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Database: UniProt
Entry: A0A1Y1CDR0_9BACT
LinkDB: A0A1Y1CDR0_9BACT
Original site: A0A1Y1CDR0_9BACT 
ID   A0A1Y1CDR0_9BACT        Unreviewed;       833 AA.
AC   A0A1Y1CDR0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:BAX78488.1};
GN   ORFNames=ALGA_0093 {ECO:0000313|EMBL:BAX78488.1};
OS   Labilibaculum antarcticum.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC   Labilibaculum.
OX   NCBI_TaxID=1717717 {ECO:0000313|EMBL:BAX78488.1, ECO:0000313|Proteomes:UP000218267};
RN   [1] {ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT   from the Antarctic marine sediment.";
RL   Mar. Genomics 0:0-0(2017).
RN   [2] {ECO:0000313|EMBL:BAX78488.1, ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|EMBL:BAX78488.1,
RC   ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT   from the Antarctic marine sediment.";
RL   Mar. Genomics 39:1-2(2018).
RN   [3] {ECO:0000313|Proteomes:UP000218267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Labilibaculum antarcticum sp. nov., a novel facultative anaerobic,
RT   psychrotorelant bacterium isolated from marine sediment of Antarctica.";
RL   Antonie Van Leeuwenhoek 113:349-355(2020).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; AP018042; BAX78488.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1CDR0; -.
DR   KEGG; mbas:ALGA_0093; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000218267; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR048229; GalB-like.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   NCBIfam; NF041463; GalB; 1.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF18565; Glyco_hydro2_C5; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAX78488.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..833
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012530627"
FT   DOMAIN          60..184
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          200..301
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          308..462
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          637..710
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          726..827
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   833 AA;  94307 MW;  36735C29BD6D4AAC CRC64;
     MDNRACKSLI LRSISFSLLI AFLFLSTSCK TTTSLNDEDF NNDWLFLKGN VSDAKQFGFN
     DSEWRKVDLP HDWAIEGPFS IENNARTGGL PVHGTGWYRK HFQISKENSD KIISVEFDGA
     MNNAHVWVNG HFAGNRPYGY IGFEFDITPF IKFGEQNVIA VRLSPKDLSA RWYPGAGIYR
     NVRIKTNYKL HIPQWGTKIT TQNVSKSHAK INFTTSVCNK FKTQQSAELE TSIVNSDGEI
     VSTITSEIIL QANTTGYVDQ LIDIENPKIW DIKHPNLYKS LSKISIQGKI IDSYESEFGV
     RTIKFTTENG FQLNGKTVKL QGVCMHHDLG PLGAAVNYRA TERQMQIMKS MGVNALRTSH
     NPPSPELLQI CDKLGIVVIV EAFDEWKLGK VINGYNKYFD EWHEKDLRDM IKRDRNHPSV
     IMWSIGNEIL EQSRKDGWKI AKELTEICHE EDSTRPTTAG FNYYPAPFTN QLAKYVDIVG
     MNYWPLNYQE ILDANPNMIV YGSETSSQTS SRGVYHFPIE ANEQHQTNQV SSYDGTVGPP
     WAYAPDVEFE QQEKVTRSLG EFMWTGFDYL GEPTPYGGKD NSTNGYWNTD WPSRSSYFAP
     VDLCGFPKDR YYLYQSQWTT KPMVHVLPHW NWEGKEGDTI PVYSYTNCDE VELFVNGKSF
     GKKIKGVDLT PIPAEFHFFP KGMYQSKYRL SWDVPYQAGT LKVVAYKNGK IEAEKTIHTA
     GKAYQIKLIP DRKTISADGK DLSFITVRVE DKDGNLCPKA NDLVKFSIEG KGEIVAVGNG
     DATSTKAYQA KKRNAFNGLC LLIVKSTTIA GEITINAESD QLITNEISIS TKK
//
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