ID   VP91_NPVEP              Reviewed;         826 AA.
AC   Q91GH8;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Capsid-associated protein Vp91;
DE   Flags: Precursor;
GN   ORFNames=ORF75;
OS   Epiphyas postvittana nucleopolyhedrovirus (EppoMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=70600;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11907346; DOI=10.1099/0022-1317-83-4-957;
RA   Hyink O., Dellow R.A., Olsen M.J., Caradoc-Davies K.M.B., Drake K.,
RA   Herniou E.A., Cory J.S., O'Reilly D.R., Ward V.K.;
RT   "Whole genome analysis of the Epiphyas postvittana nucleopolyhedrovirus.";
RL   J. Gen. Virol. 83:957-971(2002).
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; AY043265; AAK85639.1; -; Genomic_DNA.
DR   RefSeq; NP_203244.1; NC_003083.1.
DR   CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR   GeneID; 1727387; -.
DR   KEGG; vg:1727387; -.
DR   Proteomes; UP000203221; 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   SMART; SM00494; ChtBD2; 2.
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;
KW   Reference proteome; Repeat; Signal; Virion; Zinc; Zinc-finger.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..826
FT                   /note="Capsid-associated protein Vp91"
FT                   /id="PRO_0000045467"
FT   DOMAIN          223..281
FT                   /note="Chitin-binding type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   ZN_FING         147..196
FT                   /note="C2HC BV-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01148"
FT   REGION          651..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        520
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        609
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        722
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        207..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        260..273
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ   SEQUENCE   826 AA;  93452 MW;  B2B50863B4F375A9 CRC64;
     MSDVVLLVLA IIFIIIFVLI YCTIFFEFDE TTFSKRLHVL TEYAKRTNAE HPTPDVLGHV
     SDVYEHTYIV TWFNTNDLSV YHETVHDDTI EVFDFLEQKF SPAKSTVAQR VAPSASDPNA
     FVLTGDKSEV KMHCPQHFNF DYNQLKCVPI NPCDTRAPGL YAMDEHLLDA LVHSQHLDKD
     YTINAHLQHP TLYLRCLADG SYVVQECPDN YTFDAATSEC KVNELCQGRP DGYVLDYFPE
     TLLVNEFVEC YESKHVVKQC PEQHVFDRQL MTCVQAHPCA FNGAGHTYIT ADIGDTQYFE
     CLNNQESQLI TCINRVRNTD GQYACSGDAR CANLTDGTGQ LVHMHVDDTF EYASGQLVCD
     NFEVISEIDC NTSDVLTNML FLQKFKLETE FPRQVFDNGE CVPATFNNVR VLNDTFPIQN
     VPNDYNIDMQ TSIIGLTDMI PKLLAGDDLD DTFGQNVVLA RDVGAVGLNP VTAEPIDCLG
     TQLFDVLDAS RANICTESGD GVLKTLKFEN GTFLSVFRDN LTGSDIDYKR FCAISYENSL
     KIVKSDHFER RILTNILQSD VCADLYTTMY QKYTTLARKY TTTPFQYTYT FVKPPPNIVV
     YAKNIQLKNA TISKPAFDPF ANKQIDNKNN LAKPLFDPFK NAVWYSEPDG GDGDHWGPDL
     PPPVQPDSEP DESEPEPEVS PLILDKKDLF YSCYYELPSF KLTSCYAEND VIIDAITDLR
     NNVTVDAECE PAKDLHYVLN AYAYTGNGVG CRSVFNDDGV AVIKEPIPSY VFANLNTQSN
     DGVHYNRHVH VKDGRYMACP DHLYDDVEFR CNVEADKLYY LDNMQF