Reviewed, UniProtKB/Swiss-Prot P05769 (POLG_MVEV5)

Names and origin

Protein names	Recommended name:     Genome polyprotein Cleaved into the following 10 chains:     1- Recommended name:             Protein C         Alternative name(s):             Core protein             Capsid protein     2- Recommended name:             Small envelope protein M         Alternative name(s):             Matrix protein     3- Recommended name:             Envelope protein E     4- Recommended name:             Non-structural protein 1                 Short name=NS1     5- Recommended name:             Non-structural protein 2A                 Short name=NS2A     6- Recommended name:             Serine protease subunit NS2B         Alternative name(s):             Non-structural protein 2B             Flavivirin protease NS2B regulatory subunit     7- Recommended name:             Serine protease/NTPase/helicase NS3               EC=3.4.21.91               EC=3.6.1.15               EC=3.6.1.-         Alternative name(s):             Flavivirin protease NS3 catalytic subunit             Non-structural protein 3     8- Recommended name:             Non-structural protein 4A                 Short name=NS4A     9- Recommended name:             Non-structural protein 4B                 Short name=NS4B     10- Recommended name:             Methyltransferase/RNA-directed RNA polymerase NS5               EC=2.7.7.48               EC=2.1.1.56               EC=2.1.1.57         Alternative name(s):             Non-structural protein 5
Organism	Murray valley encephalitis virus (strain MVE-1-51) (MVEV) [Complete proteome]
Taxonomic identifier	301478 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Flavivirus › Japanese encephalitis virus group › Murray Valley encephalitis virus
Virus host	Homo sapiens (Human) [TaxID: 9606] Culex annulirostris (Common banded mosquito) [TaxID: 162997]

Protein attributes

Sequence length	3434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	The small proteins NS2A, NS4A and NS4B are hydrophobic, suggesting a possible membrane-related function By similarity. Non-structural protein 2B is a required cofactor for the serine protease function of NS3 By similarity. Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, cleaves the polyprotein By similarity. RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions By similarity.
Catalytic activity	Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala. Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). NTP + H2O = NDP + phosphate. S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA. S-adenosyl-L-methionine + m7G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA.
Subunit structure	NS3 and NS2B form a heterodimer. NS3 is the catalytic subunit, whereas NS2B strongly stimulates the latter By similarity.
Subcellular location	Protein C: Virion Potential. Host membrane; Single-pass membrane protein Potential. Small envelope protein M: Virion Potential. Host membrane; Single-pass membrane protein Potential. Envelope protein E: Virion Potential. Host membrane; Multi-pass membrane protein Potential. Non-structural protein 4A: Host membrane; Single-pass membrane protein Potential. Non-structural protein 4B: Host membrane; Multi-pass membrane protein Potential.
Post-translational modification	Specific enzymatic cleavages in vivo yield mature proteins By similarity.
Miscellaneous	The virion of this virus is a nucleocapsid covered by a lipoprotein envelope. The envelope contains two proteins: the protein M and glycoprotein E. The nucleocapsid is a complex of protein C and mRNA. In immature particles, there are 60 icosaedrally organized trimeric spikes on the surface. Each spike consists of three heterodimers of envelope protein M precursor (prM) and envelope protein E By similarity.
Sequence similarities	Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 peptidase S7 domain. Contains 1 RdRp catalytic domain.

Ontologies

Keywords
Biological process	RNA replication
Cellular component	Capsid protein Core protein Envelope protein Host membrane Membrane Virion
Domain	Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Helicase Hydrolase Methyltransferase Nucleotidyltransferase RNA-directed RNA polymerase Transferase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	RNA metabolic process Inferred from electronic annotation. Source: InterPro methylation Inferred from electronic annotation. Source: InterPro transcription, RNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell viral envelope Inferred from electronic annotation. Source: UniProtKB-KW viral nucleocapsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro RNA helicase activity Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW double-stranded RNA binding Inferred from electronic annotation. Source: InterPro methyltransferase activity Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed; by host Potential

