ID   CHIT_NPVAC              Reviewed;         551 AA.
AC   P41684;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Chitinase;
DE            EC=3.2.1.14;
DE   Flags: Precursor;
GN   Name=CHIA; ORFNames=ORF126;
OS   Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus;
OC   Alphabaculovirus aucalifornicae.
OX   NCBI_TaxID=46015;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6;
RX   PubMed=8030224; DOI=10.1006/viro.1994.1380;
RA   Ayres M.D., Howard S.C., Kuzio J., Lopez-Ferber M., Possee R.D.;
RT   "The complete DNA sequence of Autographa californica nuclear polyhedrosis
RT   virus.";
RL   Virology 202:586-605(1994).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9811762; DOI=10.1128/jvi.72.12.10207-10212.1998;
RA   Thomas C.J., Brown H.L., Hawes C.R., Lee B.Y., Min M.K., King L.A.,
RA   Possee R.D.;
RT   "Localization of a baculovirus-induced chitinase in the insect cell
RT   endoplasmic reticulum.";
RL   J. Virol. 72:10207-10212(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=11062048; DOI=10.1006/viro.2000.0586;
RA   Hom L.G., Volkman L.E.;
RT   "Autographa californica M nucleopolyhedrovirus chiA is required for
RT   processing of V-CATH.";
RL   Virology 277:178-183(2000).
RN   [4]
RP   FUNCTION.
RX   PubMed=21897030; DOI=10.1271/bbb.110300;
RA   Fukamizo T., Sato H., Mizuhara M., Ohnuma T., Gotoh T., Hiwatashi K.,
RA   Takahashi S.;
RT   "Chitinase from Autographa californica multiple nucleopolyhedrovirus: rapid
RT   purification from Sf-9 medium and mode of action.";
RL   Biosci. Biotechnol. Biochem. 75:1763-1769(2011).
RN   [5]
RP   INTERACTION WITH VCATH, FUNCTION, REGION, AND SUBCELLULAR LOCATION.
RX   PubMed=23302896; DOI=10.1128/jvi.01937-12;
RA   Hodgson J.J., Arif B.M., Krell P.J.;
RT   "Role of interactions between Autographa californica multiple
RT   nucleopolyhedrovirus procathepsin and chitinase chitin-binding or active-
RT   site domains in viral cathepsin processing.";
RL   J. Virol. 87:3471-3483(2013).
CC   -!- FUNCTION: Plays a role in host liquefaction to facilitate horizontal
CC       transmission of the virus by hydrolyzing beta-chitin and by regulating
CC       the cysteine protease VCATH. Localized in the host reticulum
CC       endoplasmic via its KDEL motif, interacts with and thus prevents VCATH
CC       secretion before host cell lysis occurs. {ECO:0000269|PubMed:11062048,
CC       ECO:0000269|PubMed:21897030, ECO:0000269|PubMed:23302896}.
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   -!- SUBUNIT: Interacts with host VCATH. {ECO:0000269|PubMed:23302896}.
CC   -!- SUBCELLULAR LOCATION: Host endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:23302896, ECO:0000269|PubMed:9811762}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000305}.
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DR   EMBL; L22858; AAA66756.1; -; Genomic_DNA.
DR   PIR; G72865; G72865.
DR   RefSeq; NP_054156.1; NC_001623.1.
DR   SMR; P41684; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   GlyCosmos; P41684; 2 sites, No reported glycans.
DR   GeneID; 1403959; -.
DR   KEGG; vg:1403959; -.
DR   OrthoDB; 2555at10239; -.
DR   Proteomes; UP000008292; 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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Glycoprotein; Glycosidase;
KW   Host endoplasmic reticulum; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..551
FT                   /note="Chitinase"
FT                   /id="PRO_0000011950"
FT   DOMAIN          148..548
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   REGION          1..149
FT                   /note="Chitin binding domain (CBD)"
FT                   /evidence="ECO:0000269|PubMed:23302896"
FT   MOTIF           548..551
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        305
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   551 AA;  61368 MW;  4DDAAD187873BBA2 CRC64;
     MLYKLLNVLW LVAVSNAIPG TPVIDWADRN YALVEINYEA TAYENLIKPK EQVDVQVSWN
     VWNGDIGDIA YVLFDEQQVW KGDAESKRAT IKVLVSGQFN MRVKLCNEDG CSVSDPVLVK
     VADTDGGHLA PLEYTWLENN KPGRREDKIV AAYFVEWGVY GRNFPVDKVP LPNLSHLLYG
     FIPICGGDGI NDALKTIPGS FESLQRSCKG REDFKVAIHD PWAAVQKPQK GVSAWNEPYK
     GNFGQLMAAK LANPHLKILP SIGGWTLSDP FYFMHDVEKR NVFVDSVKEF LQVWKFFDGV
     DIDWEFPGGK GANPSLGDAD GDAKTYILLL EELRAMLDDL EAQTGRVYEL TSAISAGYDK
     IAVVNYAEAQ KSLGKIFLMS YDFKGAWSNT DLGYQTTVYA PSWNSEELYT THYAVDALLK
     QGVDPNKIIV GVAMYGRGWT GVTNYTNDNY FSGTGNGPGS GTWEDGVVDY RQIQKDLNNY
     VYTFDSAAQA SYVFDKSKGD LISFDSVDSV LGKVKYVDRN KLGGLFAWEI DADNGDLLNA
     INAQFKPKDE L
//