PSO2_SCHPO
ID PSO2_SCHPO Reviewed; 560 AA.
AC Q10264; O13893;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=DNA cross-link repair protein pso2/snm1;
DE EC=3.1.-.-;
GN Name=pso2; Synonyms=snm1; ORFNames=SPAC22A12.01c, SPAC56F8.17c;
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 FUNCTION.
RX PubMed=12808110; DOI=10.1128/mcb.23.13.4728-4737.2003;
RA Lambert S., Mason S.J., Barber L.J., Hartley J.A., Pearce J.A., Carr A.M.,
RA McHugh P.J.;
RT "Schizosaccharomyces pombe checkpoint response to DNA interstrand cross-
RT links.";
RL Mol. Cell. Biol. 23:4728-4737(2003).
CC -!- FUNCTION: Required for DNA interstrand cross-link repair. This requires
CC cleavage of cross-linked DNA to generate DNA double strand breaks
CC (DSBs). This protein may have 5' exonuclease activity on single-
CC stranded and double-stranded DNA, which could be necessary for the
CC processing of DNA double strand breaks prior to religation.
CC {ECO:0000269|PubMed:12808110}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAA93588.1; -; Genomic_DNA.
DR PIR; T38927; T38927.
DR RefSeq; NP_593231.2; NM_001018628.2.
DR AlphaFoldDB; Q10264; -.
DR SMR; Q10264; -.
DR BioGRID; 278005; 24.
DR STRING; 4896.SPAC22A12.01c.1; -.
DR iPTMnet; Q10264; -.
DR MaxQB; Q10264; -.
DR PaxDb; Q10264; -.
DR PRIDE; Q10264; -.
DR EnsemblFungi; SPAC22A12.01c.1; SPAC22A12.01c.1:pep; SPAC22A12.01c.
DR GeneID; 2541503; -.
DR KEGG; spo:SPAC22A12.01c; -.
DR PomBase; SPAC22A12.01c; pso2.
DR VEuPathDB; FungiDB:SPAC22A12.01c; -.
DR eggNOG; KOG1361; Eukaryota.
DR HOGENOM; CLU_005260_4_1_1; -.
DR InParanoid; Q10264; -.
DR OMA; KSGPIYC; -.
DR PhylomeDB; Q10264; -.
DR PRO; PR:Q10264; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IMP:PomBase.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:PomBase.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IBA:GO_Central.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF07522; DRMBL; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..560
FT /note="DNA cross-link repair protein pso2/snm1"
FT /id="PRO_0000209129"
FT ZN_FING 106..135
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
SQ SEQUENCE 560 AA; 63076 MW; BF4BDE8C28EAD227 CRC64;
MSKRKSSSIL DFFKKSNNGK NMWGNEAVSV EKTDSTTKPS TVKNAISSSQ IKNEKFSQEV
LLQFNDPSFT SEVGESPQWQ SFGDANILEP LKNELVKNEE STMSELLLCP ICGITLESLT
VDANIHVNDC LDGRTTEAVS KKLKKDSVVK ADPSNSSTFP ISDSCKQALL PLPGKQINVR
SVVPFYKLMP YNIPFAVDAF AYGAIDGVEA YFLSHFHSDH YGGLTPKWKH GPIYCSEVTG
NLLINVMHVD EQYVKRLKLN QPYNIMGITV YVLDANHCPG SAMFVFETLQ SNQTRRVLHC
GDFRASKDHV MHPVLREKTI HKVYLDTTYL NPKYTFPPQA DVVQACADKA ISIKKSTDSR
LLVVVSTYSI GKEKVAVAIA KSLSSRIYVV PRKMHIIKQL ENQDLIDLLT DDPTQASVHM
VTMMGIHPNS LLDYLEQYNS SFDKIIGYKV TGWTFQPLEN RAQLSSSLDS IISRPPKFVE
YDLRAIRGST DKVAAFVAPY SEHSSFYDLT MFCLSMNIGH IIPTVNVGSQ RSREKMNVWL
DRWAWRRKKQ GLLSLENVDW