Chain

2 – 121

120

Protein C

PRO_0000037782

Propeptide

122 – 217

96

PRO_0000037783

Chain

218 – 292

75

Small envelope protein M

PRO_0000037784

Chain

293 – 793

501

Envelope protein E

PRO_0000037785

Chain

794 – 1207

414

Non-structural protein 1

PRO_0000037786

Chain

1208 – 1372

165

Non-structural protein 2A

PRO_0000037787

Chain

1373 – 1503

131

Serine protease subunit NS2B

PRO_0000037788

Chain

1504 – 2122

619

Serine protease/NTPase/helicase NS3

PRO_0000037789

Chain

2123 – 2414

292

Non-structural protein 4A By similarity

PRO_0000037790

Chain

2415 – 2529

115

Non-structural protein 4B By similarity

PRO_0000037791

Chain

2530 – 3434

905

Methyltransferase/RNA-directed RNA polymerase NS5

PRO_0000037792

Regions

Transmembrane

44 – 60

17

Potential

Transmembrane

112 – 128

17

Potential

Transmembrane

278 – 294

17

Potential

Transmembrane

773 – 789

17

Potential

Transmembrane

1178 – 1194

17

Potential

Transmembrane

1219 – 1235

17

Potential

Transmembrane

1250 – 1266

17

Potential

Transmembrane

1312 – 1328

17

Potential

Transmembrane

1378 – 1394

17

Potential

Transmembrane

1401 – 1417

17

Potential

Transmembrane

1476 – 1492

17

Potential

Domain

1510 – 1681

172

Peptidase S7

Domain

1684 – 1840

157

Helicase ATP-binding

Domain

1851 – 2016

166

Helicase C-terminal

Domain

3059 – 3211

153

RdRp catalytic

Nucleotide binding

1697 – 1704

8

ATP Potential

Motif

1788 – 1791

4

DEAH box

Sites

Active site

1554

1

Charge relay system By similarity

Active site

1578

1

Charge relay system By similarity

Active site

1638

1

Charge relay system By similarity

Active site

2590

1

For 2'-O-methyltransferase activity By similarity

Active site

2675

1

For 2'-O-methyltransferase and N-7 methyltransferase activity By similarity

Active site

2711

1

For 2'-O-methyltransferase activity By similarity

Active site

2747

1

For 2'-O-methyltransferase activity By similarity

Amino acid modifications

Glycosylation

73

1

N-linked (GlcNAc...); by host Potential

Glycosylation

140

1

N-linked (GlcNAc...); by host Potential

Glycosylation

446

1

N-linked (GlcNAc...); by host Potential

Glycosylation

923

1

N-linked (GlcNAc...); by host

Glycosylation

968

1

N-linked (GlcNAc...); by host

Glycosylation

1000

1

N-linked (GlcNAc...) (high mannose); by host

Glycosylation

2487

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2493

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2763

1

N-linked (GlcNAc...); by host Potential

Disulfide bond

295 ↔ 322

By similarity

Disulfide bond

352 ↔ 408

By similarity

Disulfide bond

366 ↔ 397

By similarity

Disulfide bond

384 ↔ 413

By similarity

Disulfide bond

482 ↔ 580

By similarity

Disulfide bond

597 ↔ 628

By similarity

Disulfide bond

797 ↔ 808

Ref.4

Disulfide bond

848 ↔ 936

Ref.4

Disulfide bond

972 ↔ 1016

Ref.4

Experimental info

Sequence conflict

115

1

L → V in CAA27184. Ref.2

Sequence conflict

754

1

P → Q in CAA27184. Ref.2

Sequence conflict

960

1

G → V in CAA27184. Ref.2

Sequence conflict

1485

1

R → W in CAA27184. Ref.2

Sequence conflict

1779

1

V → G Ref.2

Secondary structure

1

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3434

Helix Strand Turn

Details...

