AC83_NPVAC
ID AC83_NPVAC Reviewed; 847 AA.
AC Q06670;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 23-FEB-2022, entry version 86.
DE RecName: Full=Capsid-associated protein AC83;
DE Flags: Precursor;
GN Name=p95; ORFNames=ORF83;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E2;
RX PubMed=8126447; DOI=10.1099/0022-1317-75-3-487;
RA Kool M., Broer R., Zuidema D., Goldbach R.W., Vlak J.M.;
RT "Nucleotide sequence and genetic organization of a 7.3 kb region (map unit
RT 47 to 52.5) of Autographa californica nuclear polyhedrosis virus fragment
RT EcoRI-C.";
RL J. Gen. Virol. 75:487-494(1994).
RN [3]
RP FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=23864639; DOI=10.1128/jvi.01207-13;
RA Zhu S., Wang W., Wang Y., Yuan M., Yang K.;
RT "The baculovirus core gene ac83 is required for nucleocapsid assembly and
RT per os infectivity of Autographa californica nucleopolyhedrovirus.";
RL J. Virol. 87:10573-10586(2013).
CC -!- FUNCTION: Plays an essential role in nucleocapsid assembly. Essential
CC for the establishment of efficient per os infection.
CC {ECO:0000269|PubMed:23864639}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:23864639}.
CC Note=Localizes specifically to the ODV envelope.
CC {ECO:0000269|PubMed:23864639}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L22858; AAA66713.1; -; Genomic_DNA.
DR EMBL; X71415; CAA50547.1; -; Genomic_DNA.
DR PIR; D72860; D72860.
DR PIR; S36699; S36699.
DR RefSeq; NP_054113.1; NC_001623.1.
DR SMR; Q06670; -.
DR CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR GeneID; 1403916; -.
DR KEGG; vg:1403916; -.
DR Proteomes; UP000008292; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR013682; BaculoV_Vp91_N.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
DR Pfam; PF08475; Baculo_VP91_N; 1.
DR Pfam; PF01607; CBM_14; 1.
DR SMART; SM00494; ChtBD2; 1.
DR SUPFAM; SSF57625; SSF57625; 2.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS51807; ZF_C2HC_BV; 1.
PE 3: Inferred from homology;
KW Chitin-binding; Disulfide bond; Glycoprotein; Metal-binding;
KW Reference proteome; Repeat; Signal; Virion; Zinc; Zinc-finger.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..847
FT /note="Capsid-associated protein AC83"
FT /id="PRO_0000036751"
FT DOMAIN 224..282
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT ZN_FING 148..197
FT /note="C2HC BV-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01148,
FT ECO:0000269|PubMed:23864639"
FT REGION 665..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 208..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT DISULFID 261..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT CONFLICT 202
FT /note="A -> T (in Ref. 2; CAA50547)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="G -> D (in Ref. 2; CAA50547)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="S -> T (in Ref. 2; CAA50547)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="A -> T (in Ref. 2; CAA50547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 847 AA; 96210 MW; 041412831DCA341C CRC64;
MMSGVMLLML AIFLIIAFTL MYLAIYFEFD ETTFTKRLQV MTEYVKRTNA DEPTPDVIGY
VSDIMQNTYI VTWFNTVDLS TYHESVHDDR IEIFDFLNQK FQPVDRIVHD RVRANDENPN
EFILSGDKAD VTMKCPAYFN FDYAQLKCVP VPPCDNKSAG LYPMDERLLD TLVLNQHLDK
DYSTNAHLYH PTFYLRCFAN GAHAVEECPD NYTFDAETGQ CKVNELCENR PDGYILSYFP
SNLLVNQFMQ CVNGRHVVGE CPANKIFDRN LMSCVEAHPC AFNGAGHTYI TADIGDTQYF
KCLNNNESQL ITCINRIRNS DNQYECSGDS RCIDLPNGTG QHVFKHVDDD ISYNSGQLVC
DNFEVISDIE CDQSNVFENA LFMDKFRLNM QFPTEVFDGT ACVPATADNV NFLRSTFAIE
NIPNHYGIDM QTSMLGTTEM VKQLVSKDLS LNNDAIFAQW LLYARDKDAI GLNPFTGEPI
DCFGDNLYDV FDARRANICN DSGTSVLKTL NFGDGEFLNV LSSTLTGKDE DYRQFCAISY
ENGQKIVENE HFQRRILTNI LQSDVCADLY TTLYQKYTTL NSKYTTTPLQ YNHTLVKRPK
NIEIYGANTR LKNATIPKNA ATIPPVFNPF ENQPNNRQND SILPLFNPFQ TTDAVWYSEP
GGDDDHWVVA PPTAPPPPPE PEPEPEPEPE PEPELPSPLI LDNKDLFYSC HYSVPFFKLT
SCHAENDVII DALNELRNNV KVDADCELAK DLSHVLNAYA YVGNGIGCRS AYDGDAIVVK
KEAVPSHVYA NLNTQSNDGV KYNRWLHVKN GQYMACPEEL YDNNEFKCNI ESDKLYYLDN
LQEDSIV
