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Database: UniProt
Entry: A0A0S8HRW5_9BACE
LinkDB: A0A0S8HRW5_9BACE
Original site: A0A0S8HRW5_9BACE 
ID   A0A0S8HRW5_9BACE        Unreviewed;       869 AA.
AC   A0A0S8HRW5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   RecName: Full=PA14 domain-containing protein {ECO:0000259|PROSITE:PS51820};
GN   ORFNames=AMS27_03420 {ECO:0000313|EMBL:KPK87163.1};
OS   Bacteroides sp. SM23_62_1.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1703353 {ECO:0000313|EMBL:KPK87163.1, ECO:0000313|Proteomes:UP000051265};
RN   [1] {ECO:0000313|EMBL:KPK87163.1, ECO:0000313|Proteomes:UP000051265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM23_62_1 {ECO:0000313|EMBL:KPK87163.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK87163.1}.
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DR   EMBL; LJUQ01000019; KPK87163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8HRW5; -.
DR   PATRIC; fig|1703353.3.peg.916; -.
DR   Proteomes; UP000051265; 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   SMART; SM00758; PA14; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          463..602
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   869 AA;  97535 MW;  70210BF922846D42 CRC64;
     MYMKHSILYL VAITFVLINS CNPYAGLPPY QNPTLGFDER VEDLVSRMTL EEKVSQMTNN
     AAAIERLDIP EYDWWNECLH GVARMGKATV FPQAIGLAAT FDQDHMFEVA TTISDEARAK
     YHRFQSQGKR GIYQGLTFWT PNINLFRDPR WGRGMETYGE DPYLTGKMGV AFIKGMQGDD
     DKYLKTVATS KHYIVHSGPE PDRHSFDARI SERDFRDTYL PHFKMTVEEA NVWSIMCAYN
     RYMGEACCGS SRLLMDLLRD ELGFQGYVVS DCGAIRDFYT GHFVADSAAD AAALGVRSGT
     DLNCGSVYPA LVKAVEDRLI TEDEIDVSVR RLMLARMKLG MFDPDEMVPW SGITYDIVDC
     ENHRKLALET ALKSIVLLKN ENNLLPLSKN VGKIAVIGPN SNDVEVLNAN YNGIPTNPVT
     PLEGIIVKVG EENVLYAPGC EHVPGLPVFE EVPSSALFTD QNLTVNGLTG QYYTNKSFEG
     DPVETRVDPQ VDFYWWDSAP FEQLDDDDFS IKWDGYIVPP LSGEYALGGE GMNGFSVFLD
     DSLLVRFRNI HHTSKRYRFV NLKANQPYRI HIDYYEEHGD ASIKLLWSVP GKDLEKEALE
     VAGKADAVIL FMGLSPRLEG EEMGVRLEGF QGGDRTDIQL PKIQQDLIKK IHAMNKPTVL
     VLLSGSALAV NWEQENIDAI IEAWYGGQAA GTAIADVIFG DYNPGGRLPV TFYKSVKDLP
     PFTDYNMAGK TYRYFTKEPL YAFGYGLSYT TFEYSEPVLS KNIITENEPV TVSTQVTNSG
     NMAGEEVVQL YIKDDESSVA RPLRELKGFS RIYFEPGETK TVDFEITHKE LAFYDVGKGE
     YIVEPGSFTI YVGSSSRLQD LKMVMLTVQ
//
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