CHIT_NPVAC
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 29-SEP-2021, entry version 108.
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.
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 GeneID; 1403959; -.
DR KEGG; vg:1403959; -.
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 Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.50.10; -; 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 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; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR SUPFAM; SSF81296; SSF81296; 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
