053R_FRG3G
ID 053R_FRG3G Reviewed; 522 AA.
AC Q6GZS3;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 02-JUN-2021, entry version 40.
DE RecName: Full=Putative myristoylated protein 053R;
GN ORFNames=FV3-053R;
OS Frog virus 3 (isolate Goorha) (FV-3).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Pimascovirales; Iridoviridae; Alphairidovirinae; Ranavirus.
OX NCBI_TaxID=654924;
OH NCBI_TaxID=30343; Dryophytes versicolor (chameleon treefrog).
OH NCBI_TaxID=8404; Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OH NCBI_TaxID=45438; Lithobates sylvaticus (Wood frog) (Rana sylvatica).
OH NCBI_TaxID=8316; Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15165820; DOI=10.1016/j.virol.2004.02.019;
RA Tan W.G., Barkman T.J., Gregory Chinchar V., Essani K.;
RT "Comparative genomic analyses of frog virus 3, type species of the genus
RT Ranavirus (family Iridoviridae).";
RL Virology 323:70-84(2004).
RN [2]
RP FUNCTION.
RX PubMed=20633916; DOI=10.1016/j.virol.2010.06.034;
RA Whitley D.S., Yu K., Sample R.C., Sinning A., Henegar J., Norcross E.,
RA Chinchar V.G.;
RT "Frog virus 3 ORF 53R, a putative myristoylated membrane protein, is
RT essential for virus replication in vitro.";
RL Virology 405:448-456(2010).
CC -!- FUNCTION: May play a critical role in virion formation. Essential for
CC virus replication in vitro. {ECO:0000269|PubMed:20633916}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; AY548484; AAT09712.1; -; Genomic_DNA.
DR RefSeq; YP_031631.1; NC_005946.1.
DR GeneID; 2947832; -.
DR KEGG; vg:2947832; -.
DR Proteomes; UP000008770; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR003472; Virion_mem_poxvirus_L1.
DR Pfam; PF02442; L1R_F9L; 1.
PE 3: Inferred from homology;
KW Host membrane; Lipoprotein; Membrane; Myristate; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..522
FT /note="Putative myristoylated protein 053R"
FT /id="PRO_0000410511"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 503..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 522 AA; 54728 MW; C36F70EF7FE29FAA CRC64;
MGAAESINTV NIVTKAYAKI MTTMVTDQDI TADQSQVFSI DHVKGDVVIK GDVFTQMLVI
NLASLMKAIA TQSAQDQLID NIAQQAQAAV SGLNLAQYAY VSNNIDRLIT ACVQMSTDMR
VSCKSKVTMT QSFSVTDVEG DVRVTGVKFN QFANILSSCA MDASVNNDQA RDIVSQIKQR
GDAKASGLDP TTLIVIIVLV MVGAPMGAGF MAGRRAIGPL LASVGLIGGG AVALGYVPRP
VKIEGFSSDP DFTLAQPAAT VKGLTFTAAV AKLKSTDGYG ALFWKNYDVK GTTAVKLQET
LSYFAPAGYD PASWAGVGDS APPFRIFPGL YQGKGDPGAR PRAAYGYAGP VAGPKKGDAY
LDGDTGSYYV LGDSWKMRGT ISGHQNGRTD YWGTVDPTTT AALTGSERYI WVDPFTLVKS
TVWLFTGSPK KWTQQQTAPL DIPLTNTPSD FNVWVYKDDT AVQAVKWSSV GAGVAGAALT
ASALLMPDSV ASSEMSPAVG TGTPAIGTGS PAVGTGFPAH RG