Sequence of POLG_KUNJM
EC Number:2.1.1.56
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
Other sequences found for EC No. 2.1.1.56
General information:
Sequence
0 MSKKPGGPGK SRAVNMLKRG MPRVLSLTGL KRAMLSLIDG RGPTRFVLAL LAFFRFTAIA
60 PTRAVLDRWR SVNKQTAMKH LLSFKKELGT LTSAINRRSS KQKKRGGKTG IAFMIGLIAG
120 VGAVTLSNFQ GKVMMTVNAT DVTDIITIPP AAGKNLCIVR AMDVGHMCDD TITYECPVLS
180 AGNDPEDIDC WCTKLAVYVR YGRCTKTRHS RRSRRSLTVQ THGESTLSNK KGAWMDSTKA
240 TRYLVKTESW ILRNPGYALV AAVIGWMLGS NTMQRVVFAV LLLLVAPAYS FNCLGMSNRD
300 FLEGVSGATW VDLVLEGDSC VTIMSKDKPT IDVKMMNMEA ANLAEVRSYC YLATVSELST
360 KAACPTMGEA HNDKRADPSF VCKQGVVDRG WGNGCGLFGK GSIDTCAKFA CSTKATGRTI
420 LKENIKYEVA IFVHGPTTVE SHGNYFTQTG AAQAGRFSIT PAAPSYTLKL GEYGEVTVDC
480 EPRSGIDTSA YYVMTVGTKT FLVHREWFMD LNLPWSSAES NVWRNRETLM EFEEPHATKQ
540 SVIALGSQEG ALHQALAGAI PVEFSSNTVK LTSGHLKCRV KMEKLQLKGT TYGVCSKAFR
600 FLGTPADTGH GTVVLELQYT GTDGPCKIPI SSVASLNDLT PVGRLVTVNP FVSVSTANAK
660 VLIELEPPFG DSYIVVGRGE QQINHHWHKS GSSIGKAFTA TLKGAQRLAA LGDTAWDFGS
720 VGGVFTSVGK AVHQVFGGAF RSLFGGMSWI TQGLLGALLL WMGINARDRS IALTFLAVGG
780 VLLFLSVNVH ADTGCAIDIS RQELRCGSGV FIHNDVEAWI DRYKYYPETP QGLAKIIQKA
840 HKEGVCGLRS VSRLEHQMWE AVKDELNTLL KENGVDLSIV VEKQEGMYKS APRRLTATTE
900 KLEIGWKAWG KSILFAPELA NNTFVIDGPE TKECPTQNRA WNNLEVEDFG FGLTSTRMFL
960 RVRESNTTEC DSKIIGTAVK NNLAIHSDLS YWIESRFNDT WKLERAVLGE VKSCTWPETH
1020 TLWGDGVLES DLIIPITLAG PRSNHNRRPG YKTQSQGPWD EGRVEIDFDY CPGTTVTLSE
1080 SCGHRGPATR TTTESGKLIT DWCCRSCTLP PLRYQTDNGC WYGMEIRPQR HDEKTLVQSQ
1140 VNAYNADMID PFQLGLLVVF LATQEVLRKR WTAKISMPAI LIALLVLVFG GITYTDVLRY
1200 VILVGAAFAE SNSGGDVVHL ALMATFKIQP VFMVASFLKA RWTNQENILL MLAAAFFQMA
1260 YYDARQILLW EMPDVLNSLA VAWMILRAIT FTTTSNVVVP LLALLTPGLR CLNLDVYRIL
1320 LLMVGIGSLI REKRSAAAKK KGASLLCLAL ASTGFFNPMI LAAGLVACDP NRKRGWPATE
1380 VMTAVGLMFA IVGGLAELDI DSMAIPMTIA GLMFAAFVIS GKSTDMWIER TADISWEGDA
1440 EITGSSERVD VRLDDDGNFQ LMNDPGAPWK IWMLRMACLA ISAYTPWAIL PSVVGFWITL
1500 QYTKRGGVLW DTPSPKEYKR GDTTTGVYRI MTRGLLGSYQ AGAGVMVEGV FHTLWHTTKG
1560 AALMSGEGRL DPYWGSVKED RLCYGGPWKL QHKWNGQDEV QMIVVEPGKN VKNVQTKPGV
1620 FKTPEGEIGA VTLDFPTGTS GSPIVDKNGD VIGLYGNGVI MPNGSYISAI VQGERMDEPV
1680 PAGFEPEMLR KKQITVLDLH PGAGKTRRIL PQIIKEAINR RLRTAVLAPT RVVAAEMAEA
1740 LRGLPIRYQT SAVAREHNGN EIVDVMCHAT LTHRLMSPHR VPNYNLFVMD EAHFTDPASI
1800 AARGYISTRV ELGEAAAIFM TATPPGTSDP FPESNAPISD LQTEIPDRAW NSGYEWITEY
1860 IGKTVWFVPS VKMGNEIALC LQRAGKKVIQ LNRKSYETEY PKCKNDDWDF VVTTDISEMG
