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Database: UniProt
Entry: A0A094NAW2_ANTCR
LinkDB: A0A094NAW2_ANTCR
Original site: A0A094NAW2_ANTCR 
ID   A0A094NAW2_ANTCR        Unreviewed;       487 AA.
AC   A0A094NAW2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
DE   Flags: Fragment;
GN   ORFNames=N321_00981 {ECO:0000313|EMBL:KFZ63651.1};
OS   Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus carolinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Caprimulgiformes;
OC   Caprimulgidae; Antrostomus.
OX   NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ63651.1, ECO:0000313|Proteomes:UP000053620};
RN   [1] {ECO:0000313|EMBL:KFZ63651.1, ECO:0000313|Proteomes:UP000053620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ63651.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; KL358292; KFZ63651.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094NAW2; -.
DR   Proteomes; UP000053620; 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; 3.10.50.10; -; 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:SF188; ACIDIC MAMMALIAN CHITINASE; 1.
DR   PANTHER; PTHR11177; 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   Reference proteome {ECO:0000313|Proteomes:UP000053620}.
FT   DOMAIN          10..378
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          439..487
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   REGION          382..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFZ63651.1"
FT   NON_TER         487
FT                   /evidence="ECO:0000313|EMBL:KFZ63651.1"
SQ   SEQUENCE   487 AA;  52836 MW;  0F98B1360938CEB7 CRC64;
     LLYFSAGTAY VLSCYFTNWG QYRPGVGKYM PDNIDPCLCD HLIYAFAGMN NNEITTYEWN
     DVTLYKSFNG LKNQNKNLKT LLSIGGWNFG TAKFSTMVST PENRQTFINS VIKFLRQYEF
     DGLDIDWEYP GSRGSPPQDK ALFTVLIKEM LAAFEQEAKQ VNKPRLLITA AVAAGVSNIQ
     SGYQIAELGK YLDYFHVMTY DFHGSWDGQT GENSPLFKGP SDTGDNIYFN IDYTMNYWKS
     NGAPAEKLVI GFPTYGNTFT LQNPSNNGLG APTSGPGPAG PYTQEAGELA YYEICTLLNS
     GATQVWDAPQ DVPYAYKGNE WVGYDNIKSF NIKVDWLKKN NFGGAMVWTI DMDDFTGTFC
     KQGKYPLITT LKNGLGLQNS DCVPPAHPNP PVTAAPSTTA GSSESGSGSS GSSGRGRSGR
     GRGSGSGSSG SNPGGSGGSN FCAGKSSGLY ADPTNKSNFY NCVNGETFLE SCQSGLVFDT
     SCSCCNW
//
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