ID A0A1V9G1N3_9BACT Unreviewed; 816 AA.
AC A0A1V9G1N3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:OQP64418.1};
GN ORFNames=A3860_20840 {ECO:0000313|EMBL:OQP64418.1};
OS Niastella vici.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=1703345 {ECO:0000313|EMBL:OQP64418.1, ECO:0000313|Proteomes:UP000192796};
RN [1] {ECO:0000313|EMBL:OQP64418.1, ECO:0000313|Proteomes:UP000192796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ57 {ECO:0000313|EMBL:OQP64418.1,
RC ECO:0000313|Proteomes:UP000192796};
RA Chen L., Wang D., Yang S., Wang G.;
RT "Niastella vici sp. nov., isolated from farmland soil.";
RL Submitted (MAR-2016) 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:OQP64418.1}.
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DR EMBL; LVYD01000042; OQP64418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9G1N3; -.
DR STRING; 1703345.A3860_20840; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000192796; 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; 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; 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 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 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OQP64418.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192796};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..816
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012483939"
FT DOMAIN 65..193
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 195..300
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 306..518
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 645..706
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
SQ SEQUENCE 816 AA; 92019 MW; 6E194028330F7DDA CRC64;
MQKLRWLFLL TLVYGQLHAQ QTTRLTGNWE FLKQDAGGIW EVVRPVGKGN PESVPLWQNV
QLPHCVNAED AVDPDVNYYQ GPAWYRTQLE INNPYSNGRT LLFFEGAGQK TDVYVYTTKV
GSHTGGYDEF TVDITDAVAA FKKLPVYQSQ FKGKIPVSIK TDNTRDLELI PSGLSDFNVY
GGIYRYLNLV YLPPVAIDKL FAKAETDKTG KVGTVQVTAR FYPVSGMNAP VSIKLFDANG
KVVQQKEVTP AALTGDVHLT DFTVKTPQLW SPQSPVLYTV EATVTTAEGT FVQKEKIGFR
NFEFVDHGPF LLNSQRLLLR GTHRHEDHAG VGAAMTEDMM RREMIMMKEM GVNFIRLGHY
QQSRIILNLC DSLGILVWEE IPWCRGGLGG PVYQGQARRM LTNMIEQHYN HPAVIIWGMG
NENDWPGDQP EFDKEKIRNF MRELNTLSHQ LDPSRKTAIR RCDFCKDIVD VYSPSIWAGW
YRGVFTEYKQ VTEEEFKKVN HFLHVEWGGD SHAGRHAENP DKALQVVKTG NGADERAGDA
SLFGGAARVS KDGDWSETYL CNLVDWHLKE QETMPWLTGS AQWPFKDFST PVRPDNPVPY
MNQKGVVERD LTKKEAYYVF QSYWTTKPMA HIYGHTWPVR WGNEGEEKMI KVYSNCAEAE
LFVNGKSYGV KKRNSQDFPA AGLRWNVPLS AGMQQVKVIA KNGKTVLSDS ISFTYQTSKW
SKPAKLLLEK IGEENGIATM QVKLLDEKGV PCLDAANWIR FGLAGDGKLI DNQGTPSGSR
YVQAYNGRAI IRVQTNGGHS VISAQREGLT TVFKDI
//
