TYDP1_SCHPO
ID TYDP1_SCHPO Reviewed; 536 AA.
AC Q9USG9;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable tyrosyl-DNA phosphodiesterase;
DE Short=Tyr-DNA phosphodiesterase;
DE EC=3.1.4.- {ECO:0000250|UniProtKB:P38319};
GN ORFNames=SPCP31B10.05;
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 [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 [2]
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: DNA repair enzyme that can remove a variety of covalent
CC adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving
CC rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-
CC end complexes between DNA and the topoisomerase I active site tyrosine
CC residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA
CC double-strand breaks due to DNA damage by radiation and free radicals.
CC Acts on blunt-ended double-strand DNA breaks and on single-stranded
CC DNA. May have low 3'exonuclease activity and may be able to remove a
CC single nucleoside from the 3'end of DNA and RNA molecules with
CC 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with
CC a 3'phosphate (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P38319}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the tyrosyl-DNA phosphodiesterase family.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAB58371.1; -; Genomic_DNA.
DR PIR; T41695; T41695.
DR RefSeq; NP_587861.1; NM_001022854.2.
DR AlphaFoldDB; Q9USG9; -.
DR SMR; Q9USG9; -.
DR BioGRID; 276138; 41.
DR STRING; 4896.SPCP31B10.05.1; -.
DR MaxQB; Q9USG9; -.
DR PaxDb; Q9USG9; -.
DR EnsemblFungi; SPCP31B10.05.1; SPCP31B10.05.1:pep; SPCP31B10.05.
DR GeneID; 2539579; -.
DR KEGG; spo:SPCP31B10.05; -.
DR PomBase; SPCP31B10.05; -.
DR VEuPathDB; FungiDB:SPCP31B10.05; -.
DR eggNOG; KOG2031; Eukaryota.
DR HOGENOM; CLU_010413_2_0_1; -.
DR InParanoid; Q9USG9; -.
DR OMA; PLIKECW; -.
DR PhylomeDB; Q9USG9; -.
DR PRO; PR:Q9USG9; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0106334; F:3'-deoxyribose phosphate lyase activity; IDA:PomBase.
DR GO; GO:0017005; F:3'-tyrosyl-DNA phosphodiesterase activity; IDA:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; IMP:PomBase.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0000012; P:single strand break repair; IBA:GO_Central.
DR InterPro; IPR010347; Tdp1.
DR PANTHER; PTHR12415; PTHR12415; 1.
DR Pfam; PF06087; Tyr-DNA_phospho; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; Exonuclease; Hydrolase; Nuclease; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..536
FT /note="Probable tyrosyl-DNA phosphodiesterase"
FT /id="PRO_0000340099"
FT REGION 315..318
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT ACT_SITE 122
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT ACT_SITE 401
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
FT SITE 426
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q9NUW8"
SQ SEQUENCE 536 AA; 61595 MW; 8902B3EBD488DFCE CRC64;
MSTLEPEKRR QHEDKSNEII DSPIFLNKIS ALPESENVHC LLLKQLIGSP QLKQTWQFNF
CVDLNFLLEN MHASVFPTVD VRITHGYDSK SDSLARLTAQ MNHCPVNVKL YSVYVPMWGT
HHSKIMVNFF KDDSCQIVIH TANLVEPDWI GMSQAIFKTP LLYPKANDSL STSSVPEYGN
PSKIRKHEGS LDIKDDRNCD IIDVDSAFEN FKHKSDTRSS DDLGVIGRQF QQDFLAYLKN
YRHTYELIEK LKMYDFSAIR AIFIGSVPGK FEGEEESSWG LGKLKKILKM LEKDSKKDEK
TKFEESDICI SQCSSMGSFG PKQEYIAELT DGFGCQRGNW KFLFPTVKEV QQSMLGWQSG
SSIHFNILGK TAASQVETLK KGKNLCKWVA MKAGRQRVAP HIKTYMRFSN DGELLRWVLV
TSANLSKPAW GTLEGHKAKS RSTRGLRIRS YEAGVLLYPK LFEESQRAPC IMTPTYKTNT
PNLDEKRREF YGKRVIGVRM CWDFPPVEYE DKDEIWSPVI NRTDKDWLGY VWPPNW
