ID   VP91_NPVCF              Reviewed;         833 AA.
AC   Q7TLR9;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Capsid-associated protein Vp91;
DE   Flags: Precursor;
GN   ORFNames=ORF78;
OS   Choristoneura fumiferana nuclear polyhedrosis virus (CfMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=208973;
OH   NCBI_TaxID=7141; Choristoneura fumiferana (Spruce budworm moth) (Archips fumiferana).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15784887; DOI=10.1099/vir.0.80490-0;
RA   de Jong J.G., Lauzon H.A.M., Dominy C., Poloumienko A., Carstens E.B.,
RA   Arif B.M., Krell P.J.;
RT   "Analysis of the Choristoneura fumiferana nucleopolyhedrovirus genome.";
RL   J. Gen. Virol. 86:929-943(2005).
CC   -!- FUNCTION: Probable capsid-associated protein.
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}.
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; AF512031; AAP29860.1; -; Genomic_DNA.
DR   RefSeq; NP_848389.1; NC_004778.3.
DR   SMR; Q7TLR9; -.
DR   CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR   GeneID; 1482718; -.
DR   KEGG; vg:1482718; -.
DR   Proteomes; UP000204418; 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; Repeat;
KW   Signal; Virion; Zinc; Zinc-finger.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..833
FT                   /note="Capsid-associated protein Vp91"
FT                   /id="PRO_0000045466"
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          647..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
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        588
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   DISULFID        207..220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
FT   DISULFID        260..273
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00144"
SQ   SEQUENCE   833 AA;  93127 MW;  E5FFD87A2D9D5B80 CRC64;
     MSGVVLLVLA IILITIFSLI YYTIFFEFDE TTFSKRLRVL TEYAKRTNAD KPTPDVLGHV
     SDVYDHTYIV SWFRTNDLST YHETVHDDTV EVFDFLEQQF SGAQATVTQR VAPVAAELDA
     FVVTNDAGDV KLRCPQNFSF DYGQLKCVPE DPCSGRPPGR YPMNELLLDT LVHNQHSDKN
     YSAGAHLYHP TLYLRCLANG SHAVRECPDN YTFDAEAGEC RVNELCEGRP DGFVLPYFPE
     ALLVNEFVEC RNGEHVVAQC ADGQVFDRAL MTCVHAHPCA FNGAGHTYIT SDIGDTQFFK
     CLNNHEAQLV TCINRAHGAD GQYACSGDAR CADLPKGTGQ LVHIHTDDTF EYASGQMICD
     NYEVVSEINC DTGDVLGDKL FINKFKLNVQ FPLEVLEFGA CAPATLNNVS VLNDTFPIEN
     APNDYGVNMQ TSVVGRTSMV AKLMAGDDPD TAFGENVLLA RDVNTVGLNP FTAEPIDCFG
     AQLYDVMDAH RANVCTESGN DLLKTVEFGD GAFLSVFRDD LTGSDADYKQ FCAISYESPL
     KIVKSDHFQR RILTNILQSD ICADLYTTIY QKYTTLARKY TTSPVQYNYT FVKRPENMVV
     YAKNTRFKNA TISEPAFDLF AAQTTDKENG FARSLFDPFA DGVWRSEPGG DGDHWAPEVP
     PTQPEPELEP ESETELDSDL ELEPEFSPLI LNKKDLFYSC FYELPSFKLS SCHAENDVIV
     DALQQLRASV KVDTECELAK DLHFVLNAYA YTGNNIGCRS VFDGDDVAVV KEPVPSYVFT
     NLQTQSNDGV RYNKHVHVKD GRYMACPEHL YDDEAFACNA EPDKLYYLEN MQQ