UVE1_SCHPO
ID UVE1_SCHPO Reviewed; 599 AA.
AC Q10988; P87339;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=UV-damage endonuclease;
DE Short=UVDE;
DE EC=3.-.-.-;
GN Name=uve1; Synonyms=uvde; ORFNames=SPBC19C7.09c;
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], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8614629; DOI=10.1093/nar/24.7.1267;
RA Takao M., Yonemasu R., Yamamoto K., Yasui A.;
RT "Characterization of a UV endonuclease gene from the fission yeast
RT Schizosaccharomyces pombe and its bacterial homolog.";
RL Nucleic Acids Res. 24:1267-1271(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX PubMed=9023111; DOI=10.1093/nar/25.5.1002;
RA Davey S., Nass M.L., Ferrer J.V., Sidik K., Eisenberger A., Mitchell D.L.,
RA Freyer G.A.;
RT "The fission yeast UVDR DNA repair pathway is inducible.";
RL Nucleic Acids Res. 25:1002-1008(1997).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=14599746; DOI=10.1016/j.dnarep.2003.08.005;
RA Fraser J.L.A., Neill E., Davey S.;
RT "Fission yeast Uve1 and Apn2 function in distinct oxidative damage repair
RT pathways in vivo.";
RL DNA Repair 2:1253-1267(2003).
RN [5]
RP FUNCTION.
RX PubMed=14704348; DOI=10.1093/nar/gkh151;
RA Ribar B., Izumi T., Mitra S.;
RT "The major role of human AP-endonuclease homolog Apn2 in repair of abasic
RT sites in Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 32:115-126(2004).
CC -!- FUNCTION: Endonuclease for the repair of UV-irradiated DNA. Involved in
CC the excision of cyclobutane pyrimidine dimers (CPD) and 6-4 pyrimidine
CC pyrimidones (6-4PP) which forms the UV damage repair (UVDR) pathway.
CC Functions also in oxidative damage repair in vivo. Provides back-up AP
CC endonuclease activity to apn2 together with apn1.
CC {ECO:0000269|PubMed:14599746, ECO:0000269|PubMed:14704348,
CC ECO:0000269|PubMed:8614629, ECO:0000269|PubMed:9023111}.
CC -!- INDUCTION: By UV light. {ECO:0000269|PubMed:9023111}.
CC -!- SIMILARITY: Belongs to the uve1/UvsE family. {ECO:0000305}.
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DR EMBL; D78571; BAA11415.1; -; mRNA.
DR EMBL; U78487; AAC49664.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19577.1; -; Genomic_DNA.
DR PIR; S71134; S71134.
DR RefSeq; NP_596165.1; NM_001022085.2.
DR AlphaFoldDB; Q10988; -.
DR SMR; Q10988; -.
DR BioGRID; 276874; 26.
DR STRING; 4896.SPBC19C7.09c.1; -.
DR iPTMnet; Q10988; -.
DR SwissPalm; Q10988; -.
DR PaxDb; Q10988; -.
DR PRIDE; Q10988; -.
DR EnsemblFungi; SPBC19C7.09c.1; SPBC19C7.09c.1:pep; SPBC19C7.09c.
DR GeneID; 2540345; -.
DR KEGG; spo:SPBC19C7.09c; -.
DR PomBase; SPBC19C7.09c; uve1.
DR VEuPathDB; FungiDB:SPBC19C7.09c; -.
DR eggNOG; ENOG502QTMI; Eukaryota.
DR HOGENOM; CLU_017168_3_0_1; -.
DR InParanoid; Q10988; -.
DR OMA; IRETWTR; -.
DR PhylomeDB; Q10988; -.
DR PRO; PR:Q10988; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000262; C:mitochondrial chromosome; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:1990043; F:5' deoxyribonuclease (pyrimidine dimer) activity; IDA:PomBase.
DR GO; GO:0004519; F:endonuclease activity; IDA:PomBase.
DR GO; GO:0000404; F:heteroduplex DNA loop binding; IDA:PomBase.
DR GO; GO:0006284; P:base-excision repair; IMP:PomBase.
DR GO; GO:0006298; P:mismatch repair; IMP:PomBase.
DR GO; GO:0043504; P:mitochondrial DNA repair; IMP:PomBase.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR GO; GO:0006290; P:pyrimidine dimer repair; IDA:PomBase.
DR GO; GO:0070914; P:UV-damage excision repair; IDA:PomBase.
DR GO; GO:1990731; P:UV-damage excision repair, DNA incision; IDA:PomBase.
DR InterPro; IPR004601; UvdE.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR PANTHER; PTHR31290; PTHR31290; 1.
DR Pfam; PF03851; UvdE; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR00629; uvde; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA excision; DNA repair; Endonuclease; Hydrolase; Nuclease;
KW Reference proteome.
FT CHAIN 1..599
FT /note="UV-damage endonuclease"
FT /id="PRO_0000215029"
FT REGION 89..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 68816 MW; C09ED7219D5895BE CRC64;
MLRLLKRNIQ ISKRIVFTIL KQKAFKGNHP CVPSVCTITY SRFHCLPDTL KSLLPMSSKT
TLSMLPQVNI GANSFSAETP VDLKKENETE LANISGPHKK STSTSTRKRA RSSKKKATDS
VSDKIDESVA SYDSSTHLRR SSRSKKPVNY NSSSESESEE QISKATKKVK QKEEEEYVEE
VDEKSLKNES SSDEFEPVVP EQLETPISKR RRSRSSAKNL EKESTMNLDD HAPREMFDCL
DKPIPWRGRL GYACLNTILR SMKERVFCSR TCRITTIQRD GLESVKQLGT QNVLDLIKLV
EWNHNFGIHF MRVSSDLFPF ASHAKYGYTL EFAQSHLEEV GKLANKYNHR LTMHPGQYTQ
IASPREVVVD SAIRDLAYHD EILSRMKLNE QLNKDAVLII HLGGTFEGKK ETLDRFRKNY
QRLSDSVKAR LVLENDDVSW SVQDLLPLCQ ELNIPLVLDW HHHNIVPGTL REGSLDLMPL
IPTIRETWTR KGITQKQHYS ESADPTAISG MKRRAHSDRV FDFPPCDPTM DLMIEAKEKE
QAVFELCRRY ELQNPPCPLE IMGPEYDQTR DGYYPPGAEK RLTARKRRSR KEEVEEDEK
