YFZB_SCHPO
ID YFZB_SCHPO Reviewed; 995 AA.
AC Q9URX4; Q9US31; Q9UTV8;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Uncharacterized family 31 glucosidase C1039.11c;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN ORFNames=SPAC1039.11c, SPAC922.02c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-100, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
CC -!- SUBCELLULAR LOCATION: Spore wall {ECO:0000269|PubMed:10759889}.
CC Note=Spore rim.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB63547.1; -; Genomic_DNA.
DR EMBL; AB027968; BAA87272.1; -; Genomic_DNA.
DR PIR; T50061; T50061.
DR PIR; T50267; T50267.
DR RefSeq; XP_001713119.1; XM_001713067.2.
DR AlphaFoldDB; Q9URX4; -.
DR SMR; Q9URX4; -.
DR STRING; 4896.SPAC1039.11c.1; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR PaxDb; Q9URX4; -.
DR EnsemblFungi; SPAC1039.11c.1; SPAC1039.11c.1:pep; SPAC1039.11c.
DR PomBase; SPAC1039.11c; -.
DR VEuPathDB; FungiDB:SPAC1039.11c; -.
DR eggNOG; KOG1065; Eukaryota.
DR HOGENOM; CLU_000631_11_0_1; -.
DR InParanoid; Q9URX4; -.
DR OMA; FGVETCG; -.
DR PhylomeDB; Q9URX4; -.
DR Reactome; R-SPO-189085; Digestion of dietary carbohydrate.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-70221; Glycogen breakdown (glycogenolysis).
DR PRO; PR:Q9URX4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0031160; C:spore wall; IEA:UniProtKB-SubCell.
DR GO; GO:0090599; F:alpha-glucosidase activity; ISM:PomBase.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0016052; P:carbohydrate catabolic process; IC:PomBase.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR Pfam; PF16863; NtCtMGAM_N; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..995
FT /note="Uncharacterized family 31 glucosidase C1039.11c"
FT /id="PRO_0000018588"
FT ACT_SITE 502
FT /evidence="ECO:0000250"
FT ACT_SITE 669
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 995 AA; 112714 MW; 1EC1D292DC30DBA8 CRC64;
MFIHRMKSNL ASLFLSFFLL LACEFTFSYA DFSTTTSDAT HPSATATEDI FSTPAVPSLG
LAQNPSVYEP YRGDKCGGYN AIQVSEYEKG VLAILQLNGD PCYAYGTDYP FLALNVSFDS
IDRLHVSIQD LYGAQFQFSK RTDVWDAPLY HFQPQFGDRT YNFSFNSQPF EFWVTRVSDG
EVLFDTRGHK LIFEDQYIEL TTNMVDDYNV YGLAETVHGL RLGNNLTRTF WANGNPTPLD
RNAYGTHPFY LEHRYTPSEN LNSDGQPSYT SSTHGVLMLT ANGMEVLLRP NYLQYRIIGG
IVDLYIYVGG TKNPKDTVSQ FVQSVGTPAM QQHWTFGFHI CRWGYKNVFD LVEVKENFKN
FEIPVDTFWS DIDYMYEYRD FTVESNAFPK DKMMEFFNSL QQSNQHYVPI IDAAIYAANP
INRSDDVYYP YYEGVRRDIF LRNPDRSLYV GNVWPGFTTF PDFTNPETTN YWTECLMNLS
AAFGYNSSFP LPYSGLWIDM NEPTSFCIGS CGTDKLDQNP VHPAFILEGE PNNMVYMYPE
GFEHTNASEH ASAYQASVSQ YYATATSTVE SVKATSTPLN VRPKYNINYP PYALNTEQGE
GDLSNLGVSV NATYHDGTVR YNLFNTYGYD QSRVTYDSLT SIEPNVRPFI LSRSTFVGSG
KYAAHWLGDN YSLWSNMIFS IPGALTFNMV GLPMVGADVC GFMGNTDEEL CSRWMALGAF
LPFYRNHNSL GSISQEPYRW ESVAESSRCA MNIRYSLLPY WYTLMYEASS QGLPLIRPLF
FEFPNEPSLA NADRQFMVGS ALLVTPVLEP NVDYVRGVFP GDNSTIWYDW YDHKVIYRQH
NENITLSAPL THINVAIRGG NIIPMQKPSL TTHETKQNPY DLLVALDSDR KACGSLYVDD
GVSIQQESTL FVKFVANGDS LSIESYGDLQ VHEPLSKITI IGLPCAPIGV YFEGVQVESF
SYLEDTKELV LTNLEAFTST GAFSNNWTIS WNLPV
