ID G0SFN2_CHATD Unreviewed; 604 AA.
AC G0SFN2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Glucosidase-like protein {ECO:0000313|EMBL:EGS17797.1};
GN ORFNames=CTHT_0071460 {ECO:0000313|EMBL:EGS17797.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS17797.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; GL988047; EGS17797.1; -; Genomic_DNA.
DR RefSeq; XP_006697415.1; XM_006697352.1.
DR AlphaFoldDB; G0SFN2; -.
DR STRING; 759272.G0SFN2; -.
DR GeneID; 18261184; -.
DR KEGG; cthr:CTHT_0071460; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_1_1_1; -.
DR OMA; MNNHDVP; -.
DR OrthoDB; 3680211at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF222; MALTASE MALT (AFU_ORTHOLOGUE AFUA_8G07070); 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Maltose metabolism {ECO:0000256|ARBA:ARBA00026248};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066}.
FT DOMAIN 17..443
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 604 AA; 70057 MW; 5DF80DB5144C7445 CRC64;
MPSAPETPWW KDAVCYQIYP ASFKDSNGDG LGDIPGILSK LDYLKDLGVD LIWVSPMYVF
TQVTFPGVDM GYDISDYQKV YPPYGTLKDM EDLIEGCHKR GMKLILDLVV NHTSDQHAWF
KESGSSRDSS KRDWYIWKPP RYAEDGTRLP PTNWRSYFSG PAWEYDEQTG EYYLHLFAKE
MPDLNWENPE VRKAIYDTIM RFWLDKGVDG FRIDCVNMYS KEPDYKDAPI VDPKFYEQPA
WCYYANGPRI HEFLREMHEQ VLSHYDPVTV GELPHTRDPQ EVLRYVRASE KQLSMVFQFD
IVDIGQGKEY RYYYQDWKLP EFKGIVAKWQ QFIEGTDGWT TVFCENHDQG RSVSRFASDA
PEHRVASAKL LALMLTSLTG TLFLYQGQEI GMINIPHTWP ITSYKDIESV NFYHAVAAKT
NNDPAELAYV MRSLQILGRD NARLPMQWDT GVHAGFTDCE KGPWMRVHDA WREINVAKQL
AQGETSVLGF WKQMIRFRKQ HRDVLVHGSF EGFGMDDEKT FVFGKKTQDG KKVAMVALNF
SGEEQEVQLP DTPGYDELVF TVGSYEDAED METTKSIRYY QNLTTRLLTQ ARALGIIWQL
QMSE
//
