ID A0A0M8VBG7_9ACTN Unreviewed; 1220 AA.
AC A0A0M8VBG7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Beta-glucosidase {ECO:0000313|EMBL:KOV62581.1};
GN ORFNames=ADL01_29575 {ECO:0000313|EMBL:KOV62581.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV62581.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV62581.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV62581.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOV62581.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGDW01000444; KOV62581.1; -; Genomic_DNA.
DR RefSeq; WP_063783599.1; NZ_LGDW01000444.1.
DR AlphaFoldDB; A0A0M8VBG7; -.
DR PATRIC; fig|1519490.3.peg.6444; -.
DR OrthoDB; 9803863at2; -.
DR Proteomes; UP000037738; 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 CDD; cd00229; SGNH_hydrolase; 1.
DR Gene3D; 2.60.40.1080; -; 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; 2.
DR InterPro; IPR018905; A-galactase_NEW3.
DR InterPro; IPR003343; Big_2.
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; IPR008964; Invasin/intimin_cell_adhesion.
DR PANTHER; PTHR42721:SF3; BETA-D-XYLOSIDASE 5-RELATED; 1.
DR PANTHER; PTHR42721; SUGAR HYDROLASE-RELATED; 1.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF14310; Fn3-like; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR Pfam; PF01915; Glyco_hydro_3_C; 1.
DR Pfam; PF10633; NPCBM_assoc; 1.
DR SMART; SM00635; BID_2; 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; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000037738};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1220
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005825702"
FT DOMAIN 724..797
FT /note="Fibronectin type III-like"
FT /evidence="ECO:0000259|SMART:SM01217"
FT DOMAIN 845..924
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
SQ SEQUENCE 1220 AA; 127271 MW; D69DF8BB90B1C4EF CRC64;
MPRTTTPLST PLLRAAVAAV CSFGLLGAVS GTTHASPGSG VRASPPIYLD TAYSFPERAA
DLVSRMSLDE KVLQLRTNSA PAVPRLGVQQ YTYWSEGQHG INALFANTNP GSVTGGVHAT
SFPTNLAASM SWDKDLMYKE TTAISDEARG LLDKSLWGTG QNNLGPSRDN YGMLTYWAPT
VNLDRDPRWG RTDEAFGEDP YFTGQMAGAF VNGYQGQKAD GTPRSKYLKV AATAKHYALN
NVEQDRTGIS SNVSDDDLFD YYTAQFKSLI EKSHVAGLMT SYNAINGTPS AANTYTTNQI
AQRTYGFGGY ITSDCGAVGT TYQSFPAGHD WAPPGWSTDH KGAKATWTST ATGQKVSGAA
GGQAYALRAG THVNCTGTEA TSPNLEQAIG AGVLSEGVVD NALTHLFTVR MRTGEFDPVS
RQEYTKITKD VIESPAHQAL ARTVADNALV LLQNDKAAGA DRPLLPADPA TLKKVVIVGD
QAGKVTLGGY SGDPTKKVNA VQGITAQVKA ASPDAQVVHD AAGTSSTATG AARLSAETQA
AIKSADLVVV AVGTDDATAG EGKDRAGLAL PGNYGSLIDQ VTALGNPRTV LDIQSDGPVA
IEPYRAKVAS IVFAGYNGES QGDALADVLF GRQNPGGHLN FTWYKDDSQL PALSDYDLTP
GATGGLGRTY QYFTGTPTYP FGYGLSYTTF AYSHVRADRS AVNANGTVTV RFDVTNTGTV
PGTTVAQLYA GTGFTVKDRE LPKKRLVGFQ KTRALQPGAT QHITLRVRVP DLAFHDGRKA
RQVVHAGTYR FEVGPDAATT AGAARVTVHG SLTPHVKYVT VQPEAVVHRA GDTIDLTARN
RWIKDDTDPT AQPGRNLNVT ADHVVEAVND DGSFVDLSKA RVRYASSDPS VATVSRRGLV
TAVGNGVATI RATVHGVTGS AVIRVHHTLA LAAEPIVKPG ALATATTTYT NTGPTALPNA
SVTLDVPEGW RATPTSPATF PSIPAGASVR TTWTVTPPAG VRPGTYALAA SARYRGARAS
DDAAGQLAVP YASLSDITKN TGISDDATPG AANLDGGGQS LSQQALAARG ITSGGTVTHG
GLTYTWPVTG TGKPDNIVAG GQTVPFTGSG TRLGFLGTAD YGNASGTGLI TYTDGTSQRY
TLSFADWWST SPADGTDIVA TTDYININSG SGKVQQKVNV YGATVPLQAG KTVAYLTLPN
VGSDAVSGQV AMHIFATAIG
//
