ID   A0A143HN00_9GAMM        Unreviewed;      1036 AA.
AC   A0A143HN00;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:AMX03073.1};
GN   ORFNames=A3224_11300 {ECO:0000313|EMBL:AMX03073.1};
OS   Microbulbifer thermotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX03073.1, ECO:0000313|Proteomes:UP000076077};
RN   [1] {ECO:0000313|Proteomes:UP000076077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA   Lee Y.-S., Choi Y.-L.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR   EMBL; CP014864; AMX03073.1; -; Genomic_DNA.
DR   RefSeq; WP_067154568.1; NZ_CP014864.1.
DR   AlphaFoldDB; A0A143HN00; -.
DR   STRING; 252514.A3224_11300; -.
DR   GeneID; 76608634; -.
DR   KEGG; mthd:A3224_11300; -.
DR   OrthoDB; 9775889at2; -.
DR   Proteomes; UP000076077; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd12204; CBD_like; 1.
DR   CDD; cd06548; GH18_chitinase; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR032798; CBM_5_12_2.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR009470; Chi_C.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF308; CHITINASE A; 1.
DR   Pfam; PF17957; Big_7; 2.
DR   Pfam; PF14600; CBM_5_12_2; 1.
DR   Pfam; PF06483; ChiC; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 2.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076077};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1036
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007509686"
FT   DOMAIN          311..788
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          957..978
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1036 AA;  111357 MW;  D37FDA5952C2805B CRC64;
     MQRRIAIALT LGLAGTQGYA YDCSGLPAYA DGTSYNTGDQ VQNNNTAYQC TVGGWCTIGG
     PYAPGVGWAW PHAWTDLGEC GAAQDTPPQG SITSPASGTV FNKNDSVIIS VDASDNSAVV
     SVEFFVDGTS IGTDITPPWQ ISWSASGTNP VLSARITDDA GQQTVTPDIP ITVNNPEGPQ
     APQISLDAPA NGTTFDTGAS VAITATASDT DGSLLNVEFF VDGASVGVDT TPPYQFNWTA
     IEGNHTIHAV ATDDDHLSTN SNSVYISVGE AHTGDHPCRP DGLYTTPGTA PNYCDIYDAA
     GREKLGPDHQ RRIIGYFTSW RNGTNGQPSY LVKDIPWDKV THINYAFAHI DSDYSISIGD
     TSNPDNPSTG MEWPGVSGAE TDPAFNYKGH FNQLAKYKKQ HPDVKTLVSV GGWAETGGHL
     NEQGDRVNDG GFYTMTTNAD GSVNYAGIEA FANSVVDFIR TYGFDGVDID YEYPTSMNDA
     GNPLDFGFAN PLRAYLMNSY VALMRVLREK LDQAGEEDNT HYLLTIAAPS SGYLLRGMET
     MPITQYLDYV NIMTYDFHGT WNEYVGHNSA IFDNGNDPEL KAANIYNTAQ YGGIGYLNID
     WAVKYFRGSM SPGRINIGTP YYTRGWQNVT SANGEWGLGG TASLPNQSEC PAGTGGAAKC
     GYGAIGIDNI WHDSDGNGQE IGAGTNPLWH AKNLEQGILG SYIGYYGLDT VNDPADRLVG
     TYTRHYDSVS QAAWLWNDTK KVFLSTEDEA SMEAKAQYVI DQGLGGIMIW ELAGDYAWNT
     AKNEYFIGST MTDVAYEKFK SATPYREKRS NRPLPTQAVD ITITVSDFKL GDQNYPLNPK
     LAITNNTGTT IPGGTVFEFD MPTSTPDTIS DQSGAGLEVI ESGANAGGGN VGGLQHEFHR
     VRFSLPNWKD LADGESWDMT LNYYLPITGP QAYTVTINGT AYALAFEYPD LPLADLSGDH
     NNGGDGNSGD NGGDDNCAGM GIDPSVYPVY PNWPAGDHAN GGDRIVHNGS VWQAKWWTNS
     QPGSSDGSWT LICSAN
//