ID   A0A2A3N6T6_CAPSP        Unreviewed;       701 AA.
AC   A0A2A3N6T6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:PBN47443.1};
GN   ORFNames=CDC50_02320 {ECO:0000313|EMBL:PBN47443.1};
OS   Capnocytophaga sputigena.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1019 {ECO:0000313|EMBL:PBN47443.1, ECO:0000313|Proteomes:UP000218560};
RN   [1] {ECO:0000313|EMBL:PBN47443.1, ECO:0000313|Proteomes:UP000218560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H6490 {ECO:0000313|EMBL:PBN47443.1,
RC   ECO:0000313|Proteomes:UP000218560};
RA   Gulvik C.A.;
RT   "Capnocytophaga spp. assemblies.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PBN47443.1}.
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DR   EMBL; NIBW01000001; PBN47443.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3N6T6; -.
DR   Proteomes; UP000218560; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR029483; GH97_C.
DR   InterPro; IPR019563; GH97_catalytic.
DR   InterPro; IPR029486; GH97_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR35803:SF1; GLUCAN 1,4-ALPHA-GLUCOSIDASE SUSB; 1.
DR   PANTHER; PTHR35803; GLUCAN 1,4-ALPHA-GLUCOSIDASE SUSB-RELATED; 1.
DR   Pfam; PF14509; GH97_C; 1.
DR   Pfam; PF14508; GH97_N; 1.
DR   Pfam; PF10566; Glyco_hydro_97; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..701
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012110370"
FT   DOMAIN          22..287
FT                   /note="Glycosyl-hydrolase 97 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14508"
FT   DOMAIN          292..595
FT                   /note="Glycosyl-hydrolase 97 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF10566"
FT   DOMAIN          597..698
FT                   /note="Glycosyl-hydrolase 97 C-terminal oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14509"
SQ   SEQUENCE   701 AA;  80207 MW;  16D278A190438968 CRC64;
     MRKIILLMSV FAAHFVMAQQ QTSPDGNVIL SFSLKNDGTP SYKVSYKNKP VINESTLGFT
     LKKADPLTNN FKVVDTKKST FKETWKPVWG EESEILNHYN ELLVSLEQNN TKRKMNIRFR
     VYNEGVGFRY EFPSQKELTY FVVEEELSQF AMTGDHTAWW IPGDYDTQEY DYMESKLSEI
     RGLMKEAVTE NVSQFAFSPT GVQTSLMMKT KDGLYINLHE AALVDYSLMN LNLDDKTFVF
     QSWLTPDAKG DKGYLMAPCH SPWRTIMVSD DARKILASRL ILNLNEPCAI ADTSWIKPVK
     YVGVWWEMIT GKSSWSYTND LPTIDLNTVD YTKTKPNGTH GATNENVRKY IDFAAKHGFD
     QVLVEGWNVG WEDWFGHKKD YVFDFVTPYP DFDLKALNEY AHSKGVKLMM HHETSGSTRN
     YERHMKAAYE LMNKYGYNSV KSGYVGDILP VGEHHYSQST INHYLYAIKE AAKHKIMVNA
     HEAVRPTGIC RTYPNMIGNE SARGTEYEAF GGNKVFHTTI LPFTRLQGGP MDYTPGIFET
     EMKYVNPNNN NQIRTTLARQ LALYVTMYSP LQMAADLPEN YEKYADAFQF IKDVPVDWQK
     SVYLEAEPGR YITIARKDKH SNDWYVGCTA HEGGHTSELL LNFLDKGKKY EATIYVDAKD
     ANWKTNPKAY TITKQKVNAK TKLKLTAAQG GGYAISIKEI K
//