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VP91_NPVBM
ID   VP91_NPVBM              Reviewed;         839 AA.
AC   O92446; O57075;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   29-SEP-2021, entry version 72.
DE   RecName: Full=Capsid-associated protein Vp91;
DE   Flags: Precursor;
GN   Name=p95; ORFNames=ORF69;
OS   Bombyx mori nuclear polyhedrosis virus (BmNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=271108;
OH   NCBI_TaxID=7091; Bombyx mori (Silk moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate ML1;
RX   PubMed=9573244; DOI=10.1128/jvi.72.6.4789-4797.1998;
RA   Lu M., Swevers L., Iatrou K.;
RT   "The p95 gene of Bombyx mori nuclear polyhedrosis virus: temporal
RT   expression and functional properties.";
RL   J. Virol. 72:4789-4797(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T3;
RX   PubMed=10355780; DOI=10.1099/0022-1317-80-5-1323;
RA   Gomi S., Majima K., Maeda S.;
RT   "Sequence analysis of the genome of Bombyx mori nucleopolyhedrovirus.";
RL   J. Gen. Virol. 80:1323-1337(1999).
CC   -!- FUNCTION: Probable capsid-associated protein. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=In virions, associates
CC       with the capsid and maybe also with the envelope surrounding the
CC       capsid. {ECO:0000250}.
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DR   EMBL; U83330; AAC59473.1; -; Genomic_DNA.
DR   EMBL; L33180; AAC63755.1; -; Genomic_DNA.
DR   PIR; T41826; T41826.
DR   RefSeq; NP_047486.1; NC_001962.1.
DR   CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR   GeneID; 1488701; -.
DR   KEGG; vg:1488701; -.
DR   Proteomes; UP000204315; 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; 1.
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; Repeat;
KW   Signal; Virion; Zinc; Zinc-finger.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..839
FT                   /note="Capsid-associated protein Vp91"
FT                   /id="PRO_0000045465"
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   REGION          624..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        666..688
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        613
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        619
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   VARIANT         107
FT                   /note="I -> T (in strain: T3)"
FT   VARIANT         127
FT                   /note="D -> E (in strain: T3)"
FT   VARIANT         202
FT                   /note="A -> R (in strain: T3)"
FT   VARIANT         217..219
FT                   /note="KTR -> ETS (in strain: T3)"
FT   VARIANT         295
FT                   /note="S -> T (in strain: T3)"
FT   VARIANT         320
FT                   /note="S -> L (in strain: T3)"
FT   VARIANT         331
FT                   /note="R -> K (in strain: T3)"
FT   VARIANT         370
FT                   /note="E -> D (in strain: T3)"
FT   VARIANT         379
FT                   /note="N -> S (in strain: T3)"
FT   VARIANT         468
FT                   /note="N -> D (in strain: T3)"
FT   VARIANT         599
FT                   /note="P -> S (in strain: T3)"
FT   VARIANT         638
FT                   /note="Q -> R (in strain: T3)"
FT   VARIANT         644
FT                   /note="P -> S (in strain: T3)"
FT   VARIANT         665
FT                   /note="A -> V (in strain: T3)"
FT   VARIANT         678..681
FT                   /note="Missing (in strain: T3)"
FT   VARIANT         740
FT                   /note="S -> L (in strain: T3)"
FT   VARIANT         766
FT                   /note="G -> E (in strain: T3)"
FT   VARIANT         803
FT                   /note="D -> G (in strain: T3)"
FT   VARIANT         816
FT                   /note="D -> N (in strain: T3)"
FT   VARIANT         838
FT                   /note="I -> V (in strain: T3)"
SQ   SEQUENCE   839 AA;  95764 MW;  E4CC688BC53B050C CRC64;
     MMSGVMLLVF AIFLIIAFTL IYLAIYFKFD ETTYTKRLQV MIEYIKRTNA DEPTPNVIGY
     VSDITQNTYT VTWFNTVDLS TYQESVHDDR NEIFDFLNQK LQPVDRIVHD RVRANDENPN
     EFILSGDKDD VTMKCPAYFN FDYAQLKCVP VPPCDNKPAG RYPMDERLLD TLVLNQHLDK
     DYSSNEHLYH PTFYLRCFAN GAHAVEECPD NYTFDAKTRQ CKVNELCENR PDGYILSYFP
     SNLLVNQFMQ CVSGRHVVRE CPANKIFDRN LMSCVEAHPC TFNGAGHTYI TADISDAQYF
     KCLNNNESQL MTCINRIRNS DNQYECSGDS RCIDLPNGTG QQVFKHADDD ISYNSGQLVC
     DNFEIISNIE CDQSNVFENK LFMDKFRLNM QFPTEVFDGT ACVPATADNV NFLRSTFAIE
     NIPNHYDIDM QTSMLGKIEM IKQLVSKDLS LNNDAIFAQW LLYARDKNAI GLNPLTGEPI
     DCFGNNLYDV FDARRANVCK DLGKSVLKTL NFGDGEFLNV LSDTLTGKDE DYRQFCAISY
     ENGQKIVENE HFQRRILTNI LQSDVCANIY TTLYQKYTTL NPKYTTTPLQ YNRILVKRPK
     NIEIYGANTR LKNATIPKNA TTISPVFNPF ENQPNNRQND SISPLFNPFQ TTDAVWYSEP
     DGDEAVAPPP TAPPPPSEPE PEPEPELPSP LILDNKDLFY SCHYSVPFFK LTSCHAENDV
     IINALNELRN NVKVDADCES AKDLSHVLNA YAYVGNGIGC RSAYDGDAIV VKKEAVPSHV
     YANLNTQSND GVKYNRWLHV KNDQYMACPE ELYDNDEFKC NVESDKLYYL DNLQEDSIV
 
 
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