ID A0A329LGW2_9BACL Unreviewed; 1753 AA.
AC A0A329LGW2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:RAV06470.1};
GN ORFNames=DQG13_01135 {ECO:0000313|EMBL:RAV06470.1};
OS Paenibacillus sp. YN15.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1742774 {ECO:0000313|EMBL:RAV06470.1, ECO:0000313|Proteomes:UP000251619};
RN [1] {ECO:0000313|EMBL:RAV06470.1, ECO:0000313|Proteomes:UP000251619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YN15 {ECO:0000313|EMBL:RAV06470.1,
RC ECO:0000313|Proteomes:UP000251619};
RA Niu L.;
RT "Paenibacillus sp.YN15.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:RAV06470.1}.
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DR EMBL; QMFA01000001; RAV06470.1; -; Genomic_DNA.
DR OrthoDB; 273314at2; -.
DR Proteomes; UP000251619; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate 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 CDD; cd04083; CBM35_Lmo2446-like; 3.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 4.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.40.4270; Listeria-Bacteroides repeat domain; 1.
DR InterPro; IPR044060; Bacterial_rp_domain.
DR InterPro; IPR005102; Carbo-bd_X2.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013378; InlB-like_B-rpt.
DR InterPro; IPR042229; Listeria/Bacterioides_rpt_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR001119; SLH_dom.
DR NCBIfam; TIGR02543; List_Bact_rpt; 1.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF16990; CBM_35; 3.
DR Pfam; PF03442; CBM_X2; 1.
DR Pfam; PF09479; Flg_new; 1.
DR Pfam; PF18998; Flg_new_2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF14200; RicinB_lectin_2; 2.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 4.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS51175; CBM6; 4.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR PROSITE; PS51272; SLH; 3.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000251619};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1753
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016283246"
FT DOMAIN 372..498
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 501..626
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 631..757
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 762..887
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1571..1634
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1635..1698
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1700..1753
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 1402..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1753 AA; 188565 MW; E37C58F04AB3DBF1 CRC64;
MRKKGLFAVS LAVLLAMVLV NVGNMANVAY ADVSSHYLNP LMKGADPTIE RQDDGYYYSA
AGDGNVVLKR HETILGVSTA KSKEVWKRPD NLEFIWGPDV HRIDGKWYIY FASGPKVSDE
AGRFAYGHPS SYVLENSSPD PFEGTWELKG SYDNGDGLTP QEGLLNTQSY GLPLGFVNIK
GQRYMSYTKY FYYTDPVTGN VRFDECPTIV KMKNPWTLEG EEITVARPVY DWEKYVDNVN
EGAAVVERNG KVYFAYSASS YTHDNYAVGL SWADLTQDVE NEAAWNKHPE PIMKRSDENG
SYSTGSPLFL KSEDGTEDWN TYHGIPTHSQ GGKNREVRAQ RINWDDNDFI NLGIPSNPGT
VLSRPSGEEK SEVYEAEDME LSGAARATMN SIYASSGRYA RYSNGSDSDY TEFTINTDVG
GTYSLDFRYN NNTAEPVTMT LGVNQEAPAA LVFPSNAGPE NKLNFDLKTV HNIQLNSGSN
TVRLSGKSAL GLDAIIVKKG VLYEAENAAL SGGAAIAQVN PGYSGTGYAG GLNGPEAAVS
FTVNAPQAGS YSVKLAYGAG TEDDGTLTMY VNGTRIKQAD FFGLKQWDKW ADRYDNVFLK
EGSNVITYKL DSGDTANVNL DYITVTEAAT WTYEAESAKT AGGTDAGIVQ AQDGNTGTGY
VSGLSQVNSS VEFSVDVEYA ASYDLKLRYA TETGGKTLSL EVNGAPVQEV VLPHSGGPKM
WKEQIVTVPL NKGKNSITYK NAAADSGVIH IDHVHLNKRI PWKYQAETAA LTGTPGIGRD
RLWFEGNGYA GLFQKKGDAI RFEVNVPYTA DYTSTLRYSG VQSTNRTMTM YVNGNRIKQV
SLPPTANWDT WTDATETVRL EAGKNSIEFR REDGDTGQLN MDSLTLDKFS GGFMSTAAKE
LNPEKMVKIQ PKHSGKALSV AGEKYNQGAA LIQFSNGETN SQLMRFVDLG TGYYRILIMR
GARFLDIKPG SAIQELILNE TIETAPIPSD TEQWRLEKDG DYYKIINKSN GKVITVNEAS
KSNNALIRLA DDEGKDHQRF KIELRNLYDT AFHAVTDIAD VPAAAQAGQE LTLLGTVSPD
WATRKSITWS IKDAGQTRAS LDGNVLSATR AGTVVVTAVI EEGSGTGASY SKDFTIAVSK
KDADVNPEKA TYDLYVPGDV SASIIWNEAQ SVTGVVYAAT VTGAVYNGTL GPDSYTVNGD
ILTIKRETMA ALGLKSGDTV DFSILFNQGN PAVLSVNVID SFALTSHSIT VATEGPGTAS
ANVSSAVKDT EITLTATPEP GQLFKGWRVD SPSGLNVTGN TFTMPDEAVV ITAVFGAPSY
RVIYNGNGAA SGLVPVDDSS YEQGVTVSVY GNTGNLQKPG YLFAGWNVRA DGSGAGYTEG
QTFTMGGANL TLYAQWTLNN SGGSSGGDSS DGDSSGDSSP STPTGGGVIP ANSSQFTVPA
DKKGEFGIGD EIKLEIPAGA SGKEFQLTIS RVTDTQKLLA GKAAPASPVF EVRKDFPGDF
HKEIMLTIAF DPTQIKQGQK PAVFSYDEAQ KNWRELGGQV NGTASITVKV NSAAKFAVFG
VDQAANPPAP KPAVSLSDLA AHWAESDVKQ AVELGFISGY PDGTFRPDRA VTRAEFAAML
INALKPQGNR PNNEPLTFTD QEKIGVWALN AVAQAVHAGI ISGYEDGSFR PDAEITRSEM
AKMIANALGQ PGEQAATTEF ADDTAIPDWA KGAVAALSKR GIMEGKGENQ FAPGDQATRA
EAVRVLLNML RNR
//
