ID   CHIT_NPVOP              Reviewed;         550 AA.
AC   O10363;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Probable endochitinase;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   ORFNames=ORF124;
OS   Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus;
OC   Alphabaculovirus orpseudotsugatae.
OX   NCBI_TaxID=262177;
OH   NCBI_TaxID=33414; Orgyia pseudotsugata (Douglas-fir tussock moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9126251; DOI=10.1006/viro.1997.8448;
RA   Ahrens C.H., Russell R.R., Funk C.J., Evans J., Harwood S., Rohrmann G.F.;
RT   "The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear
RT   polyhedrosis virus genome.";
RL   Virology 229:381-399(1997).
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   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum lumen {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; U75930; AAC59123.1; -; Genomic_DNA.
DR   RefSeq; NP_046280.1; NC_001875.2.
DR   SMR; O10363; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GeneID; 912030; -.
DR   KEGG; vg:912030; -.
DR   OrthoDB; 2555at10239; -.
DR   Proteomes; UP000009248; Genome.
DR   GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02848; E_set_Chitinase_N; 1.
DR   CDD; cd06548; GH18_chitinase; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR013540; ChitinaseA_N.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR   Pfam; PF08329; ChitinaseA_N; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Chitin degradation; Glycoprotein; Glycosidase;
KW   Host endoplasmic reticulum; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..550
FT                   /note="Probable endochitinase"
FT                   /id="PRO_0000011951"
FT   DOMAIN          147..547
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   MOTIF           547..550
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        304
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        146
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   550 AA;  60734 MW;  77947F5CF00E07BD CRC64;
     MLHYLATILW LAVAHASPGT PVIDWADRNY ALVSVNSEAT AYENLVERKA GVSVPVSWNV
     WNGGVGDMAY VLFNENQVWK GAAAAKRATI DVSKSGQFNM RVKLCDDDGF SVSEPVTVRV
     ADTDGGHLSP LEYAWGENNK PGRPHNKTVA AYFVEWGVYG RGFPVDKVPL PNLSHLLYGF
     IPICGGDGLN DALKTIPGSF EALQRSCKGR ADFKVAIHDP WAAIQKPQKG VSAWNEPYKG
     NFGQLMAAKL ANPHLKILPS IGGWTLSDPF YFMHDADKRR VFVESVKEFL QVWKFFDGVD
     IDWEFPGGKG ANPALGNGER DADTYLVLLK ELRAMLDELQ LQTNKTYELT SAISSGYDKI
     AVVKYDAAQR FLDKIFLMSY DFKGAWSNTD LGYQTTLYAP SWNANELYTT DHAVKLLTGQ
     GVAAHKLIVG VAMYGRGWTG VSGYAGDKYF SGTADGPVPG TWENGVVDYR QINNELSKYI
     YRFDAAAKAA YVFNKERGDL ISFDSVDSVL AKNVYVQQNG LGGLFAWEID ADNGDLLNAM
     NERVRVKDEL
//