WSS1_SCHPO
ID WSS1_SCHPO Reviewed; 283 AA.
AC Q9P7B5;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 ORFNames=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; CAB86466.1; -; Genomic_DNA.
DR RefSeq; NP_593097.1; NM_001018494.2.
DR AlphaFoldDB; Q9P7B5; -.
DR SMR; Q9P7B5; -.
DR BioGRID; 279888; 3.
DR STRING; 4896.SPAC521.02.1; -.
DR MEROPS; M80.A03; -.
DR PaxDb; Q9P7B5; -.
DR EnsemblFungi; SPAC521.02.1; SPAC521.02.1:pep; SPAC521.02.
DR GeneID; 2543468; -.
DR KEGG; spo:SPAC521.02; -.
DR PomBase; SPAC521.02; -.
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:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; ISO:PomBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0019985; P:translesion synthesis; ISO:PomBase.
DR InterPro; IPR013536; WLM_dom.
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..283
FT /note="DNA-dependent metalloprotease WSS1 homolog"
FT /id="PRO_0000351446"
FT DOMAIN 29..216
FT /note="WLM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00730"
FT REGION 199..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 256..263
FT /note="SUMO interaction motif (SIM)"
FT /evidence="ECO:0000250|UniProtKB:P38838"
FT COMPBIAS 199..218
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 283 AA; 32359 MW; 3B80DEEEE39A6E35 CRC64;
MIAILYLYYI LTTSILLSVS FMLRINDDDH PNEKIGFISA IKGDFHDLSS DYLKRIAAMA
FPIMKEHGFG VTSLDEVAYN AKFWGRNWNK GECIELVLRD ASNRWLPFEF VMDVFLHELC
HIWQGPHDRR FFSHLSTLRA ALIALYAKGY KGPGKYMTWD SFVLANVVGN YNTVVFNGIT
LERSTMHGVE TCGGSLQRKK KIRRKPTPSS TKKRKLTRTG QKLGTDMNIR LELLKSPAKP
QAQSMRGREA RIAAALLRVD NSNEYKPKDH NSSTTLENYF VVE
