ID   A0A0Q8ZRN8_9FLAO        Unreviewed;      1318 AA.
AC   A0A0Q8ZRN8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:KRD08985.1};
GN   ORFNames=ASE21_14135 {ECO:0000313|EMBL:KRD08985.1};
OS   Flavobacterium sp. Root901.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1736605 {ECO:0000313|EMBL:KRD08985.1, ECO:0000313|Proteomes:UP000051400};
RN   [1] {ECO:0000313|EMBL:KRD08985.1, ECO:0000313|Proteomes:UP000051400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root901 {ECO:0000313|EMBL:KRD08985.1,
RC   ECO:0000313|Proteomes:UP000051400};
RX   PubMed=26633631; DOI=.1038/nature16192;
RA   Bai Y., Muller D.B., Srinivas G., Garrido-Oter R., Potthoff E., Rott M.,
RA   Dombrowski N., Munch P.C., Spaepen S., Remus-Emsermann M., Huttel B.,
RA   McHardy A.C., Vorholt J.A., Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiota.";
RL   Nature 528:364-369(2015).
RN   [2] {ECO:0000313|Proteomes:UP000051400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000051400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root901 {ECO:0000313|Proteomes:UP000051400};
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC       {ECO:0000256|ARBA:ARBA00006865}.
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:KRD08985.1}.
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DR   EMBL; LMJB01000007; KRD08985.1; -; Genomic_DNA.
DR   RefSeq; WP_057123392.1; NZ_LMJB01000007.1.
DR   STRING; 1736605.ASE21_14135; -.
DR   OrthoDB; 9809583at2; -.
DR   Proteomes; UP000051400; Unassembled WGS sequence.
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; cd08023; GH16_laminarinase_like; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR045829; PKD_6.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR10963:SF55; GH16 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   Pfam; PF19408; PKD_6; 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KRD08985.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          5..292
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   DOMAIN          1085..1221
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
SQ   SEQUENCE   1318 AA;  143322 MW;  5E952BBBD62DA03D CRC64;
     MNQNDSFFGR PPEDNFYYFK RFLAAAVFIL LPFLNVQSQC KTLVWSDEFN GTTVDLTKWQ
     SISGNGCPSL CGFGNAEAQR YDPNQATIVK EGTNSYLNIQ AKYEPNASFP DQPYASSKLT
     TEGKYSLKYG RVEARMKLSN GQGAWPAFWM LPVGGNWPYT GEIDIMEAKH RNPQSVDGTI
     HYDGNGYHFT GRSYSSPTDL STDFHIYAVE WGPNFIKWYV DDVLFHTATP NTTVNGGWPF
     NDNQFYIILN LAVGSAGTPY TSVNGAGVAP VPGDFPAKLQ VDYVRVYDGS YKYAVAGDAK
     VYQNETGKTY SINAIAGASY NWSVPSGATI TAGQGTNAVT VNWGTTGGDV VVTATTSGCT
     ANTYKLAVIT EAAIPVEKIQ EDFQSNRNIV YGNKTGVLTE AVANPSATGI NTSALVGKYV
     RNSSEQYDVF NIKNVVISNA NDYVYGRKRI SFDLYTSAPV GTKISMQLEN SNVTTATNYP
     SGRHSGYKAT TTVQNKWETI EFEFEKIIDP NTSALTINNV AFLFESNSNS GATYYFDNLL
     TRATPEKPIV ATDVLQNYDG INKIIKGTTT GTYSVVANPG SNAVNSSANV AKYVRNVTEQ
     YDVLFFNTQN TIEDAGLLKN QTNKIMIDVY TSAPVGTVVS LNLENSATSL PANYPTGRNS
     NYVAITTKQN QWETLTFYYN SSPDAGTSNL AVNQMVLLFN SGSYTSDTYY FDNIRIGATK
     LPDTLTPGVV YEDYQTIHNI SFRDAIGTYT ANTPNPSATG INTSSNVGKY VRKSTEMYDN
     FSFNTTLTNI GDFKAGTKKF AMDVYTSAPV GSIISWQAES SASVPSNYPV GRHSIYQGVV
     KQTNTWHTIT FTYVSTPDAS TLDSEVNRFV FLYEPGTNSG NTYYFDNIRA LNLVSTETPA
     GLPSPWISTD LGAVTPAGEA SHSAGTFTIK GSGNDIWETS DQFQFVNQSI TGDAEIIAKI
     NSLTNTSTYS KAGVMFRETL TATSKHAMTD VTPAAGVEFL SRNTSSGVTA ADAAAGTAPK
     WVRLVRSGNV FTSYTSDNGT TWTQLGTPKT ISMSNTIYVG MAVTSHANGT LGTGVFSDVI
     VRNITANPNV NLALSKTATA STEENAMYTA AKATDGDAAV SRWASSFANA TEWIYVDLGS
     NYNLNRVVLK WEAAYATQYK VQLSTDNVFT ENETISTQTA SDGGTDDLTV SGTGRYLRIL
     CTAKALAPYG YSLYEIEAYG SASSAKKANV IVEESKPENA VFTIYPNPAS NYIQVSLPEN
     LDNKIITIYD NSGTLMLQNI PEAEAVESVI DLSRLTKGIY ILNFKSDQKS WTKKLIKK
//