1920 ANFKASRVID SRKSVKPTII TEGEGRVILG EPSAVTAASA AQRRGRTGRN PSQAGDEYCY
1980 GGHTNEDDSN CAHWTEARIM LDNINMPNGL IAQFYQPERE KVYTMDGEYR LRGEERKNFL
2040 ELLRTADLPV WLAYKVAAAG VSYHDRRWCF DGPRTNTILE DNNEVEVITK LGERKILRPR
2100 WIDARVYSDH QALKSFKDFA SGKRSQIGFI EVLGKMPEHF MGKTWEALDT MYVVATAEKG
2160 GRAHRMALEE LPDALQTIAL IALLSVMTMG VFFLLMQRKG IGKIGLGGVV LGAATFFCWM
2220 AEVPGTKIAG MLLLSLLLMI VLIPEPEKQR SQTDNQLAVF LICVLTLVGA VAANEMGWLD
2280 KTKSDISGLF GQRIETKENF SIGEFLLDLR PATAWSLYAV TTAVLTPLLK HLITSDYITT
2340 SLTSINVQAS ALFTLARGFP FVDVGVSALL LAAGCWGQVT LTVTVTSATL LFCHYAYMVP
2400 GWQAEAMRSA QRRTAAGIMK NAVVDGIVAT DVPELERTTP IMQKKVGQVM LILVSLAALV
2460 VNPSVKTVRE AGILITAAAV TLWENGASSV WNATTAIGLC HIMRGGWLSC LSITWTLVKN
2520 MEKPGLKRGG AKGRTLGEVW KERLNQMTKE EFIRYRKEAI TEVDRSAAKH ARKERNITGG
2580 HPVSRGTAKL RWLVERRFLE PVGKVIDLGC GRGGWCYYMA TQKRVQEVRG YTKGGPGHEE
2640 PQLVQSYGWN IVTMKSGVDV FYRPSECCDT LLCDIGESSS SAEVEEHRTL RVLEMVEDWL
2700 HRGPKEFCVK VLCPYMPKVI EKMELLQRRY GGGLVRNPLS RNSTHEMYWV SRASGNVVHS
2760 VNMTSQVLLG RMEKKTWKGP QYEEDVNLGS GTRAVGKPLL NSDTSKIKNR IERLRREYSS
2820 TWHHDENHPY RTWNYHGSYE VKPTGSASSL VNGVVRLLSK PWDTITNVTT MAMTDTTPFG
2880 QQRVFKEKVD TKAPEPPEGV KYVLNETTNW LWAFLAREKR PRMCSREEFI RKVNSNAALG
2940 AMFEEQNQWR SAREAVEDPK FWEMVDEERE AHLRGECHTC IYNMMGKREK KPGEFGKAKG
3000 SRAIWFMWLG ARFLEFEALG FLNEDHWLGR KNSGGGVEGL GLQKLGYILR EVGTRPGGRI
3060 YADDTAGWDT RITRADLENE AKVLELLDGE HRRLARAIIE LTYRHKVVKV MRPAADGRTV
3120 MDVISREDQR GSGQVVTYAL NTFTNLAVQL VRMMEGEGVI GPDDVEKLTK GKGPKVRTWL
3180 SENGEERLSR MAVSGDDCVV KPLDDRFATS LHFLNAMSKV RKDIQEWKPS TGWYDWQQVP
3240 FCSNHFTELI MKDGRTLVTP CRGQDELVGR ARISPGAGWN VRDTACLAKS YAQMWLLLYF
3300 HRRDLRLMAN AICSAVPVNW VPTGRTTWSI HAGGEWMTTE DMLEVWNRVW IEENEWMEDK
3360 TPVEKWSDVP YSGKREDIWC GSLIGTRARA TWAENIQVAI NQVRSIIGDE KYVDYMSSLK
3420 RYEDTTLVED TVL
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
76811
Coia G.,Parker M.D.,Speight G.,Byrne M.E.,Westaway E.G.
Nucleotide and complete amino acid sequences of Kunjin virus: definitive gene order and characteristics of the virus-specified proteins.
J. Gen. Virol.
69
1-21
1988
76812
Liu W.J.,Chen H.B.,Khromykh A.A.
Molecular and functional analyses of Kunjin virus infectious cDNA clones demonstrate the essential role for NS2A in virus assembly and for a nonconservative residue in NS3 in RNA replication.
J. Virol.
77
7804-7813
2003
76813
Mackenzie J.M.,Khromykh A.A.,Jones M.K.,Westaway E.G.
