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Database: UniProt
Entry: I3JC25_ORENI
LinkDB: I3JC25_ORENI
Original site: I3JC25_ORENI 
ID   I3JC25_ORENI            Unreviewed;       453 AA.
AC   I3JC25;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   Name=LOC100706435 {ECO:0000313|Ensembl:ENSONIP00000006415.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000006415.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000006415.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; I3JC25; -.
DR   STRING; 8128.ENSONIP00000075132; -.
DR   Ensembl; ENSONIT00000006420.2; ENSONIP00000006415.2; ENSONIG00000005104.2.
DR   eggNOG; KOG2806; Eukaryota.
DR   GeneTree; ENSGT00940000162989; -.
DR   HOGENOM; CLU_002833_3_1_1; -.
DR   TreeFam; TF315610; -.
DR   Proteomes; UP000005207; Linkage group LG5.
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:SF332; CHITINASE; 1.
DR   Pfam; PF01607; CBM_14; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 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   Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..453
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5025462303"
FT   DOMAIN          20..387
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          404..453
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
SQ   SEQUENCE   453 AA;  50098 MW;  07B7B2DE916A8C00 CRC64;
     MAKLLIALGI LCVIHIGSAN KLVCQMTNWA QYRPSAGKFT PDNIDPFLCT HVIYALATIN
     SFNQIIPVEQ NDEELYSSLN SLKNVNPALK TLLTVGGTVN GVSPFIAMVA TSENRALFIK
     SAINFLHAHN FDGINLDWEY PGHNGSPEGD KEKFTLLVTE LVKAFEADAI ENKRTQLLLS
     ANVAAFPQTV DRAYEVAKIA PHFDFINIMT YDYHGSWDPV TGHNSPLYES AVDSGVQLHY
     NINSSIAYWV SLGAPSEKLL LGFPTYGRTF RLSSGANGLG APANGPADAG PYTRTEGFWA
     FYEICDFTNT ATLGWISEQE VPYATYGSSW LGYDDQRSYS SKVQWMTANN LGGAHVWTLD
     MDDFSGSFCS AGAYPLINHL RTLMGFTPKP TTTPRPTTTR DPSADFCHAR PDGLYENPAD
     KTTFFQCFQG NTYLHRCQPG LIYWDSCKCC NWP
//
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