VF475_ASFM2
ID VF475_ASFM2 Reviewed; 486 AA.
AC Q8V9T2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Uncharacterized protein B475L;
DE Short=pB475L;
GN OrderedLocusNames=Mal-085; ORFNames=L09NL;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Roberts P.C., Lu Z., Rock D.L.;
RT "Nucleotide sequence and analysis of 16.25 kilobase pairs of the African
RT swine fever virus genome that span the central variable region.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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:0000305}.
CC -!- SIMILARITY: Belongs to the asfivirus B475L family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL31331.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL31331.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L00966; AAL31331.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; Q8V9T2; -.
DR Proteomes; UP000000860; 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 3: Inferred from homology;
KW Coiled coil; Glycoprotein; Host membrane; Late protein; Membrane;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..486
FT /note="Uncharacterized protein B475L"
FT /id="PRO_0000373697"
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 299..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 183..233
FT /evidence="ECO:0000255"
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 461
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 41
FT /note="E -> G (in Ref. 1; AAL31331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 57745 MW; 6A5AEAFDA4749794 CRC64;
MDQEESHVIS IFETVGAYFI NIFYNFLYKN ALYKKHSIVM EYQYQVKGYI LGVKQNKKLY
EKMLDSFYKY FCNITQINSK TLNFSNFVST IVDSFLPKEY SQSISLEKKD SILELLLCDY
ISNLGTFITT EKMLPFIVKN RKENYHKVTK EMQDYSLTFL LKKRMELYNK FLRKQAYVEP
ETELEETYAR LSSYNRSLLY QIEELTSEKK SFLEELSTLR KKYEKRQSEY RRLVQLLYQQ
IQRSSSSKTS YPLTKFIETL PSEHFSNEEY QKEASADQKV ILREQEETEL LREQELLASQ
EVTSKSPNNY PVPQSRTIVN KPSDNYPVPR SRSTKIDFDN SLQKQELHAK NGFSEKAIVE
FNQDKQPMFK EEAIVEFNQD KPEIKEETIV EFNQNKQPMF KEEAILEFNQ DKQPEFKETI
LDNKEILDNK EDILEEENQD EPIVQNPFLE NFWKPEQKTF NQSGLFEESS DFSNDWSGGD
VTLNFS