Subcellular localization and some biochemical properties of the flavivirus Kunjin nonstructural proteins NS2A and NS4A.
Virology
245
203-215
1998
76814
Liu W.J.,Chen H.B.,Wang X.J.,Huang H.,Khromykh A.A.
Analysis of adaptive mutations in Kunjin virus replicon RNA reveals a novel role for the flavivirus nonstructural protein NS2A in inhibition of beta interferon promoter-driven transcription.
J. Virol.
78
12225-12235
2004
76815
Liu W.J.,Wang X.J.,Mokhonov V.V.,Shi P.Y.,Randall R.,Khromykh A.A.
Inhibition of interferon signaling by the New York 99 strain and Kunjin subtype of West Nile virus involves blockage of STAT1 and STAT2 activation by nonstructural proteins.
J. Virol.
79
1934-1942
2005
76816
Guo J.T.,Hayashi J.,Seeger C.
West Nile virus inhibits the signal transduction pathway of alpha interferon.
J. Virol.
79
1343-1350
2005
76817
Liu W.J.,Wang X.J.,Clark D.C.,Lobigs M.,Hall R.A.,Khromykh A.A.
A single amino acid substitution in the West Nile virus nonstructural protein NS2A disables its ability to inhibit alpha/beta interferon induction and attenuates virus virulence in mice.
J. Virol.
80
2396-2404
2006
76818
Roosendaal J.,Westaway E.G.,Khromykh A.,Mackenzie J.M.
Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein.
J. Virol.
80
4623-4632
2006
76819
Leung J.Y.,Pijlman G.P.,Kondratieva N.,Hyde J.,Mackenzie J.M.,Khromykh A.A.
Role of nonstructural protein NS2A in flavivirus assembly.
J. Virol.
82
4731-4741
2008
76820
Laurent-Rolle M.,Boer E.F.,Lubick K.J.,Wolfinbarger J.B.,Carmody A.B.,Rockx B.,Liu W.,Ashour J.,Shupert W.L.,Holbrook M.R.,Barrett A.D.,Mason P.W.,Bloom M.E.,Garcia-Sastre A.,Khromykh A.A.,Best S.M.
The NS5 protein of the virulent West Nile virus NY99 strain is a potent antagonist of type I interferon-mediated JAK-STAT signaling.
J. Virol.
84
3503-3515
2010
76821
Ambrose R.L.,Mackenzie J.M.
A conserved peptide in West Nile virus NS4A protein contributes to proteolytic processing and is essential for replication.
J. Virol.
85
11274-11282
2011
76822
Ambrose R.L.,Mackenzie J.M.
Conserved amino acids within the N-terminus of the West Nile virus NS4A protein contribute to virus replication, protein stability and membrane proliferation.
Virology
481
95-106
2015
76823
Lopez-Denman A.J.,Russo A.,Wagstaff K.M.,White P.A.,Jans D.A.,Mackenzie J.M.
Nucleocytoplasmic shuttling of the West Nile virus RNA-dependent RNA polymerase NS5 is critical to infection.
Cell. Microbiol.
20
0-0
2018
76824
Lopez-Denman A.J.,Tuipulotu D.E.,Ross J.B.,Trenerry A.M.,White P.A.,Mackenzie J.M.
Nuclear localisation of West Nile virus NS5 protein modulates host gene expression.
Virology
559
131-144
2021
76825
Dokland T.,Walsh M.,Mackenzie J.M.,Khromykh A.A.,Ee K.H.,Wang S.
West Nile virus core protein; tetramer structure and ribbon formation.
Structure
12
1157-1163
2004
76826
Malet H.,Egloff M.P.,Selisko B.,Butcher R.E.,Wright P.J.,Roberts M.,Gruez A.,Sulzenbacher G.,Vonrhein C.,Bricogne G.,Mackenzie J.M.,Khromykh A.A.,Davidson A.D.,Canard B.
Crystal structure of the RNA polymerase domain of the West Nile virus non-structural protein 5.
J. Biol. Chem.
282
10678-10689
2007
76827
Mastrangelo E.,Milani M.,Bollati M.,Selisko B.,Peyrane F.,Pandini V.,Sorrentino G.,Canard B.,Konarev P.V.,Svergun D.I.,de Lamballerie X.,Coutard B.,Khromykh A.A.,Bolognesi M.
Crystal structure and activity of Kunjin virus NS3 helicase; protease and helicase domain assembly in the full length NS3 protein.
J. Mol. Biol.
372
444-455
2007
76828
Zhang Y.,Kaufmann B.,Chipman P.R.,Kuhn R.J.,Rossmann M.G.
Structure of immature West Nile virus.
J. Virol.
81
6141-6145
2007
