ID A0A2T6FN76_9GAMM Unreviewed; 498 AA.
AC A0A2T6FN76;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Beta-glucanase {ECO:0008006|Google:ProtNLM};
GN ORFNames=B0W54_05050 {ECO:0000313|EMBL:PUA29912.1};
OS Cellvibrio sp. 79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1954207 {ECO:0000313|EMBL:PUA29912.1, ECO:0000313|Proteomes:UP000243979};
RN [1] {ECO:0000313|EMBL:PUA29912.1, ECO:0000313|Proteomes:UP000243979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=79 {ECO:0000313|EMBL:PUA29912.1};
RA Zhang Y., Xu J., Wang N.;
RT "Cellvibrio sp. 79 recovered from metagenome.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC {ECO:0000256|ARBA:ARBA00006865}.
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:PUA29912.1}.
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DR EMBL; MVDH01000001; PUA29912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6FN76; -.
DR Proteomes; UP000243979; Unassembled WGS sequence.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.30.32.30; CBM10; 1.
DR InterPro; IPR008264; Beta_glucanase.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR036601; CBM10_sf.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR018366; CBM2_CS.
DR InterPro; IPR009031; CBM_fam10.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR PANTHER; PTHR10963:SF22; GLYCOSIDASE CRH2-RELATED; 1.
DR PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR Pfam; PF02013; CBM_10; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PRINTS; PR00737; GLHYDRLASE16.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM01064; CBM_10; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57615; Type X cellulose binding domain, CBDX; 1.
DR PROSITE; PS51763; CBM10; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00561; CBM2_A; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000243979};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..498
FT /note="Beta-glucanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015558095"
FT DOMAIN 1..195
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT DOMAIN 310..339
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 389..498
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 256..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 498 AA; 53240 MW; 8558048AD5857875 CRC64;
MFNKRSIYLL ITTLCIAMLN AGFAAAKPYK GAEIYSAEAT KYGRYVMRMR MAEGSGLLST
FFTYKNGSEV SGAVWEEIDI EVLGKNDAYQ MQSNIIVGAP RQTTEGLHTA SQSLADDYHT
YALEWTPDYV AWFIDGQQVR RINGSNFVTG LVNPQSMRFN IWASTSESWV GAFNPSILPV
YQFVNYMEYY AYNTNSKTFT LSWRDDFNNF DTNRWSKADW TFDGNYVDFD PANVVIQNGT
LILALTTENA KGFSGTVPVD GNASSRSSSS VISSSRSSSS TGTSASAATS KSSVINSSVA
SSNPNTTGGQ CNWYGTLYPL CVNTSNGWGY ENNRSCISRS TCVSQPAPFG IIGATSSAAS
SSPVSSSPAS SSIQSSIIPS SSSRSSISST ASSTVSSVNT SGLNCTAKVV NNWGSGYQLD
VVINNGRTTT VTGWNVTLTF SENPQRTGGW NATIGGSGNV VMASNVNWNA TIAPGQSVSF
GLQGNHDGSF VAPACKVN
//
