ID A0A162XIB9_9FLAO Unreviewed; 808 AA.
AC A0A162XIB9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=AWE51_13755 {ECO:0000313|EMBL:KZS38654.1};
OS Aquimarina aggregata.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1642818 {ECO:0000313|EMBL:KZS38654.1, ECO:0000313|Proteomes:UP000076715};
RN [1] {ECO:0000313|EMBL:KZS38654.1, ECO:0000313|Proteomes:UP000076715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RZW4-3-2 {ECO:0000313|EMBL:KZS38654.1,
RC ECO:0000313|Proteomes:UP000076715};
RA Wang Y.;
RT "The draft genome sequence of Aquimarina sp. RZW4-3-2.";
RL Submitted (JAN-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}.
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:KZS38654.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LQRT01000046; KZS38654.1; -; Genomic_DNA.
DR RefSeq; WP_066318184.1; NZ_LQRT01000046.1.
DR AlphaFoldDB; A0A162XIB9; -.
DR STRING; 1642818.AWE51_13755; -.
DR OrthoDB; 9775889at2; -.
DR Proteomes; UP000076715; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd02871; GH18_chitinase_D-like; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR011583; Chitinase_II.
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 InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF17957; Big_7; 2.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SMART; SM00495; ChtBD3; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding 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:ARBA00023024};
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:ARBA00023024};
KW Reference proteome {ECO:0000313|Proteomes:UP000076715};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 375..709
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 808 AA; 88332 MW; 75AC75760E48878C CRC64;
MKRKHKPYSR WLPFKYSLVL LVFILLGNSY NSLASNLIKV IDVKPYVVCD APTWSASATY
VGGNQVVFNG IVYEAKWWNK NKNPETYSGR DDEWKRLGPC DGGGDSNIPP VVSIITPISG
ETFITGDSIS ITASTSDQDG EIRKVEFYVN GNNIGEDLTA PYTVNWIAVQ GNHSITAKAI
DNDNANNTSG IITITVQSDT GGGTDCNTPQ YSEGDDYTEG STVQKAGSIY ECKPWPFSGW
CNGIASAYAP GTGTNWEDAW VLLGECDPDG GNGEPLVSIV SPNDGQSFVE GSNAIINVNA
TDRDGTITKV EFFSNGSKIG EDTTEPYSYT WNTLQVGNYA LTAKATDNQD LSTTSSAVNI
RVTTSGGGGG PLPQKILNGY WHNFQNGSGL IRLRDVSSNW DVINVSFAEP RVSSTDGELS
FELAPEFSTI NYTENDFKSD IQYLKGIGKK VIISIGGAEG QVRLNTVSAR DKFVNSMIAI
IEEYDFDGMD IDFEGQSLSL DLGDDDFKNP TTPVLVNTIN AVKSVCNHFG NDFMLTMAPE
TFFVQLGYSF YGGISQGADR RAGAYLPLIH ALRDKLTFLQ VQYYNSGSIT GLDDRFYSMG
NSDFYVALVD MLLKGFPITR DSSKFFPALR PDQILIGVPA TVNAGGGFTG ANGVIDAFDY
LVKGNSFGGQ YQLSQTYPGL RGVMSWSINW DEFGGFAFSN PVRIYLDGLS GKEGDMQALD
INSNGVKAVL FPNPVDNYLN IQFTSKKEIG YTLKIYNSLG TEVIDRIKVN NAHDFNVHRY
DLSILESGLY FYEMKVNGKV FTGRIIKK
//
