ID   A0A0Q5K3Q0_9MICO        Unreviewed;      1365 AA.
AC   A0A0Q5K3Q0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=BIG2 domain-containing protein {ECO:0000259|SMART:SM00635};
GN   ORFNames=ASF76_10060 {ECO:0000313|EMBL:KQR23505.1};
OS   Microbacterium sp. Leaf151.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736276 {ECO:0000313|EMBL:KQR23505.1, ECO:0000313|Proteomes:UP000051582};
RN   [1] {ECO:0000313|EMBL:KQR23505.1, ECO:0000313|Proteomes:UP000051582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf151 {ECO:0000313|EMBL:KQR23505.1,
RC   ECO:0000313|Proteomes:UP000051582};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR23505.1, ECO:0000313|Proteomes:UP000051582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf151 {ECO:0000313|EMBL:KQR23505.1,
RC   ECO:0000313|Proteomes:UP000051582};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQR23505.1}.
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DR   EMBL; LMOR01000003; KQR23505.1; -; Genomic_DNA.
DR   STRING; 1736276.ASF76_10060; -.
DR   Proteomes; UP000051582; Unassembled WGS sequence.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.40.1080; -; 1.
DR   Gene3D; 1.20.1270.90; AF1782-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.70.98.50; putative glycoside hydrolase family protein from bacillus halodurans; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR049053; AFCA-like_C.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR027414; GH95_N_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   PANTHER; PTHR31084; ALPHA-L-FUCOSIDASE 2; 1.
DR   PANTHER; PTHR31084:SF19; GLYCOSYL HYDROLASE FAMILY 95 N-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02368; Big_2; 1.
DR   Pfam; PF14498; Glyco_hyd_65N_2; 1.
DR   Pfam; PF21307; Glyco_hydro_95_C; 1.
DR   SMART; SM00635; BID_2; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1365
FT                   /note="BIG2 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039311226"
FT   DOMAIN          1074..1155
FT                   /note="BIG2"
FT                   /evidence="ECO:0000259|SMART:SM00635"
SQ   SEQUENCE   1365 AA;  145199 MW;  19BF030A99BCFA3A CRC64;
     MLTAAVAAAL VAPLGFVSAG DQAHAETVPA AEYGPRLWYD EPASAGAREN FPGESFPSTT
     ENQIWQQRTL PIGNGNIGAT VYGEIGKEHL VFNEKTLWTG GPSSSRPDYV GGNLEDKGRN
     GEALREVQRL FANGQTAEAQ SLAQSALVGG ENGYGAYESY GDLWLDYGFD GSGVSNYQRS
     LDLETATASV AFDRGGVRYT RDFFTSYPDN VMVVRLTASQ AGALDIDVAF DFALGGASTV
     VSGDTLTVSG ALADNQLKHN AIVKAVPSGG TVSANGTQMR IRDADEVLLY VTASTDYEDV
     YPNYRTGQSD ADVASEVRTR VDLAAADGYS TVRDRHLADY RELYSRVDLT LGGQLSTDAT
     DDLLAKYRNS TATDVEKRTL EVVLYQYGRY LGIESSREGT LPSNLQGIWA DRNTGNSGSP
     VPWGSDYHMN VNLQMNYWPA YSGNLAETAT PLVDYVEGLR EPGRVTAEIY GGVASTPDNP
     ENGFTAHTQN TPFGWTTPGW QFTWGWSPAA VPWILQNVYE YYEYTGDETY LRDVVYPMMK
     EATRYYDQTL VEDAATGMLV SSPTYSPEHG PITNGNFYEE QLIWQLYSDV ITAAEKLGLD
     ADLVQTWEAT KARLVPVEVG ASGQIKEWYE ETTLGSVSGA QSNHRHISQL LGLYPGDLIS
     VETPEYLQAA EVSLNDRGDA ATGWGIAQRL NAWARIGDGD RSLKIIEQLL RTGIYANLFD
     THPPFQIDGN FGYTAGVNEM LMQSNMGYVS LLPALPTDWD SGSVDGIVAR GDFELGIDWA
     QGRATTVSVT SRSGGDFVGD YPGISLGTVT DGSGKRIAPT VISQDRISFP TVAGQTYTVT
     SLPAVGSFAS TPTDVAALRT SDTAVDVRWA AGAPGSASFV VERKVGDGDF QVITDAASGT
     SFVDESAASG AGEYRYRVST RVGSGTSRPS LPVQVVDIRA IGVIDDRSSR LTYTGAWGNW
     NESKHLNGTI KFIEQTTGGE SISLDFVGTG VSFISPMNTS FTSVEFYVDG EKVGAQPYSL
     YSATSKVQQE HLIIDNLPKG VHRLKVVATG ASSPAGGSKI EFDAFRVRDD SAVPVQSIRI
     DSLSGSRSIG AAGGTLRLVA EASPSNASNR GVVWSVNDSS LATVDSAGTV TAGSKNGTVT
     VTATATDGSG ISATTQIRVY GDSTTRTVVD DADPGITYSS GWGVWNQDSR NRNGTLHYVE
     SGPGATATYT FTGTGVDVYG TKNDANSRRT WGTVIVSVDG VEKAAVPTND ASDAHQVLLA
     SVTGLSNGSH TVQIRNAATA QGGSKIELDY LSVSAPLAAS AERAGLQAQL QRADALDKQA
     YSAAAWEAFT VDLRAAASVM NDPSATATQL STATADLSSA IDDLG
//