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YEO3_SCHPO
ID   YEO3_SCHPO              Reviewed;         635 AA.
AC   O13781;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Uncharacterized protein C17G6.03;
GN   ORFNames=SPAC17G6.03;
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16214.1; -; Genomic_DNA.
DR   PIR; T37835; T37835.
DR   RefSeq; NP_594250.1; NM_001019673.2.
DR   AlphaFoldDB; O13781; -.
DR   SMR; O13781; -.
DR   BioGRID; 278757; 11.
DR   STRING; 4896.SPAC17G6.03.1; -.
DR   PaxDb; O13781; -.
DR   EnsemblFungi; SPAC17G6.03.1; SPAC17G6.03.1:pep; SPAC17G6.03.
DR   GeneID; 2542289; -.
DR   KEGG; spo:SPAC17G6.03; -.
DR   PomBase; SPAC17G6.03; -.
DR   VEuPathDB; FungiDB:SPAC17G6.03; -.
DR   eggNOG; KOG4419; Eukaryota.
DR   HOGENOM; CLU_019028_0_0_1; -.
DR   InParanoid; O13781; -.
DR   OMA; NEIMGLY; -.
DR   PhylomeDB; O13781; -.
DR   PRO; PR:O13781; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0008253; F:5'-nucleotidase activity; ISO:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046085; P:adenosine metabolic process; ISO:PomBase.
DR   GO; GO:0034655; P:nucleobase-containing compound catabolic process; IC:PomBase.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   CDD; cd07407; MPP_YHR202W_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; -; 1.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR014485; Pesterase_C1039.
DR   InterPro; IPR041823; YHR202W_N.
DR   PANTHER; PTHR11575; PTHR11575; 1.
DR   PANTHER; PTHR11575:SF22; PTHR11575:SF22; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF017316; Pesterase_C1039; 1.
DR   SUPFAM; SSF55816; SSF55816; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..635
FT                   /note="Uncharacterized protein C17G6.03"
FT                   /id="PRO_0000310953"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            126
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   635 AA;  71442 MW;  DF9517858D8EA9A0 CRC64;
     MKPAHTFSLI FSLLFVINPC YSATLPLAIR RELTWGQVNI LHTTDIHGWL AGHARDKRYS
     GDLGDFASFV QHMKHLAKQK DVDLLLVDTG DLHDGTGLSD LTDPPGSWTD SLLANMDYDI
     LVAGNHELYL STVANDTYHN FIPLWEGRYL AANIDIYDEH VSSFVPFGDR YAIFSTPHNV
     KILAFGFVNS FSGATDTVRV LPVSQFSLQP WWNDMVSNKD IDLILIPAHV PVHNASELDI
     VLSELRIHFP TTPIQVLGGH SHIRDYAIYD EKAVGIESGR YCETVGWVSI NGIPSFKSLV
     KLSGISSLMG VESYLAERLR FIGESIRRSS QQIFSSLQSA KSASVSFSRS YIDWNPEGFM
     FHSKTKKSSF NTSLGEFISN GIYEARKALG LLTPIGCSPK KFAFSEVPFN DSNSIYHLFQ
     SELFPKIVVN ESRHHIPHYI IVNSGGIRGG LNSGAFGLDE VFQVCPFKSN IFYVLKDVPW
     SITKYLPQAL QHSGYLIAED TLQINTPQVS DAKFEDFYEH SIRKTYGYTT HDDLGDDGDD
     TAHLTTPHYE PLRFICSQVG FDDSFSGDDK QVVDVVAPSF VIPRLDDILN KIADKPLYSP
     DDWELYFTRP DGKHSMTDLL PLYADLYWDH DCLYK
 
 
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