Helix

1684 – 1687

4

Beta strand

1692 – 1695

4

Beta strand

1699 – 1701

3

Turn

1703 – 1706

4

Helix

1707 – 1717

11

Beta strand

1722 – 1728

7

Helix

1729 – 1738

10

Turn

1739 – 1741

3

Beta strand

1744 – 1746

3

Beta strand

1761 – 1765

5

Helix

1766 – 1773

8

Beta strand

1775 – 1777

3

Beta strand

1783 – 1789

7

Helix

1795 – 1809

15

Beta strand

1814 – 1818

5

Beta strand

1836 – 1840

5

Beta strand

1849 – 1851

3

Helix

1853 – 1857

5

Beta strand

1862 – 1865

4

Helix

1869 – 1881

13

Beta strand

1886 – 1889

4

Turn

1891 – 1893

3

Helix

1894 – 1901

8

Beta strand

1907 – 1911

5

Helix

1913 – 1916

4

Beta strand

1924 – 1928

5

Beta strand

1935 – 1938

4

Beta strand

1944 – 1947

4

Helix

1955 – 1962

8

Beta strand

1974 – 1978

5

Helix

1990 – 1999

10

Helix

2014 – 2016

3

Turn

2024 – 2027

4

Helix

2031 – 2042

12

Helix

2048 – 2055

8

Turn

2056 – 2058

3

Helix

2064 – 2067

4

Helix

2072 – 2074

3

Beta strand

2078 – 2081

4

Beta strand

2098 – 2101

4

Helix

2102 – 2104

3

Helix

2108 – 2118

11

Helix

2537 – 2546

10

Helix

2550 – 2557

8

Turn

2558 – 2560

3

Beta strand

2562 – 2564

3

Helix

2566 – 2568

3

Helix

2587 – 2596

10

Beta strand

2604 – 2609

6

Helix

2615 – 2620

6

Beta strand

2626 – 2632

7

Helix

2650 – 2652

3

Beta strand

2653 – 2656

4

Helix

2661 – 2663

3

Beta strand

2670 – 2674

5

Helix

2683 – 2701

19

Beta strand

2706 – 2713

8

Helix

2718 – 2731

14

Beta strand

2734 – 2736

3

Beta strand

2748 – 2751

4

Helix

2758 – 2771

14

Beta strand

2782 – 2784

3

Sequences

	Sequence		Length	Mass (Da)
	P05769-1 [UniParc]. Last modified December 21, 2004. Version 2. Checksum: 20D7110791C567A9	FASTA	3,434	380,577
	10 20 30 40 50 60 MSKKPGGPGK PRVVNMLKRG IPRVFPLVGV KRVVMNLLDG RGPIRFVLAL LAFFRFTALA 70 80 90 100 110 120 PTKALMRRWK SVNKTTAMKH LTSFKKELGT LIDVVNKRGK KQKKRGGSET SVLMLIFMLI 130 140 150 160 170 180 GFAAALKLST FQGKIMMTVN ATDIADVIAI PTPKGPNQCW IRAIDIGFMC DDTITYECPK 190 200 210 220 230 240 LESGNDPEDI DCWCDKQAVY VNYGRCTRAR HSKRSRRSIT VQTHGESTLV NKKDAWLDST 250 260 270 280 290 300 KATRYLTKTE NWIIRNPGYA LVAVVLGWML GSNTGQKVIF TVLLLLVAPA YSFNCLGMSS 310 320 330 340 350 360 RDFIEGASGA TWVDLVLEGD SCITIMAADK PTLDIRMMNI EATNLALVRN YCYAATVSDV 370 380 390 400 410 420 STVSNCPTTG ESHNTKRADH NYLCKRGVTD RGWGNGCGLF GKGSIDTCAK FTCSNSAAGR 430 440 450 460 470 480 LILPEDIKYE VGVFVHGSTD STSHGNYSTQ IGANQAVRFT ISPNAPAITA KMGDYGEVTV 490 500 510 520 530 540 ECEPRSGLNT EAYYVMTIGT KHFLVHREWF NDLLLPWTSP ASTEWRNREI LVEFEEPHAT 550 560 570 580 590 600 KQSVVALGSQ EGALHQALAG AIPVEFSSST LKLTSGHLKC RVKMEKLKLK GTTYGMCTEK 610 620 630 640 650 660 FTFSKNPADT GHGTVVLELQ YTGSDGPCKI PISSVASLND MTPVGRMVTA NPYVASSTAN 670 680 690 700 710 720 AKVLVEIEPP FGDSYIVVGR GDKQINHHWH KEGSSIGKAF STTLKGAQRL AALGDTAWDF 730 740 750 760 770 780 GSVGGVFNSI GKAVHQVFGG AFRTLFGGMS WISPGLLGAL LLWMGVNARD KSIALAFLAT 790 800 810 820 