPBC3E7.08c.
DR GeneID; 2541051; -.
DR KEGG; spo:SPBC3E7.08c; -.
DR PomBase; SPBC3E7.08c; rad13.
DR VEuPathDB; FungiDB:SPBC3E7.08c; -.
DR eggNOG; KOG2520; Eukaryota.
DR HOGENOM; CLU_003018_0_0_1; -.
DR InParanoid; P28706; -.
DR OMA; PNSMDFS; -.
DR PhylomeDB; P28706; -.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR PRO; PR:P28706; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004520; F:DNA endonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; ISO: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 CDD; cd09904; H3TH_XPG; 1.
DR CDD; cd09868; PIN_XPG_RAD2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 2.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR001044; XPG/Rad2_eukaryotes.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR NCBIfam; TIGR00600; rad2; 1.
DR PANTHER; PTHR16171:SF7; DNA EXCISION REPAIR PROTEIN ERCC-5; 1.
DR PANTHER; PTHR16171; DNA REPAIR PROTEIN COMPLEMENTING XP-G CELLS-RELATED; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR PRINTS; PR00066; XRODRMPGMNTG.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS00841; XPG_1; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..1112
FT /note="DNA repair protein rad13"
FT /id="PRO_0000154036"
FT DOMAIN 395..414
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 1..95
FT /note="N-domain"
FT REGION 660..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..870
FT /note="I-domain"
FT REGION 1056..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 777
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 779
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 798
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 800
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 849
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 8
FT /note="D -> N (in Ref. 1; CAA47291)"
FT /evidence="ECO:0000305"
FT CONFLICT 738..743
FT /note="LKNQKR -> AQKSKKG (in Ref. 1; CAA47291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1112 AA; 126329 MW; 7ECF4229D5BF4768 CRC64;
MGVSGLWDIL EPVKRPVKLE TLVNKRLAID ASIWIYQFLK AVRDKEGNQL KSSHVVGFFR
RICKLLFFGI KPVFVFDGGA PSLKRQTIQK RQARRLDREE NATVTANKLL ALQMRHQAML
LEENNKKATA LANASVQNER QMPSSMTLDN SEIKPVLNQR KNYLKPDPYQ LPEMDVSFDK
LGSSYDPRIM SQDELTQYVS SFTKIEDINL FDFSNIDFDS ELFQSLPDTD KYSILSAARL
RSRLRMGLSS EQLSEMFPNR MDFSRFQIER LKERNDLTQR LMDFTGMNEF GPSRVVSEKN
REYILVKNEG AEGGWALGVI SGSTNNEPII IDDEATKLSS NLIDEDEDEA FYDVPLPSRS
HSMNPRELVA AKLKEIKENS FSENQQSDEA DYNVTDDLIL QLATQQSLEE NKKSKELFSL
SASEFDKLNS EKKTFEILST DIPAEDSMNS LLNDEENLKL EHVGDVSNDS LAFAEKKHPE
NGTSIFMDAL PSASREKKTN DLIDPLPFQP MDWGKSIFFE KLKKPTETFM DSKTDIPSEA
PDNSKLVEDT NLHTINATVN IESDLDAAKP GIENPIISPL LPVKDDEKDL DLRELNPLEP
FENMKEQADD GTVTNPLNVS SDKAMSVYLL SSENAKDTGD IKSESIDAVL PTLETSSPSL
SIPTDFQKEA SPNKGAAALS SKVEPEVVEK LLDEEEEEMI IRMAEEEKEY DRFVSELNQR
HETEEWNQEA FEKRLKELKN QKRSEKRDAD EVTQVMIKEC QELLRLFGLP YIVAPQEAEA
QCSKLLELKL VDGIVTDDSD VFLFGGTRVY RNMFNQNKFV ELYLMDDMKR EFNVNQMDLI
KLAHLLGSDY TMGLSRVGPV LALEILHEFP GDTGLFEFKK WFQRLSTGHA SKNDVNTPVK
KRINKLVGKI ILPSEFPNPL VDEAYLHPAV DDSKQSFQWG IPDLDELRQF LMATVGWSKQ
RTNEVLLPVI QDMHKKQFVG TQSNLTQFFE GGNTNVYAPR VAYHFKSKRL ENALSSFKNQ
ISNQSPMSEE IQADADAFGE SKGSDELQSR ILRRKKMMAS KNSSDSDSDS EDNFLASLTP
KTNSSSISIE NLPRKTKLST SLLKKPSKRR RK
//
