ID A0A0Q9J0D9_9BACL Unreviewed; 1342 AA.
AC A0A0Q9J0D9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRE22682.1};
GN ORFNames=ASG81_28375 {ECO:0000313|EMBL:KRE22682.1};
OS Paenibacillus sp. Soil522.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE22682.1, ECO:0000313|Proteomes:UP000051180};
RN [1] {ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE22682.1, ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE22682.1,
RC ECO:0000313|Proteomes:UP000051180};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE22682.1}.
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DR EMBL; LMRV01000110; KRE22682.1; -; Genomic_DNA.
DR RefSeq; WP_056642770.1; NZ_LMRV01000110.1.
DR STRING; 1736388.ASG81_28375; -.
DR OrthoDB; 9805821at2; -.
DR Proteomes; UP000051180; Unassembled WGS sequence.
DR GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR026891; Fn3-like.
DR InterPro; IPR026876; Fn3_assoc_repeat.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR42715; BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR42715:SF10; BETA-GLUCOSIDASE F-RELATED; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF13290; CHB_HEX_C_1; 2.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF13287; Fn3_assoc; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF00395; SLH; 2.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM00606; CBD_IV; 1.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
DR PROSITE; PS51272; SLH; 2.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361161};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361161};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1342
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006375512"
FT DOMAIN 40..163
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1219..1282
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1285..1342
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
SQ SEQUENCE 1342 AA; 141447 MW; 46E73FED57A6A0D0 CRC64;
MSRAQKKVLP VLLITALSFS FLAMSPPKVA LAATTATVPG LIEAEYFTTA PSFTSTIGTS
QTASEGLALR RVIAGDQFNY LINAAAAGTY KVVVRYGASV SETESFTLRD STGKVLYTFN
TPATGGVYNW NTMTGYVTLP AGKQTISLYC QKGDYNIDSF QFTPVTTVSA PTASSAPGTY
ASTVNVALAD DIPGAQIYYT TDGSTPAVTS DTNGAYRPGN GLTLLYENPI AVASAATINA
VAVRSGLENG NVAAFTYAID PSAKAAAPVA SKVSGTYGGT QSVTLSSTFS NAKIYYTTDG
TTPATSATGS TKLYSTAISI STGTTLKAIT VADSLNNSDV AEYTYNITTA APTSDITSGV
SIPDGVKASL SSTSAGAKTY YTTDGSDPTV SSTLYTGPIS LTNSIASNKQ ITIKAISITP
NLGTSGISTF TYTIDSSLVK LTGAASIPGV IGSMTLQEKA DLVSGNGVVR IPGAAGASKA
IPRLDIPGTT SVDGPAGVRI SAHPEGWVDS TGNPATRYAT QWPNATARAA TWNTSLEHSL
GTAFGRETHY FGADLLLAPA VNLHRSVLNG RNFEYYSEDP VLSGKMAAAE INGIESQGVG
ATIKHFSSNA QETQRSNGIT NVSQRTLREI ELRSFEIAIR ESQPMALMTA YNHINGVSTA
QNPELLNTVL RDEWGFKGFV MTDWNGQGNA SYWAKQSGNN PYSSNLKAGV DIGMPNGDAS
KIIEGVNSGF LTMAELDKGV KNILEFVVTS LSFKGEPANT EPNPYAEQHE AIAYQEAVES
MILLKNNSVN NKPVLPLTSG NITTIGRAST DMVRGGDGSG GANIDTAKLL QLPQALAAIN
KGGSVIDTSK NGYPQVPSVL PIGGFSTTGA KNEVQISDSQ MDELVQNTGI IIMTIARGSS
EGSDIRKSKG AYYISDAERD LINKASAKAR AAGKPFIVVL NIGSPIEMES WEDKADAILL
AWEPGTVLAK PVAAVLTGAE NPSGKLPTTI PVDVTGKDSK GHLYSPAEDF GQTNGQGGLT
YNEGIYNGYR YYDTFNVPVS YEFGFGKNYS TFDYSNLKLS SPVFKKASDK LNITVNVKNT
SAETGKETVQ IYAGAPGKSM DKPVKELKVF GKTNNLVANA SQTLNFTLDA KSLASYDEAR
NAWVVEPGTY VIYAAASSKD IRQAATFTVP KEIIAETVHD VLKPKVELDL IKPAQTSNVT
RAEFIKLLMQ TLDLANERAV STLKDVKEGD WYYSSIAVAQ KLGIVSGKKD GTFGVNETIS
RQDMAVMMFR AAKRLKVELK GNVAVSSFKD NAHIASYAKE AVSALQKAGI INGMGGGVFM
PNGQATKAQA VVSIDRLVNT VK
//
