ID B6JZN4_SCHJY Unreviewed; 1107 AA.
AC B6JZN4;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=glucan 1,4-alpha-glucosidase {ECO:0000256|ARBA:ARBA00012593};
DE EC=3.2.1.3 {ECO:0000256|ARBA:ARBA00012593};
DE AltName: Full=1,4-alpha-D-glucan glucohydrolase {ECO:0000256|ARBA:ARBA00033473};
DE AltName: Full=Glucan 1,4-alpha-glucosidase {ECO:0000256|ARBA:ARBA00033442};
GN Name=meu17 {ECO:0000313|JaponicusDB:SJAG_02076};
GN ORFNames=SJAG_02076 {ECO:0000313|EMBL:EEB07002.2};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB07002.2, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB07002.2, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC successively from non-reducing ends of the chains with release of
CC beta-D-glucose.; EC=3.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001863};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC {ECO:0000256|ARBA:ARBA00006188}.
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DR EMBL; KE651168; EEB07002.2; -; Genomic_DNA.
DR RefSeq; XP_002173295.2; XM_002173259.2.
DR AlphaFoldDB; B6JZN4; -.
DR STRING; 402676.B6JZN4; -.
DR EnsemblFungi; EEB07002; EEB07002; SJAG_02076.
DR GeneID; 7047922; -.
DR JaponicusDB; SJAG_02076; meu17.
DR VEuPathDB; FungiDB:SJAG_02076; -.
DR eggNOG; ENOG502QPM2; Eukaryota.
DR HOGENOM; CLU_282306_0_0_1; -.
DR OMA; DEHKDNC; -.
DR OrthoDB; 1586242at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0005976; P:polysaccharide metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR000165; Glucoamylase.
DR PANTHER; PTHR31616:SF12; GLUCOAMYLASE-RELATED; 1.
DR PANTHER; PTHR31616; TREHALASE; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR PRINTS; PR00736; GLHYDRLASE15.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1107
FT /note="glucan 1,4-alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002847344"
FT DOMAIN 41..437
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT REGION 472..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1107 AA; 130416 MW; DAAFBD6CD95E3330 CRC64;
MKTLAWIGII SWLTGISQAT IVKHDDWSLD NWAEAQKGVA FGHLLDNIGD SGKYAKDVDP
GCIIASPSKE NPNYFYQWVR DSAIVIMNLC DKFLEGDHKL EPIIHKYMDE SIRLQKTPNP
SGDYYNGGLG EPKFNTDGSA FTEQWGRPQN DSPALRAMAF MKYLNYLLEN GASPSEFPHW
IEAVLADLDY TVAHWMNESF DLWEEVQDIH YFTLTVQKAA LENGAHFAKR IGAVDQGVLY
ERVVYSIQLK LGEFWNPKKG WIDAYKNRPE RMGLDCSTLL ASIYSNQFDM QTLPTLLSMQ
QVMSRIYPIN AGYKFAMGRY PEDIYNGIDK TIGNPWFICT STAAHVIYKA VDYYDTYGLP
ELTGANIHFF MHFSEYGDPY NWPVVRKNLL AYADRFLEVV AEFQLPNGSM SEQFSREDGH
QMGARDLSWS YSSLLSTLRA REKVVKKHYP EHKGRKCKLV CEPEGMWDHE HKENWEPEHK
EHCKPEDHKH KEPCKPEHHE HHHEHKEPCK PEHKPEKPCK PEEHCKPEPK KPCKPEEHCK
PVEPCKPEPK KPCKPEEHCK PEPKKPCKPE EPKPKPEKPC KPEDHDHKHK RPCKPGEDEH
KDNCEHKRPC KPGEDEHKDN CQHKHDHKDE HKRPCKPGED EHKDNCEHKR PCKPGEDEHK
NNCQHKPDHK DEHKRPCKPG EDEHKDNCEH KRPCKPGEDE HKNNCQHKPD HKDEHKRPCK
PGEDEHKDNC EHKRPCKPGE DEHKNNCQHK PDHKDEHKRP CKPGEDEHKN NCQHKPDHKD
EHKRPCKPGE DEHKDNCEHK RPCKPGEDEH KNNCQYKHDH DHEPKRPCKP GEDEHKNNCE
FKRPCKPGED ERKNNCQYKH DHDHEPKRPC KPGEDEHKNN CEFKRPCKPG EDERKNNCQH
KPDHKDEHKD EHKPDHKDGH KDEHKPDHKD GHKDEHKRPC KPGEDEHKDN CEFKRPCKPG
EDERKNNCEF KRPCKPGEDE RKNNCEFKRP CKPGEDERKN NCVFKHDHKD EHKHDHKDEH
KDEHKDEHKD EHKRPCKPGE DEHKDNCEFK HDHEHKHDHK DEHKRPCKPG EDEHKDNCKY
KHDHKDEDGH DRMKPKNNDH HEKPEHN
//
