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Database: UniProt
Entry: A0A0J7KQC0_LASNI
LinkDB: A0A0J7KQC0_LASNI
Original site: A0A0J7KQC0_LASNI 
ID   A0A0J7KQC0_LASNI        Unreviewed;       482 AA.
AC   A0A0J7KQC0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   08-NOV-2023, entry version 35.
DE   SubName: Full=Acidic mammalian chitinase {ECO:0000313|EMBL:KMQ92444.1};
GN   ORFNames=RF55_7554 {ECO:0000313|EMBL:KMQ92444.1};
OS   Lasius niger (Black garden ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Lasius; Lasius.
OX   NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ92444.1, ECO:0000313|Proteomes:UP000036403};
RN   [1] {ECO:0000313|EMBL:KMQ92444.1, ECO:0000313|Proteomes:UP000036403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:KMQ92444.1};
RA   Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT   "Lasius niger genome sequencing.";
RL   Submitted (APR-2015) 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:KMQ92444.1}.
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DR   EMBL; LBMM01004407; KMQ92444.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J7KQC0; -.
DR   STRING; 67767.A0A0J7KQC0; -.
DR   PaxDb; 67767-A0A0J7KQC0; -.
DR   OrthoDB; 2663738at2759; -.
DR   Proteomes; UP000036403; 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; 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:SF360; CHITINASE 12-RELATED; 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   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000036403};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..482
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005290370"
FT   DOMAIN          22..390
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          424..482
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS50940"
FT   REGION          390..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..421
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   482 AA;  53455 MW;  419A9988B32FC96B CRC64;
     MNCWIFIFAA LAALASADDS EKKIVCYFGS WSVYRPPGGK FDISDIPPQL CTHLIYSFVG
     INTQGNVIVL DAWNDLPDNW GKDGFGRFNK LREQSPKTKT LIAIGGWNEG SVKYSDVVAN
     PTIRARFVKN VVEFCQKHNF DGFDVDWEYP NQRGGKPADV QNYISLLKEL RTEFDKHGLI
     LSAAVAAAEP SASLSYDIPA MSKYLHFINV MTYDFHGAWE KTTGLNAPLY PRKDESGNDL
     KLNVDASVRY WLKSGCPPEK LILGVPFYGR AFTLANNNQN GLVAPTRGPG AAGPYTREAG
     MLGYNEICES LKQGGWTIVR HAEHRVPYAF KGDQWIGYDD ITSLNEKMDY INSLNLGGAM
     MWSIETDDFN GNCGEKYPLL KTLNAKLRGG VPIEPSKPTE APKETNPPKP TAQPTQPPAT
     TPPNGICKKA GFVRDEKDCN VFYQCVDLNG IYKVERFTCP SGLVFDTNTN NCNYKNLVAG
     CN
//
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