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 27-MAR-2024, entry version 91. 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; 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 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 GlyCosmos; Q06670; 8 sites, No reported glycans. DR GeneID; 1403916; -. DR KEGG; vg:1403916; -. DR OrthoDB; 542at10239; -. DR Proteomes; UP000008292; Genome. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW. 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; Invertebrate chitin-binding proteins; 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 //