ID   VP91_NPVOP              Reviewed;         819 AA.
AC   O10336;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Capsid-associated protein Vp91;
DE   Flags: Precursor;
GN   Name=p91; ORFNames=ORF86;
OS   Orgyia pseudotsugata multicapsid polyhedrosis virus (OpMNPV).
OC   Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX   NCBI_TaxID=262177;
OH   NCBI_TaxID=33414; Orgyia pseudotsugata (Douglas-fir tussock moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9126251; DOI=10.1006/viro.1997.8448;
RA   Ahrens C.H., Russell R.R., Funk C.J., Evans J., Harwood S., Rohrmann G.F.;
RT   "The sequence of the Orgyia pseudotsugata multinucleocapsid nuclear
RT   polyhedrosis virus genome.";
RL   Virology 229:381-399(1997).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9201231; DOI=10.1006/viro.1997.8599;
RA   Russell R.L.Q., Rohrmann G.F.;
RT   "Characterization of P91, a protein associated with virions of an Orgyia
RT   pseudotsugata baculovirus.";
RL   Virology 233:210-223(1997).
CC   -!- FUNCTION: Probable capsid-associated protein.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:9201231}. Note=In
CC       virions, associates with the capsid and maybe also with the envelope
CC       surrounding the capsid.
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DR   EMBL; U75930; AAC59085.1; -; Genomic_DNA.
DR   RefSeq; NP_046242.1; NC_001875.2.
DR   CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR   GeneID; 912002; -.
DR   KEGG; vg:912002; -.
DR   Proteomes; UP000009248; 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; 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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..819
FT                   /note="Capsid-associated protein Vp91"
FT                   /id="PRO_0000036752"
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          650..671
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        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   CARBOHYD        752
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   819 AA;  91067 MW;  108942AF0A8F925A CRC64;
     MSDVVLLVLA IILITIFTLI YYTIFFEFDE TTFSKRLQVL TEYAKRTNAD KPTPDVLGHV
     SDVYDHTYIV SWFKTDDLST YHETVHDDTV EVFDFLEQRF AAAAAAVAHR VAPLAAEPDA
     FVVTGDAGDV KLRCPQHFRF DYDQLKCVPV DPCAGRAPGR YPMDERLLDT LVHNQPSDKD
     YSAGEHLHHP TLYLRCLADG SHAVRECPDN YTFDAASGEC RVNELCEGRP DGFVLAYFPE
     TLRVNEFVEC RGGKHVVARC PDQQVFDRAL MTCVQTHPCA FNGAGHTYIT ADIGDAQFFK
     CLNDREAQLI TCINRVRGAD GQYACSGDAR CADLPDGTGR LMHTHTDDTF EYVSGQTICD
     NYNVISEIEC DTGNVLENKL FVNKFTLGAQ FPREVLDAGV CAPATLNNVR VLSDAFPVEN
     LPNDYKVDMQ TSVVGLATMM ADLTTGADPD TAFGQNVLLA REVDAVGLSP LTAESIDCFG
     ARLFDVMDAR RANVCTESGG DLLRTIEFGD GAFLSVFRDD LTGSDADYKQ FCAISYESPL
     KIVNSDHFER RILANILQAD ICAELYTTIY QKYTTLARKY TTASPKYNYT FVKRPPNIVV
     YAENTHLKNS TISVPTFDPF APQPADNKIG PTNALFDPFA DRVWRSEPGG DGDHWAPEAP
     PTQPEAPPAP EPSPLILDKK ELFYSCYYEL PTFKLTSCHA ENDVIIDALQ QLRAAVEVDP
     GCEPAKDLHF VLNAYAYMGN GVGCRSVFDG NNVTVIKEPV PTYTFNNLQT QSDDGVRYNK
     HVHVKDGRYM ACPEHLYDGA AFACNAEPDK LYYLDNMQK