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Database: UniProt
Entry: A0A1A6HCP6_NEOLE
LinkDB: A0A1A6HCP6_NEOLE
Original site: A0A1A6HCP6_NEOLE 
ID   A0A1A6HCP6_NEOLE        Unreviewed;       469 AA.
AC   A0A1A6HCP6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
DE   Flags: Fragment;
GN   ORFNames=A6R68_14035 {ECO:0000313|EMBL:OBS75407.1};
OS   Neotoma lepida (Desert woodrat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Neotominae; Neotoma.
OX   NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS75407.1, ECO:0000313|Proteomes:UP000092124};
RN   [1] {ECO:0000313|EMBL:OBS75407.1, ECO:0000313|Proteomes:UP000092124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=417 {ECO:0000313|EMBL:OBS75407.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:OBS75407.1};
RA   Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT   "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT   lepida.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OBS75407.1}.
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DR   EMBL; LZPO01037266; OBS75407.1; -; Genomic_DNA.
DR   STRING; 56216.A0A1A6HCP6; -.
DR   Proteomes; UP000092124; 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: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; 3.20.20.80; 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:SF248; CHITOTRIOSIDASE-1; 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   Reference proteome {ECO:0000313|Proteomes:UP000092124}.
FT   DOMAIN          22..381
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          410..458
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   REGION          378..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        386..405
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         469
FT                   /evidence="ECO:0000313|EMBL:OBS75407.1"
SQ   SEQUENCE   469 AA;  51977 MW;  EF7EEE7A45D3CED1 CRC64;
     MGLTSARASI MVQFMALAGS AAKLVCYFTS WAQYRPGTAR FLPRDVDPNL CTHLNYAFAG
     MDNHQLNSVE WNDKRLYQEL NGLKKMNPKL KTLISIGGWT FGTQKFTDMV ATASNRQTFV
     NSAIKFLRTH GFDGLDLDWE YPGSHGSPAE DKERFTALLQ DLATAFQEEA QTSGKERLLL
     TAAVPAGQDH VDAGYEVDKI ALSLDFINLM AYDFHGSWEK TTGHNSPLYK XQEESEAATR
     FNVDAAVQLW LQKGMPASKL ILGMPTYGRS FTLASSXDNR VGAPATGPGA PGPYTREGGI
     LAYFEEKHRI KDQKVPYVFQ DNQWVGFDDM ESFRAKVSYL KQKGLGGAMV WSLDLDDFTG
     SFCNQGQYPL IRTLQQELSL PSLPPRSPEQ EVPRPHQPPE PEQGPSPELD TFCQGKADGL
     YPNPGEKSSY YSCAQGRLFQ QNCPQGLVFS DSCKCCTWSR VPGTPSTPA
//
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