ID A0A164YAJ9_9CRUS Unreviewed; 1127 AA.
AC A0A164YAJ9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Chitinase 3 {ECO:0000313|EMBL:KZS15054.1};
GN ORFNames=APZ42_019604 {ECO:0000313|EMBL:KZS15054.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS15054.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS15054.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS15054.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS15054.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
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}.
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:KZS15054.1}.
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DR EMBL; LRGB01000930; KZS15054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164YAJ9; -.
DR STRING; 35525.A0A164YAJ9; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProt.
DR CDD; cd02872; GH18_chitolectin_chitotriosidase; 2.
DR Gene3D; 3.10.50.10; -; 2.
DR Gene3D; 2.170.140.10; Chitin binding domain; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
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 PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF359; CHITINASE 10-RELATED; 1.
DR Pfam; PF01607; CBM_14; 2.
DR Pfam; PF00704; Glyco_hydro_18; 2.
DR SMART; SM00494; ChtBD2; 2.
DR SMART; SM00636; Glyco_18; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF54556; Chitinase insertion domain; 2.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 2.
DR PROSITE; PS50940; CHIT_BIND_II; 2.
DR PROSITE; PS01095; GH18_1; 2.
DR PROSITE; PS51910; GH18_2; 2.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1127
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007854576"
FT DOMAIN 130..185
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 241..613
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 636..688
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 745..1117
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 192..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 125071 MW; 0F035E3BBDAB2061 CRC64;
MTATSLRLLA LFATLLVGFP GVENLAVKRQ AVQPEAPKSG SFYRGAVESP PPAVQTGRGF
QRGAVEYRPN PDFRPINPFA LRNLNSAVFL SQFYYPSLYA DHFRKLYPDY YTPFAVLPVP
ISNSIIQKDG SECLNGQALR PNPDDCAGYQ SCVHGLWENQ KCPDGLHWNA EYSICDWPSN
VRCAIEDTSS ATQAPATQAP QLSTTTPRPP ASSTTPVAPS TTSPSPTASP SAPPSSTSSE
AKVICYYTNW SWYRQGEAKY SPDNIDLKLC THILYGFATL DPNKSIMQVF DSWSDTDEYG
PSLYAKVTAL KKHGIKVLIA LGGWNDSAGG KYSVMVNNPA ARRRFIENAV IFIENYGFDG
LDLDWEYPKC WQVDCNAGPA SDKPAFAAFV KELREAFNPK GWLLTAAVSP SKAVIDAGYD
IPSLSRDLDW IGVMTYDYHG HWDKRTGHVA PLGFHSEADV AYFNTEYTLN YWIRGGADAA
KIIMGIPLYG QSFTLENPSN NGLNAPAKGT GQAGEFTRQA GFLAYYEICK MIGNGGWNVV
QDEEGALGPY AYRGDQWVSF DDVNMVRKKS EIAKAMKIGG AMIWALDLDD FRNKCGCETY
PLLKTINRVL RNYPESSAKC DVKSVPEVTR PTALSKSTCQ ENSYKSHESD CASYYHCVFG
QWSGYTCPNG LFWNKEYCDW PYNTECKGSS ETYLPAVAAP TAAPAKPDST GTTESGAYVE
WKPTTTTAKP TPSPFPEVAL PDTGFKVICY FTNWAGYRTG EGKYKPEDID PAMCTHIIYG
FATLSPSELT MRVFDSWADT DEYGPNLYAK VTALKKKGIK VLIALGGWND SLGSKYSQLV
NNPSARKRFV DNAVAFVEKY GFDGLDLDWE YPKCWQVDCK AGPDSDKPAF TAWVRELSEA
FKPRGWLLSS AVSPSKTVID LGYEVAELSP YFDWIGVMTY DYFGNWDKNT GHVAPLYAHS
QVENKFFNTN FTLNYWIELG ADPSKIIMGM PMYGQSFTLE DPASNGSNAK AKGPGEAGEF
TRQGGFLAFY EICHRMKQGG WTVVQDSEEA MGPYAYKGNQ WTSFDDVAII RRKSELVKSM
KIGGAMIWAL DLDDFRNRCG CERYPLLRTI NRVLRNYPEA DPNCNYA
//
