ID RAD14_SCHPO Reviewed; 289 AA.
AC O59753;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 01-MAY-2013, entry version 74.
DE RecName: Full=DNA repair protein rad14;
DE AltName: Full=XP-A family homolog rhp14;
GN Name=rhp14; Synonyms=rad14; ORFNames=SPBC649.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales;
OC Schizosaccharomycetaceae; Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
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.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=11408483; DOI=10.1074/jbc.M104039200;
RA Hohl M., Christensen O., Kunz C., Naegeli H., Fleck O.;
RT "Binding and repair of mismatched DNA mediated by Rhp14, the fission
RT yeast homologue of human XPA.";
RL J. Biol. Chem. 276:30766-30772(2001).
CC -!- FUNCTION: Involved in nucleotide excision repair (NER). Functional
CC in repair of ultraviolet radiation induced damages and in mitotic
CC mutation avoidance. Binds damaged DNA. Binds specifically to base-
CC base mismatches or small insertion/deletion loops with unpaired
CC nucleotides. Maintains GT repeat stability. Functions as a part of
CC the short-patch excision repair system.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC -!- SIMILARITY: Belongs to the XPA family.
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DR EMBL; CU329671; CAA19045.1; -; Genomic_DNA.
DR PIR; T40596; T40596.
DR RefSeq; NP_595222.1; NM_001021128.2.
DR HSSP; P23025; 1D4U.
DR ProteinModelPortal; O59753; -.
DR STRING; 4896.SPBC649.03-1; -.
DR EnsemblFungi; SPBC649.03.1; SPBC649.03.1:pep; SPBC649.03.
DR GeneID; 2541120; -.
DR KEGG; spo:SPBC649.03; -.
DR PomBase; SPBC649.03; -.
DR eggNOG; COG5145; -.
DR HOGENOM; HOG000161510; -.
DR KO; K10847; -.
DR OMA; ECDSIEL; -.
DR OrthoDB; EOG44N22D; -.
DR NextBio; 20802233; -.
DR GO; GO:0000109; C:nucleotide-excision repair complex; ISO:PomBase.
DR GO; GO:0003684; F:damaged DNA binding; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IMP:PomBase.
DR GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; ISO:PomBase.
DR GO; GO:0070914; P:UV-damage excision repair; IMP:PomBase.
DR InterPro; IPR009061; DNA-bd_dom_put.
DR InterPro; IPR000465; XPA.
DR InterPro; IPR022656; XPA_C.
DR InterPro; IPR022652; Znf_XPA_CS.
DR PANTHER; PTHR10142; PTHR10142; 1.
DR Pfam; PF05181; XPA_C; 1.
DR Pfam; PF01286; XPA_N; 1.
DR SUPFAM; SSF46955; Putativ_DNA_bind; 1.
DR TIGRFAMs; TIGR00598; rad14; 1.
DR PROSITE; PS00752; XPA_1; FALSE_NEG.
DR PROSITE; PS00753; XPA_2; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; DNA damage; DNA repair; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1 289 DNA repair protein rad14.
FT /FTId=PRO_0000274248.
FT ZN_FING 116 140
SQ SEQUENCE 289 AA; 34663 MW; F9C2D8B582D30D6F CRC64;
MENSSIVKSP NPTIEEQRNE IEKLKNLTGI EEVHVDGAKV NKRKRTFDEQ SEITKDYIEY
DFSKIEDTKG GYLLEEKKVE DLREKPAERE LREQEERQKK LRLAPLNLDP ETAPKCFECD
SIELDTKYFD IFHCRVCHTC REKYPDKYSL LTKTECKLDY LLTEPELQDQ ELLPRLLKAN
PHQQGWSNMM LYLRYQVEEF AKKKWGSMEA LDAEFERREV QKKEMKEKKF EKQLLELRKR
TRTSNYSRMS IREKRKHVHS YDEEFEKPNE PGVIVQRCKC GLEIEQLEI
//
