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Database: UniProt
Entry: A0A3B4TU66_SERDU
LinkDB: A0A3B4TU66_SERDU
Original site: A0A3B4TU66_SERDU 
ID   A0A3B4TU66_SERDU        Unreviewed;       463 AA.
AC   A0A3B4TU66;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000009844.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000009844.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC         (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00000822};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR   AlphaFoldDB; A0A3B4TU66; -.
DR   STRING; 41447.ENSSDUP00000009844; -.
DR   Ensembl; ENSSDUT00000010034.1; ENSSDUP00000009844.1; ENSSDUG00000007225.1.
DR   GeneTree; ENSGT00940000162989; -.
DR   OMA; AGVYSHI; -.
DR   Proteomes; UP000261420; Unplaced.
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:UniProtKB-EC.
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; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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:SF379; CHITINASE; 1.
DR   Pfam; PF01607; CBM_14; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00494; ChtBD2; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR   PROSITE; PS50940; CHIT_BIND_II; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..463
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017485924"
FT   DOMAIN          22..389
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          414..463
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
SQ   SEQUENCE   463 AA;  51685 MW;  7A73B4756934E1CB CRC64;
     MHLSVFLSIG LCLVMCQLAT ASQMVCYFTN WSQYRPGTGK YTPQNVDPFM CTHLIYAFSI
     INNKNELVTY EWNDETLYKT FNGLKSKNPG LKTLLAVGGW NFGSAQFSIM VSNPANRQTF
     IQSSIKFLRT HGFDGLDLDW EYPGSRGSPP EDKKRFSLLC KELVAAFAAE AKATGKPQLM
     LTAAVSAGKG TIDAGYEIAE IAKHLDFINV MTYDFHGAWE RSTGHNSPLY RGSQDKGDLI
     YFNTDYAMKY WRDKGTPVEK LRMGFAAYGR TFRLTSSNTN IGASASGAAS AGPFTREAGF
     WSYYEVCNFL KGTTIQWIDD QKVPYASKNN EWVGFDSRES YEIKVQYMKN MKYGGAFVWA
     LDLDDFKGEF CGQGNYPLLS HLRKLLDIAS TTTPKPSGTT NAPSTRTTIP IPGRGFCKDK
     PDGTYAHPDD KTSFYVCAGG RTYLRKCGNG TIFEESCKCC VWP
//
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