位置:首页 > 蛋白库 > WSS2_SCHPO
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024