ID   WSS1_SCHPO              Reviewed;         262 AA.
AC   Q9P7B5; A0AAN2H635;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-APR-2025, sequence version 2.
DT   02-SEP-2026, entry version 118.
DE   RecName: Full=DNA-dependent metalloprotease WSS1 homolog;
DE            EC=3.4.24.- {ECO:0000250|UniProtKB:P38838};
DE   AltName: Full=DNA damage response protein WSS1 homolog;
GN   Name=wss1; ORFNames=SPAC521.02 {ECO:0000312|PomBase:SPAC521.02};
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: Metalloendopeptidase that acts selectively on DNA-binding
CC       proteins. DNA is needed to bring the protease and substrates together
CC       to enable proteolysis. Involved in the repair of toxic DNA-protein
CC       cross-links (DPCs) such as covalently trapped topoisomerase 1 (top1)
CC       adducts on DNA lesions or DPCs induced by reactive compounds such as
CC       formaldehyde. Involved in DNA damage response and processing of stalled
CC       or collapsed replication forks by removing the covalently trapped top1
CC       from chromatin. DPC proteolysis enables the repair of the lesions via
CC       downstream DNA repair pathways. May be recruited to DPCs via the
CC       SUMOylation of substrate proteins at damaged DNA sites (By similarity).
CC       {ECO:0000250|UniProtKB:P38838}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q9H040};
CC   -!- SUBUNIT: Binds to DNA. Interacts with pmt3/smt3.
CC       {ECO:0000250|UniProtKB:P38838}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- DOMAIN: The SUMO interaction motif (SIM) is important for binding to
CC       pmt3/smt3 (SUMO). {ECO:0000250|UniProtKB:P38838}.
CC   -!- SIMILARITY: Belongs to the peptidase M3 family. WSS1-like
CC       metalloprotease (WLM) subfamily. {ECO:0000305}.
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DR   EMBL; CU329670; CAK9837308.1; -; Genomic_DNA.
DR   RefSeq; NP_593097.2; NM_001018494.3.
DR   AlphaFoldDB; Q9P7B5; -.
DR   SMR; Q9P7B5; -.
DR   BioGRID; 279888; 3.
DR   FunCoup; Q9P7B5; 270.
DR   STRING; 284812.Q9P7B5; -.
DR   MEROPS; M80.A03; -.
DR   PaxDb; 284812-Q9P7B5; -.
DR   GeneID; 2543468; -.
DR   KEGG; spo:2543468; -.
DR   PomBase; SPAC521.02; wss1.
DR   VEuPathDB; FungiDB:SPAC521.02; -.
DR   eggNOG; KOG4842; Eukaryota.
DR   HOGENOM; CLU_1058290_0_0_1; -.
DR   InParanoid; Q9P7B5; -.
DR   OMA; YMTWDSF; -.
DR   PhylomeDB; Q9P7B5; -.
DR   PRO; PR:Q9P7B5; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004222; F:metalloendopeptidase activity; ISO:PomBase.
DR   GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR   GO; GO:0106300; P:protein-DNA covalent cross-linking repair; ISO:PomBase.
DR   GO; GO:0019985; P:translesion synthesis; ISO:PomBase.
DR   InterPro; IPR013536; WLM_dom.
DR   InterPro; IPR053000; WSS1-like_metalloprotease.
DR   PANTHER; PTHR46622; DNA-DEPENDENT METALLOPROTEASE WSS1; 1.
DR   PANTHER; PTHR46622:SF1; DNA-DEPENDENT METALLOPROTEASE WSS1; 1.
DR   Pfam; PF08325; WLM; 1.
DR   PROSITE; PS51397; WLM; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   DNA damage; Hydrolase; Metal-binding; Metalloprotease; Nucleus; Protease;
KW   Reference proteome; Zinc.
FT   CHAIN           1..262
FT                   /note="DNA-dependent metalloprotease WSS1 homolog"
FT                   /id="PRO_0000351446"
FT   DOMAIN          8..195
FT                   /note="WLM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00730"
FT   REGION          178..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           235..242
FT                   /note="SUMO interaction motif (SIM)"
FT                   /evidence="ECO:0000250|UniProtKB:P38838"
FT   COMPBIAS        178..196
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   262 AA;  29939 MW;  297C435F3139FE8D CRC64;
     MLRINDDDHP NEKIGFISAI KGDFHDLSSD YLKRIAAMAF PIMKEHGFGV TSLDEVAYNA
     KFWGRNWNKG ECIELVLRDA SNRWLPFEFV MDVFLHELCH IWQGPHDRRF FSHLSTLRAA
     LIALYAKGYK GPGKYMTWDS FVLANVVGNY NTVVFNGITL ERSTMHGVET CGGSLQRKKK
     IRRKPTPSST KKRKLTRTGQ KLGTDMNIRL ELLKSPAKPQ AQSMRGREAR IAAALLRVDN
     SNEYKPKDHN SSTTLENYFV VE
//