ID A0A372ISI7_9BACT Unreviewed; 758 AA.
AC A0A372ISI7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:RFU17864.1};
GN ORFNames=D0Y96_07090 {ECO:0000313|EMBL:RFU17864.1};
OS Paracidobacterium acidisoli.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Paracidobacterium.
OX NCBI_TaxID=2303751 {ECO:0000313|EMBL:RFU17864.1, ECO:0000313|Proteomes:UP000264702};
RN [1] {ECO:0000313|EMBL:RFU17864.1, ECO:0000313|Proteomes:UP000264702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G-K13 {ECO:0000313|EMBL:RFU17864.1,
RC ECO:0000313|Proteomes:UP000264702};
RA Gao Z.-H., Qiu L.-H.;
RT "Acidipila sp. 4G-K13, an acidobacterium isolated from forest soil.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family.
CC {ECO:0000256|ARBA:ARBA00005336, ECO:0000256|RuleBase:RU361161}.
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:RFU17864.1}.
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DR EMBL; QVQT01000002; RFU17864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372ISI7; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000264702; 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; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 1.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR019800; Glyco_hydro_3_AS.
DR InterPro; IPR002772; Glyco_hydro_3_C.
DR InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Reference proteome {ECO:0000313|Proteomes:UP000264702};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..758
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017026745"
FT DOMAIN 676..745
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
SQ SEQUENCE 758 AA; 81198 MW; 357BD14187E8A4CC CRC64;
MRLRRSILTA FCPLAAAGLL SLPAATAQSP AQTASTAAAD RPWMNTSLTP DQRADLVIKA
MTLDEKLDLV HGTGWGALKD GSPIAEGSNE GAGYVQGIPR LGIPGINMAD SAVGVRLAAR
ESRYATLLPS VLGAASSWDP EAAHLYGSVI GRELRDQGYN MSIGGGVDIT REPRNGRNFE
YAGEDPVLAG TMVGNVEKGV LDEKVMNDIK HYALNDQETG RTIVNAVLGK RAMRESDLLA
FQIAIGIATP SAVMCSYNRV NGDYSCENDY LLNQVLKKDW DFKGFVVSDW MGTHSTVKAA
LAGLDNEEPG PNHPDDQEHD DNDAWFAAPL KAAVQNGQVP MSRLEDMDHR VLRSMFAAGV
IDHPPFPRRV VDPFRGRDDA ERIANESIVL LKNAEHLLPL DGGVKSIALI GSHADVGVLS
GGGSAQVDAP GGNAADPQPG TMKWGEAVYF PSSPLKEIRR QAPHAAVEFN AGTDVAAAAA
LAKQSQVAIV FVNQPMIEGK DAKTLSLPDD QDALVEAVTA ANPHTIVVLE TGGPVTMPWA
DRVAGIVEAW YPGIGGAQSL ANLLFGQVNP SGKLPVTFAK SDDQLPHPEV PGIGLKEKAV
PGNPDHKELP RFDADYNTEG ARVGYKWYES EHRTPLFPFG YGLSYTTYAY SNLKANAQER
SVSFEVKNTG SVAGTEIAEV YAELPAKADE PFKRLVAWQR VALDPGESKT VTLKVDPLYL
SIFNTDKNSF ELLPGEYRIL AGPSSAEPPL HATMTVAE
//
