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YEI1_SCHPO
ID   YEI1_SCHPO              Reviewed;         491 AA.
AC   O13996;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Uncharacterized glycosyl hydrolase C27E2.01;
DE            EC=3.2.1.-;
GN   ORFNames=SPAC27E2.01;
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=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB11675.1; -; Genomic_DNA.
DR   PIR; T38448; T38448.
DR   RefSeq; NP_594401.1; NM_001019832.2.
DR   AlphaFoldDB; O13996; -.
DR   SMR; O13996; -.
DR   BioGRID; 279134; 3.
DR   STRING; 4896.SPAC27E2.01.1; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   MaxQB; O13996; -.
DR   PaxDb; O13996; -.
DR   EnsemblFungi; SPAC27E2.01.1; SPAC27E2.01.1:pep; SPAC27E2.01.
DR   GeneID; 2542681; -.
DR   KEGG; spo:SPAC27E2.01; -.
DR   PomBase; SPAC27E2.01; -.
DR   VEuPathDB; FungiDB:SPAC27E2.01; -.
DR   eggNOG; KOG0471; Eukaryota.
DR   HOGENOM; CLU_006462_7_2_1; -.
DR   InParanoid; O13996; -.
DR   OMA; YSINSHF; -.
DR   PhylomeDB; O13996; -.
DR   PRO; PR:O13996; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0009986; C:cell surface; IC:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004556; F:alpha-amylase activity; ISM:PomBase.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IC:PomBase.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR013777; A-amylase-like.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW   Metal-binding; Nucleus; Reference proteome.
FT   CHAIN           1..491
FT                   /note="Uncharacterized glycosyl hydrolase C27E2.01"
FT                   /id="PRO_0000310320"
FT   ACT_SITE        221
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        245
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         224..225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         225
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            313
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   491 AA;  56679 MW;  2013808DC0EE581D CRC64;
     MSLDKQIPII YDFGENYEKN KDIWRRQCIY QILTDRFALD DHCTTAPSTG RMYLGGTWRG
     IIQKLDYIQS LGCTAVWISP IVKNIEGVTG YGEAYHGYWA EDLTQLNPHF GTKQDLTELV
     DQLHKRNMLC MIDIVVNHMA HAGDSPIDYS KYAPFNSPSH YHPKRFLHNY DDTWDCEIAW
     LGDEVVSLMD IRTEDQEVHN FFQNWIRDLI QTYHFDGLRI DTAKHVQKEF YPPFIAAANV
     FAFGEVYHGD PKFIAKYLEY IPSAANYPLY YQIENTFFPP KQSMNIFYQK AILEARATSM
     DTTILGNFTE NHDVPRFLNR STDYSLLCNT LTLLLFTDGI PIIFQGQEQM YAGGHDPENR
     DALWTSNYNQ QNPIFQFLKK LIKLRQFLVD NVSGFTTELS NMLFVNEHVY VFRRPGVIIV
     VSNAGSNSDV DTSAEFSITE RESLEFIDVL SGSQFSSLPT EDSSTISMNL EFSFPRVLVH
     RGLFHSMNEL A
 
 
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