ID U3SYM3_MCFA Unreviewed; 587 AA.
AC U3SYM3;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
GN Name=NS3 {ECO:0000313|EMBL:BAN83986.1};
OS Mosquito cell fusing agent (CFA flavivirus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Flavivirus.
OX NCBI_TaxID=31658 {ECO:0000313|EMBL:BAN83986.1};
OH NCBI_TaxID=7158; Aedes.
RN [1] {ECO:0000313|EMBL:BAN83986.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NS3-175_08 {ECO:0000313|EMBL:BAN83986.1};
RA Yamanaka A., Thongrungkiat S., Ramasoota P., Konishi E.;
RT "Genetic and evolutionary analysis of cell-fusing agent virus based on Thai
RT strains isolated in 2008 and 2012.";
RL Infect. Genet. Evol. 19:188-194(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of
CC the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.;
CC EC=3.4.21.91; Evidence={ECO:0000256|ARBA:ARBA00024468};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001491};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004153}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; AB813779; BAN83986.1; -; Genomic_RNA.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR011492; Flavi_DEAD.
DR InterPro; IPR001850; Flavi_NS3_S7.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR Pfam; PF20907; Flav_NS3-hel_C; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF00949; Peptidase_S7; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT DOMAIN 1..179
FT /note="Peptidase S7"
FT /evidence="ECO:0000259|PROSITE:PS51528"
FT DOMAIN 176..329
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAN83986.1"
FT NON_TER 587
FT /evidence="ECO:0000313|EMBL:BAN83986.1"
SQ SEQUENCE 587 AA; 65400 MW; 697D9F0B9DED4707 CRC64;
SDDLLGLGGP IEADLQTSFQ DIPNGVYRIV VRSLFGDRQR GAGFSKNGVF HTLMHVTRGE
PVKWRGRAVV PHSGSALRDV VSYGGPWQLD TPTTTDDLVL MACKPDKTIE YHRYRPGVMS
IDGEPVMFIS DDFGKGSSGS PFFINGEPVG FYGFGFYVNG IYRSTVAGGK PSDVTENLDC
DSTRRFVTWH PGKGKTRKVI VEETKKNYDS NQRTVILTPT RVVMAEVVEA LKNSGMKSDK
NLSYCTRNLI TVACHATFTK FVLSHGVKKV RVAMIIMDEC HFMDPMSIAA RGVMEYLHNQ
GTKLIYLSAT PPGHAPDVGS NYAISDQSIS FPTWLSPSWI GNVQKSVGAK KTILFVPSHN
QANTLASAIP GSVPLHRANF STNYAQAGDA ATALVISTDI SEMGANLGVD LVIDTRRALR
PLVDSATRVK LVETNITTSS MIQRRGRTGR REPGTYVYPI DSQTEENPVS WVCWPEAQMI
LDQLGMTFML EEAAYSQPPG RFTLVGEDRM RFSKLMDRDD IPIWLAWHWA EAGDRRHSAL
FQGEGTGKII ENRFGKQEYR PQYVDDRFES IEWETRKVSI DFYMNCR
//