ID A0A261Q9S1_9BACT Unreviewed; 1147 AA.
AC A0A261Q9S1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Glycoside hydrolase family 2 {ECO:0000313|EMBL:OZI09539.1};
GN ORFNames=BWI93_03480 {ECO:0000313|EMBL:OZI09539.1};
OS Siphonobacter sp. BAB-5385.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Siphonobacter.
OX NCBI_TaxID=1864822 {ECO:0000313|EMBL:OZI09539.1, ECO:0000313|Proteomes:UP000215802};
RN [1] {ECO:0000313|EMBL:OZI09539.1, ECO:0000313|Proteomes:UP000215802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-5385 {ECO:0000313|EMBL:OZI09539.1,
RC ECO:0000313|Proteomes:UP000215802};
RA Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT "Draft genome of Siphonobacter sp. BAB-5385.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:OZI09539.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NMPS01000038; OZI09539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261Q9S1; -.
DR OrthoDB; 857501at2; -.
DR Proteomes; UP000215802; Unassembled WGS sequence.
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; 2.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006101; Glyco_hydro_2.
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; IPR021720; Malectin_dom.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 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 Pfam; PF11721; Malectin; 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; 2.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OZI09539.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215802}.
FT DOMAIN 25..187
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 200..305
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 317..451
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 617..678
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 711..875
FT /note="Malectin"
FT /evidence="ECO:0000259|Pfam:PF11721"
SQ SEQUENCE 1147 AA; 129396 MW; 69353B06D7C74239 CRC64;
MHSKLILLSL FLTFTAWGQS RKEISLQANW QSTATDDTTA HPDFYRSEFK PQSWKTVQVP
HNWDQYGGYR RKVNGNRYGV AWYRKTFTVQ ETAAGKRFFL FFEGVGSYAT LWLNGKKIGY
HAGGRTSFTL DITDVIRLNN QTNLLAVRAD HPDQIQDLPW VSGGSSSERG FSEGSQPMGI
FRPVQLIVTR DVRIEPFGVH VWNDTSVSAT AAKLHVTSEI KNYGTRPRTL TVVQQLLDRS
GKTVTKVEQK LNLKAGETVT LASPDLSVSR PQLWSPEQPY LYRLVTQVLE QGQRMDQLTT
PYGIRRVSWD LSPNAKTRLR INGQPVFING VAEYEHLLGN SHAFSEEQIH TRVRQVKAVG
FNAFRDAHQP HNLRYHLYWD EAGILWWPQM AAHIWYDTPA FRQNFKRLLI DWVKERRNSP
SIILWGLENE STLPEDFARE CSELIRQLDP TASSQRKITT CNGGKGTDWD VPQNWTGTYG
GDPQQYGEDL KRQILVGEYG AWRTIDQHTE GRGVFSENRM TDLMETKIRL AESVRDRTAG
HFFWLLNSHD NPGRVQGGEG LRELDRIGPV NYKGLFTAWE EPTDAFYLFR SNYAPKETEP
MVYIVSHTWP NRWTTPGRKD SLIVYSNCDA VELFNDVNHR SLGRKTRQGV GTHFQWDGAD
IQTNTLYAVG YVKGKAVATD VVVLNHLPEA PHLSEVTGKV TAASTSGLRY LYRVNCGGPT
YTDVQKKVWY ADQRKTETNA WGSTSWTEHY PGMPAFFASQ RRTFDPIRGT SDPKLFQTFR
YGRDQLAYHF NVPDGDYQVE LYFIEPWYGT GGGLDATGWR LFDVAINDEV RLKNLDIWKE
VGHDALLKKT LRVRVRGGQL KVSFPHVPSA QAVISAIAIA ALDTKSVITQ QSSSILKSTQ
GSVESWLDTG DGLFADETTR AVSLPSHLYG ATWLKRKRNE AATVQVTEAA DVFLAVPASA
LPPSGFEATD TFLTTDEPRQ YSLVRKRMQA NEKLMAAAGS WLAALPVYTL EPAYDLKAAT
SYKATQAQPI GQGVGKEVFL DKERMVFKKA SGDTLEWILA VGVADTYSLT LKYHNPAQKA
LKVSVELILK DGTVVKPAET LELEPSKPGK WTYATTNTGT MINAGTYTLR LKTLDADRLY
LDTLDVQ
//
