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YAUB_SCHPO
ID   YAUB_SCHPO              Reviewed;         322 AA.
AC   Q10166;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Hydrolase C26A3.11;
DE            EC=3.5.-.-;
GN   ORFNames=SPAC26A3.11;
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).
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       NIT1/NIT2 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA93234.1; -; Genomic_DNA.
DR   PIR; T38399; T38399.
DR   RefSeq; NP_594154.1; NM_001019578.2.
DR   AlphaFoldDB; Q10166; -.
DR   SMR; Q10166; -.
DR   BioGRID; 279126; 17.
DR   STRING; 4896.SPAC26A3.11.1; -.
DR   iPTMnet; Q10166; -.
DR   MaxQB; Q10166; -.
DR   PaxDb; Q10166; -.
DR   PRIDE; Q10166; -.
DR   EnsemblFungi; SPAC26A3.11.1; SPAC26A3.11.1:pep; SPAC26A3.11.
DR   GeneID; 2542673; -.
DR   KEGG; spo:SPAC26A3.11; -.
DR   PomBase; SPAC26A3.11; -.
DR   VEuPathDB; FungiDB:SPAC26A3.11; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   HOGENOM; CLU_030130_1_0_1; -.
DR   InParanoid; Q10166; -.
DR   OMA; LFDSGYC; -.
DR   PhylomeDB; Q10166; -.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q10166; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0050152; F:omega-amidase activity; ISS:PomBase.
DR   GO; GO:0006528; P:asparagine metabolic process; IBA:GO_Central.
DR   GO; GO:1990748; P:cellular detoxification; ISO:PomBase.
DR   GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; ISO:PomBase.
DR   CDD; cd07572; nit; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR   InterPro; IPR001110; UPF0012_CS.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS01227; UPF0012; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..322
FT                   /note="Hydrolase C26A3.11"
FT                   /id="PRO_0000213254"
FT   DOMAIN          44..290
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        83
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        154
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        195
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   322 AA;  35680 MW;  EA6F39B160C7F49F CRC64;
     MNSKFFGLVQ KGTRSFFPSL NFCYTRNIMS VSASSLVPKD FRAFRIGLVQ LANTKDKSEN
     LQLARLKVLE AAKNGSNVIV LPEIFNSPYG TGYFNQYAEP IEESSPSYQA LSSMAKDTKT
     YLFGGSIPER KDGKLYNTAM VFDPSGKLIA VHRKIHLFDI DIPGGVSFRE SDSLSPGDAM
     TMVDTEYGKF GLGICYDIRF PELAMIAARN GCSVMIYPGA FNLSTGPLHW ELLARARAVD
     NEMFVACCAP ARDMNADYHS WGHSTVVDPF GKVIATTDEK PSIVYADIDP SVMSTARNSV
     PIYTQRRFDV YSEVLPALKK EE
 
 
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