ID A0A1C2GN41_9SPHI Unreviewed; 867 AA.
AC A0A1C2GN41;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:OCX53000.1};
GN ORFNames=BEL04_01395 {ECO:0000313|EMBL:OCX53000.1};
OS Mucilaginibacter sp. PPCGB 2223.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1886027 {ECO:0000313|EMBL:OCX53000.1, ECO:0000313|Proteomes:UP000095113};
RN [1] {ECO:0000313|EMBL:OCX53000.1, ECO:0000313|Proteomes:UP000095113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PPCGB 2223 {ECO:0000313|EMBL:OCX53000.1,
RC ECO:0000313|Proteomes:UP000095113};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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:OCX53000.1}.
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DR EMBL; MDJS01000001; OCX53000.1; -; Genomic_DNA.
DR RefSeq; WP_065999380.1; NZ_MDJS01000001.1.
DR AlphaFoldDB; A0A1C2GN41; -.
DR STRING; 1886027.BEL04_01395; -.
DR OrthoDB; 9758670at2; -.
DR Proteomes; UP000095113; 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 NCBIfam; NF041776; xylosidase_Xyl3A; 1.
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, ECO:0000313|EMBL:OCX53000.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095113};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..867
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008662291"
FT DOMAIN 459..601
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
SQ SEQUENCE 867 AA; 95945 MW; 8E18778C3A4F8172 CRC64;
MNFKQKIIAP LLVLCQLGLH AQQVLLPYQN PKLSSEVRAK DLVKRLTLKE KVGLMKDVSD
PVPRLGIKKF NWWSEALHGY ANQGPVTVFP EPIGMAASFD DQTLFHVFDA VSDEARAKNN
DYRKKGESQR FHDLSVWTPN VNIFRDPRWG RGQETYGEDP YLTSRMGISV VKGLQGPADS
KYRKLLACAK HYAVHSGPEW SRHQMNVTDV SARDLMETYL PAFKSLVTEA DVREVMCAYQ
RLDDEPCCGN SRLLGQILRD DWKFKYLVVS DCGAITDFYR SHHSSSDATH ASAKAVLSGT
DVECAGYAYD EIPKAVAKGL IKEKDINTSV IRLLTQRFEL GEMDKDDLVP WTKIPLSVVN
SPQHQQLALD MARETITLLQ NKNNTLPLNK SLPKIAVIGP NANDNQMLWG NYNGTPAKTV
NILEGIKSKI ADSQLIYDKA CDLTEDKVVE TEIAQTSIYG KTGLKATYWS NRTMTGDPVI
VEQITSPIAL TTMGAHQFAQ GVPTENFSAK YETVYKPTFS GEIAFKLEAT GGAEVKVNGQ
SVLRSGGWRA LPAKANYQVE AGKTYNIEVD YRQVNNWAAS LGFNFGKEFP IAYDQLLAKV
KDADVVIFVG GISPKLEGEE MPVQLPGFKG GDRTDIELPA VQRECMAALK KAGKKVVFVN
CSGSAIALVP ETSNCDAIVQ AWYPGEFGGQ AVADVLFGDY NPAGHLPVTF YKNTQQLPDF
SDYNLKGRTY RFMTDAPLFP FGFGLSYTTF EIGKATLNKT TIAPNEAIQF SVPVANTGKI
DGTEILQLYV RKVNDPDGPV KTLRAFKRLP VAAGKSTTAS ISLEPKMFEF YNADNYRVQV
SPGEYELFYG TSSADSDLKS VKITIHS
//