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VF475_ASFB7
ID   VF475_ASFB7             Reviewed;         475 AA.
AC   Q65167;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 60.
DE   RecName: Full=Uncharacterized protein B475L;
DE            Short=pB475L;
GN   OrderedLocusNames=Ba71V-077; ORFNames=B475L;
OS   African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus.
OX   NCBI_TaxID=10498;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA   Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA   Rodriguez J.F., Vinuela E.;
RT   "Analysis of the complete nucleotide sequence of African swine fever
RT   virus.";
RL   Virology 208:249-278(1995).
RN   [2]
RP   INDUCTION.
RX   PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA   Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA   Dixon L., Werner F.;
RT   "The African Swine Fever Virus Transcriptome.";
RL   J. Virol. 94:0-0(2020).
CC   -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:32075923}.
CC   -!- SIMILARITY: Belongs to the asfivirus B475L family. {ECO:0000305}.
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DR   EMBL; U18466; AAA65307.1; -; Genomic_DNA.
DR   RefSeq; NP_042771.1; NC_001659.2.
DR   SMR; Q65167; -.
DR   GeneID; 22220307; -.
DR   KEGG; vg:22220307; -.
DR   Proteomes; UP000000624; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Coiled coil; Glycoprotein; Host membrane; Late protein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..475
FT                   /note="Uncharacterized protein B475L"
FT                   /id="PRO_0000373695"
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          295..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          183..233
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        295..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        450
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        460
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   475 AA;  56068 MW;  682FCB97CBC13D8F CRC64;
     MDQEESHVIS IFETLGAYFI NIFYNFLYKN ALYKKHSIVT EYQYQVKGYI LGVKQNKKLY
     EKMLDSFYKY FCNITQINSK TLNFSNFITT IVDSFIPKEY SQSISLEKKE SILELLLCDY
     ISNLGTFITT EKMLPFIIKN RKENYHKVTK EMQDYSLTFL LKKRMELYNK FLRKQAYVEP
     ETELEETYAR LSSYNRSLLH QIEELTSEKK SLLADLSTLR KKYEKRQSEY RRLVQLLYQQ
     IQRSSTSKSS YPLTKFIETL PSEHFSNEEY QKETPADQKE VVEMELLRKQ ELLTSQELTS
     KSPNNYPVPH SRTIVSKPPD NYPVPRSRTT TKLDFDNSLQ NQELHTKNGF SEKDIVEFGQ
     DKPEEENILA IDQDKPEEEN ILAIKQDIPE EENILAIDQD KPEFNQDTPE FKEAVLDTKE
     NILEEENQDE PIVQNPFLEN FWKPEQKTFN QSGLFEESSN FSNDWSGGDV TLNFS
 
 
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