ID   A0A0Q5VGF0_9CAUL        Unreviewed;      1138 AA.
AC   A0A0Q5VGF0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:KQS55567.1};
GN   ORFNames=ASG17_05700 {ECO:0000313|EMBL:KQS55567.1};
OS   Brevundimonas sp. Leaf363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS55567.1, ECO:0000313|Proteomes:UP000051182};
RN   [1] {ECO:0000313|EMBL:KQS55567.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55567.1,
RC   ECO:0000313|Proteomes:UP000051182};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS55567.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55567.1,
RC   ECO:0000313|Proteomes:UP000051182};
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 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:KQS55567.1}.
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DR   EMBL; LMPZ01000002; KQS55567.1; -; Genomic_DNA.
DR   RefSeq; WP_056100370.1; NZ_LMPZ01000002.1.
DR   AlphaFoldDB; A0A0Q5VGF0; -.
DR   STRING; 1736353.ASG17_05700; -.
DR   OrthoDB; 9758603at2; -.
DR   Proteomes; UP000051182; Unassembled WGS sequence.
DR   GO; GO:0052761; F:exo-1,4-beta-D-glucosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR043534; EBDG/EBM.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR041351; Ig_GlcNase.
DR   InterPro; IPR006558; LamG-like.
DR   PANTHER; PTHR43536; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43536:SF1; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   Pfam; PF18368; Ig_GlcNase; 1.
DR   Pfam; PF13385; Laminin_G_3; 1.
DR   SMART; SM00560; LamGL; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KQS55567.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051182};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1138
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006265817"
FT   DOMAIN          55..183
FT                   /note="LamG-like jellyroll fold"
FT                   /evidence="ECO:0000259|SMART:SM00560"
SQ   SEQUENCE   1138 AA;  123433 MW;  D993067D2115F72D CRC64;
     MRWLHGAAAL VLAFAASQAE AGVPEQGGPY NVSVLAGGVG VERDLNAPAL MAEGSSFSFS
     AWVRPELAQG GTVTLLALGA AGANCRCLVL TDGRLGYQSG GQTLTTRERI APGQWTHVAV
     SSEGDQATLY VNGRRVARGR VAAVATSAKI GVAPVVGAGE SLRHFGGQMA EATLHDTALD
     GAAVTALAGD RPNFDVVHFW RVNQGWEWQN RANTGYFRPQ DPWTLPQARG EGTAPVATPV
     AARPVLEAGE PGRWTINGWT LAAAPEVTAD GAALSQPGSP AGTWRPATVP GTVLTTLVDR
     GVYPDPYYGL NNLEIPESLA RQDYWYRTSF TAPSEAAGRR HTLVLNGVNY ASEVWLNGEK
     VGSTRGAFVR GQFEVTLKPG ENVVAIQVSP PPHPGTPHEQ SIRGGVGENG GQLAIDGPTF
     VATEGWDWIP GIRDRNTGLW QNVELVTHGD VRVVDPQVIT DLPLPRTDSA DVHINVPVEN
     EADGPRTVTV RAAFDDVVVE KTVTAPPGRS VVAFAPSEFA ALRVANPRLW WPNGYGDPVL
     HDLTVTAIVD GQTSDTATSR FGIREVSYDL SLFAADGELR RVNVQTTDGG LAGQRLIDVT
     HEGIKQSPRG WAESLTPAGE ASAAVVAIDE TLPEPHLTIR VNGVRIAARG GNWGMDDAMK
     RVSRERLEPY FRLQRDGHMN VIRNWMGNNY QDSFLDLADE YGMMILSDFW QSTQNFQVEP
     QDPQLFLDNA RDTVARYRNH PSIILWFGRN EGVPYPMLNE GLDDVVAELD GTRWFTGSSN
     SINLQGSGPY NYRPPVGYFT DLATGFSVET GTPSLSTLES IQSYVPAEDL WPLSDTLAYH
     DWHFAGNGDT ATFMAALDTM FGAATSFEDF ERKAQMMNLE THKAMYEGFL GHLWTKNSGR
     LLWMTHPAWP SNAWQIYSWD YDTSAAYYGS RTATEPLHVQ MNLPDNGVVV LNTTRDDRSG
     LSVKTRIVSL DNRELFTRTD AVDALSNRVT TVGDTPLASI LETERAALVV LQLVDGEGRV
     LSDNRYWRGA TPADYRRLND LPAQPVTVSL SAARVDGDER MVTAELANTG AAPSLNLKLT
     LVDGEGRRIL PAYYADNYVT LLPGESRRID IRYPATATGA PSVRLRGWNA VAAQATAN
//