WSS2_SCHPO
ID WSS2_SCHPO Reviewed; 282 AA.
AC O94580;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA-dependent metalloprotease WSS1 homolog 2 {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:P38838};
DE AltName: Full=DNA damage response protein WSS1 homolog 2 {ECO:0000305};
GN Name=wss2 {ECO:0000312|PomBase:SPCC1442.07c};
GN Synonyms=wss1b {ECO:0000303|PubMed:27871365}; ORFNames=SPCC1442.07c;
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).
RN [3] {ECO:0007744|PDB:5JIG, ECO:0007744|PDB:5LN5}
RP X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) OF 106-232 IN COMPLEX WITH NICKEL.
RX PubMed=27871365; DOI=10.1016/j.molcel.2016.09.031;
RA Stingele J., Bellelli R., Alte F., Hewitt G., Sarek G., Maslen S.L.,
RA Tsutakawa S.E., Borg A., Kjaer S., Tainer J.A., Skehel J.M., Groll M.,
RA Boulton S.J.;
RT "Mechanism and regulation of DNA-protein crosslink repair by the DNA-
RT dependent metalloprotease SPRTN.";
RL Mol. Cell 64:688-703(2016).
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. {ECO:0000250|UniProtKB:P38838}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:27871365};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the peptidase M3 family. WSS1-like
CC metalloprotease (WLM) subfamily. {ECO:0000305}.
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DR EMBL; CU329672; CAA21441.1; -; Genomic_DNA.
DR PIR; T40972; T40972.
DR RefSeq; NP_588321.1; NM_001023312.2.
DR PDB; 5JIG; X-ray; 1.00 A; A=107-232.
DR PDB; 5LN5; X-ray; 1.75 A; A/B=107-233.
DR PDBsum; 5JIG; -.
DR PDBsum; 5LN5; -.
DR AlphaFoldDB; O94580; -.
DR SMR; O94580; -.
DR BioGRID; 275334; 9.
DR STRING; 4896.SPCC1442.07c.1; -.
DR MEROPS; M80.A04; -.
DR MaxQB; O94580; -.
DR PaxDb; O94580; -.
DR EnsemblFungi; SPCC1442.07c.1; SPCC1442.07c.1:pep; SPCC1442.07c.
DR GeneID; 2538751; -.
DR KEGG; spo:SPCC1442.07c; -.
DR PomBase; SPCC1442.07c; -.
DR VEuPathDB; FungiDB:SPCC1442.07c; -.
DR eggNOG; KOG4842; Eukaryota.
DR HOGENOM; CLU_056790_0_0_1; -.
DR InParanoid; O94580; -.
DR OMA; WELFRQL; -.
DR PhylomeDB; O94580; -.
DR PRO; PR:O94580; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:PomBase.
DR GO; GO:0070628; F:proteasome binding; IPI:PomBase.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:PomBase.
DR GO; GO:0046914; F:transition metal ion binding; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0006281; P:DNA repair; IDA:PomBase.
DR GO; GO:0016925; P:protein sumoylation; ISO:PomBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR013536; WLM_dom.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF08325; WLM; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS51397; WLM; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA repair; Hydrolase; Metal-binding;
KW Metalloprotease; Nucleus; Protease; Reference proteome; Zinc.
FT CHAIN 1..282
FT /note="DNA-dependent metalloprotease WSS1 homolog 2"
FT /id="PRO_0000350746"
FT DOMAIN 1..75
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 99..274
FT /note="WLM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00730"
FT REGION 234..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000305|PubMed:27871365, ECO:0007744|PDB:5JIG,
FT ECO:0007744|PDB:5LN5"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000305|PubMed:27871365, ECO:0007744|PDB:5JIG,
FT ECO:0007744|PDB:5LN5"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000305|PubMed:27871365, ECO:0007744|PDB:5JIG,
FT ECO:0007744|PDB:5LN5"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:5JIG"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:5JIG"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:5JIG"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:5JIG"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:5JIG"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:5JIG"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:5JIG"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:5JIG"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:5JIG"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:5JIG"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:5JIG"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:5JIG"
SQ SEQUENCE 282 AA; 32464 MW; F464FAE9FE8CB57E CRC64;
MELKFSCRGN VIALSFNEND TVLDAKEKLG QEIDVSPSLI KLLYKGNLSD DSHLQDVVKN
ESKIMCLIRQ DKDIVNQAIS QLKVPDYSTN TYSLKPKKPH TTPKPASIYT FNELVVLDYP
HKDRALRYLE RLRDDTGIKK IMDSHRWTVP LLSEMDPAEH TRHDSKTLGL NHNQGAHIEL
RLRTDRYDGF RDYKTVKSTL IHELTHNVHG EHDSSFWELF RQLTKEADAA DLLGKPGSYV
SDRASYTPQQ DNDDEDQKNH RRDLLLAAAE RRKQSGSKVQ KE
