ID A0A1H8DIT7_9SPHN Unreviewed; 890 AA.
AC A0A1H8DIT7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:SEN07085.1};
GN ORFNames=SAMN05192583_1941 {ECO:0000313|EMBL:SEN07085.1};
OS Sphingomonas gellani.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1166340 {ECO:0000313|EMBL:SEN07085.1, ECO:0000313|Proteomes:UP000199206};
RN [1] {ECO:0000313|Proteomes:UP000199206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S6-262 {ECO:0000313|Proteomes:UP000199206};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOCF01000004; SEN07085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8DIT7; -.
DR STRING; 1166340.SAMN05192583_1941; -.
DR OrthoDB; 9781691at2; -.
DR Proteomes; UP000199206; Unassembled WGS sequence.
DR GO; GO:0009044; F:xylan 1,4-beta-xylosidase activity; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1700; Glycoside hydrolase family 3 C-terminal domain; 2.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR044993; BXL.
DR InterPro; IPR026891; Fn3-like.
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; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF07691; PA14; 1.
DR PRINTS; PR00133; GLHYDRLASE3.
DR SMART; SM01217; Fn3_like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR SUPFAM; SSF52279; Beta-D-glucan exohydrolase, C-terminal domain; 1.
DR PROSITE; PS51820; PA14; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000199206};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..890
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011685956"
FT DOMAIN 468..620
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 866..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 94374 MW; B417F493F6CC60AD CRC64;
MGMTTRAAAL ATAGLALAFT PTLARQPSAP ARQQLASDQA VRMAETLVAR MTLDEKLPQL
LNVAPAIPRL GIPAYNWWTE SLHGALGPLA TTNFPEPIGL AASFDAPIVH DVAGAISQEV
RGLHTLGRQT GRNGRIGTGL DTWSPNINIF RDPRWGRGQE TYGEDPFLTA TMGVAFVTGV
QGPDPDRPQV IATPKHFAVH SGPEGTRHAA NVYISAHDLE DTYLPAFRAA LVDGRAGSVM
CAYNRIDGQP ACASDLLLKE HLRGAWGFKG YVVSDCDAVK DIADNHKYAP DSAAAVAAAM
RTGVDNECNG ETLSDTAGLE ARYREALRRD LITEADVDQS LVRLFAARYR TGDLAGLSGA
PAALPTSVVG APEHRRLALA AAERSMVLLK NNGVLPLKPG AKVAVIGPLG DATRVLRGNY
SSPLSGQPVS ILEGLRTAMG ASQVTLVPFG ESVTDGDRVP TSALQTPDGK PGLLARYYNP
TTPLPRQFAP GTREKVVATV TYQKEPVETR IEPDVGDRNL DLARVADVHH TEWTGFLVPP
ETGTYRVGLS GSGGTLTLDG TMISDRRKTR WNDLPGMTTL KLKGGQRYAI RAEGSGIDLV
WKRVSDAPAA DLRRAAAQAD VLVAVVGLTS DLEAEETGVT VPGFSGGDKT TLDLPADQLA
MLDQARATGK PIVLVSMNGS PINLSWAKDN AAAVLEAWYP GETGGTAAAN ILTGRTNPSG
RLPLTFYRSV ADLPPFGDYA VNGRTYRYFT GTPVYPFGYG LSYTSFGYTT PSVAPLRGGA
ENGIRVTTRL TNQGQRLGEE VAQLYLNFPD RPGAPRVALR GFQRVSLRPG ESRTLTFTLS
PRDLSSVAPD GARSVAAGTY RVTVGSGQPG TGVPGQSTSF TARQSAELPK
//
