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Database: UniProt
Entry: Q06670
LinkDB: Q06670
Original site: Q06670 
ID   VP91_NPVAC              Reviewed;         847 AA.
AC   Q06670;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   14-MAY-2014, entry version 63.
DE   RecName: Full=Capsid-associated protein Vp91;
DE   Flags: Precursor;
GN   Name=p95; ORFNames=ORF83;
OS   Autographa californica nuclear polyhedrosis virus (AcMNPV).
OC   Viruses; dsDNA viruses, no RNA stage; Baculoviridae; Alphabaculovirus.
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
RT   polyhedrosis virus.";
RL   Virology 202:586-605(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=E2;
RX   PubMed=8126447;
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
RT   unit 47 to 52.5) of Autographa californica nuclear polyhedrosis virus
RT   fragment EcoRI-C.";
RL   J. Gen. Virol. 75:487-494(1994).
CC   -!- FUNCTION: Probable capsid-associated protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Virion (By similarity). Note=In virions,
CC       associates with the capsid and maybe also with the envelope
CC       surrounding the capsid (By similarity).
CC   -!- SIMILARITY: Contains 2 chitin-binding type-2 domains.
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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   CAZy; CBM14; Carbohydrate-Binding Module Family 14.
DR   GeneID; 1403916; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0006030; P:chitin metabolic process; IEA:InterPro.
DR   Gene3D; 2.170.140.10; -; 1.
DR   InterPro; IPR013682; BaculoV_Vp91_N.
DR   InterPro; IPR002557; Chitin-bd_dom.
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; 2.
PE   3: Inferred from homology;
KW   Chitin-binding; Complete proteome; Disulfide bond; Glycoprotein;
KW   Repeat; Signal; Virion.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    847       Capsid-associated protein Vp91.
FT                                /FTId=PRO_0000036751.
FT   DOMAIN      151    221       Chitin-binding type-2 1.
FT   DOMAIN      224    282       Chitin-binding type-2 2.
FT   COMPBIAS    671    698       Pro-rich.
FT   CARBOHYD    156    156       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    211    211       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    306    306       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    337    337       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    500    500       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    592    592       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    613    613       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   CARBOHYD    639    639       N-linked (GlcNAc...); by host
FT                                (Potential).
FT   DISULFID    208    221       By similarity.
FT   DISULFID    261    274       By similarity.
FT   CONFLICT    202    202       A -> T (in Ref. 2; CAA50547).
FT   CONFLICT    328    328       G -> D (in Ref. 2; CAA50547).
FT   CONFLICT    433    433       S -> T (in Ref. 2; CAA50547).
FT   CONFLICT    469    469       A -> T (in Ref. 2; CAA50547).
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
//
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