ID   A0A3N7HXI8_9BURK        Unreviewed;       503 AA.
AC   A0A3N7HXI8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:RQP26623.1};
GN   ORFNames=DZC73_06395 {ECO:0000313|EMBL:RQP26623.1};
OS   Albitalea terrae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Albitalea.
OX   NCBI_TaxID=2496871 {ECO:0000313|EMBL:RQP26623.1, ECO:0000313|Proteomes:UP000267464};
RN   [1] {ECO:0000313|EMBL:RQP26623.1, ECO:0000313|Proteomes:UP000267464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S-16 {ECO:0000313|EMBL:RQP26623.1,
RC   ECO:0000313|Proteomes:UP000267464};
RA   Khan S.A., Jeon C.O., Chun B.H., Jeong S.E.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RQP26623.1, ECO:0000313|Proteomes:UP000267464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S-16 {ECO:0000313|EMBL:RQP26623.1,
RC   ECO:0000313|Proteomes:UP000267464};
RA   Shunsuke S.S.;
RT   "Rhizobacter gummiphilus sp. nov., a rubber-degrading bacterium isolated
RT   from the soil of a botanical garden in Japan.";
RL   Submitted (DEC-2018) 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:RQP26623.1}.
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DR   EMBL; QUSW01000001; RQP26623.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N7HXI8; -.
DR   OrthoDB; 6018988at2; -.
DR   Proteomes; UP000267464; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; cd12214; ChiA1_BD; 1.
DR   CDD; cd12215; ChiC_BD; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR42976; BIFUNCTIONAL CHITINASE/LYSOZYME-RELATED; 1.
DR   PANTHER; PTHR42976:SF1; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02839; CBM_5_12; 2.
DR   SMART; SM00495; ChtBD3; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RQP26623.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267464};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..503
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018092425"
FT   DOMAIN          32..79
FT                   /note="Chitin-binding type-3"
FT                   /evidence="ECO:0000259|SMART:SM00495"
FT   DOMAIN          118..167
FT                   /note="Chitin-binding type-3"
FT                   /evidence="ECO:0000259|SMART:SM00495"
FT   REGION          62..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..116
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..192
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  52134 MW;  06A0C5524FD9F2DE CRC64;
     MTTTASTRLQ TLRVLSALTA ALAATSIYAA NYPAWKPDTF YAAGTKVYYN GRDYQALVDQ
     TDYSSTGWNP TTTSLWKDLG PDSAPSPAPA PAPSPAPAPA PSPAPAPAPA PAPAPGCQPA
     WNASTAYTQG QQASVNGVNY KANWWTQGQN PATNNGPSGS GQPWTQVNTC APAPAPAPAP
     APAPAPAPAP APAPAPSGFV FGPYKDVTIN MDWNTNVMST MVTGSRQPAV SVMPARAKTV
     TWAFASGECG SETWAGVQPA ALAAANVQRF IDAGKTYIIS TGGAAGTFTC GSDPNFTKFI
     NTYNSANMIG VDFDIEGGQS QDVINNLVQR SMAAQSKYPK LRFSFTIATL GGNAANSLGS
     AGANVMTAIK NFGMKNYIIN LMVMDYGSTT ATNCTIGSNG KCDMGKSAIA AAQSLHNFYG
     VPYSQIELTP MVGGNDTQDE VFTLTDVDTL SAWAKGNGLA GVHFWSLDRD VDCPAGSASA
     TCNSYGQAGT WGFTNRFVSK LGL
//