830 840 GGVLLFLATN VHADTGCAID ITRRELKCGS GIFIHNDVEA WIDRYKYLPE TPKQLAKVVE 850 860 870 880 890 900 NAHKSGICGI RSVNRFEHQM WESVRDELNA LLKENAIDLS VVVEKQKGMY RAAPNRLRLT 910 920 930 940 950 960 VEELDIGWKA WGKSLLFAAE LANSTFVVDG PETAECPNSK RAWNSFEIED FGFGITSTRG 970 980 990 1000 1010 1020 WLKLREENTS ECDSTIIGTA VKGNHAVHSD LSYWIESGLN GTWKLERAIF GEVKSCTWPE 1030 1040 1050 1060 1070 1080 THTLWGDAVE ETELIIPVTL AGPRSKHNRR EGYKVQVQGP WDEEDIKLDF DYCPGTTVTV 1090 1100 1110 1120 1130 1140 SEHCGKRGPS VRTTTDSGKL VTDWCCRSCT LPPLRFTTAS GCWYGMEIRP MKHDESTLVK 1150 1160 1170 1180 1190 1200 SRVQAFNGDM IDPFQLGLLV MFLATQEVLR KRWTARLTLP AAVGALLVLL LGGITYTDLV 1210 1220 1230 1240 1250 1260 RYLILVGSAF AESNNGGDVI HLALIAVFKV QPAFLVASLT RSRWTNQENL VLVLGAAFFQ 1270 1280 1290 1300 1310 1320 MAASDLELTI PGLLNSAATA WMVLRAMAFP STSAIAMPML AMLAPGMRML HLDTYRIVLL 1330 1340 1350 1360 1370 1380 LIGICSLLNE RRRSVEKKKG AVLIGLALTS TGYFSPTIMA AGLMICNPNK KRGWPATEVL 1390 1400 1410 1420 1430 1440 TAVGLMFAIV GGLAELDIDS MSVPFTIAGL MLVSYVISGK ATDMWLERAA DVSWEAGAAI 1450 1460 1470 1480 1490 1500 TGTSERLDVQ LDDDGDFHLL NDPGVPWKIW VLRMTCLSVA AITPRAILPS AFGYWLTLKY 1510 1520 1530 1540 1550 1560 TKRGGVFWDT PSPKVYPKGD TTPGVYRIMA RGILGRYQAG VGVMHEGVFH TLWHTTRGAA 1570 1580 1590 1600 1610 1620 IMSGEGRLTP YWGNVKEDRV TYGGPWKLDQ KWNGVDDVQM IVVEPGKPAI NVQTKPGIFK 1630 1640 1650 1660 1670 1680 TAHGEIGAVS LDYPIGTSGS PIVNSNGEII GLYGNGVILG NGAYVSAIVQ GERVEEPVPE 1690 1700 1710 1720 1730 1740 AYNPEMLKKR QLTVLDLHPG AGKTRRILPQ IIKDAIQKRL RTAVLAPTRV VAAEMAEALR 1750 1760 1770 1780 1790 1800 GLPVRYLTPA VQREHSGNEI VDVMCHATLT HRLMSPLRVP NYNLFVMDEA HFTDPASIAA 1810 1820 1830 1840 1850 1860 RGYIATRVEA GEAAAIFMTA TPPGTSDPFP DTNSPVHDVS SEIPDRAWSS GFEWITDYAG 1870 1880 1890 1900 1910 1920 KTVWFVASVK MSNEIAQCLQ RAGKRVIQLN RKSYDTEYPK CKNGDWDFVI TTDISEMGAN 1930 1940 1950 1960 1970 1980 FGASRVIDCR KSVKPTILDE GEGRVILSVP SAITSASAAQ RRGRVGRNPS QIGDEYHYGG 1990 2000 2010 2020 2030 2040 GTSEDDTMLA HWTEAKILLD NIHLPNGLVA QLYGPERDKT YTMDGEYRLR GEERKTFLEL 2050 2060 2070 2080 2090 2100 IKTADLPVWL AYKVASNGIQ YNDRKWCFDG PRSNIILEDN NEVEIITRIG ERKVLKPRWL 2110 2120 2130 2140 2150 2160 DARVYSDHQS LKWFKDFAAG KRSAIGFFEV LGRMPEHFAG KTREALDTMY LVATSEKGGK 2170 2180 2190 2200 2210 2220 AHRMALEELP DALETITLIA ALGVMTAGFF LLMMQRKGIG KLGLGALVLV VATFFLWMSD 2230 2240 2250 2260 2270 2280 VSGTKIAGVL LLALLMMVVL IPEPEKQRSQ TDNQLAVFLI CVLLVVGLVA ANEYGMLERT 2290 2300 2310 2320 2330 2340 KTDIRNLFGK SLIEENEVHI PPFDFFTLDL KPATAWALYG GSTVVLTPLI KHLVTSQYVT 2350 2360 2370 2380 2390 2400 TSLASINAQA GSLFTLPKGI PFTDFDLSVA LVFLGCWGQV TLTTLIMATI LVTLHYGYLL 2410 2420 2430 2440 2450 2460 PGWQAEALRA AQKRTAAGIM KNAVVDGIVA TDVPELERTT PQMQKRLGQI LLVLASVAAV 2470 2480 2490 2500 2510 2520 CVNPRITTIR EAGILCTAAA LTLWDNNASA AWNSTTATGL CHVMRGSWIA GASIAWTLIK 2530 2540 2550 2560 2570 2580 NAEKPAFKRG RAGGRTLGEQ WKEKLNAMGK EEFFSYRKEA ILEVDRTEAR RARREGNKVG 2590 2600 2610 2620 2630 2640 GHPVSRGTAK LRWLVERRFV QPIGKVVDLG CGRGGWSYYA ATMKNVQEVR GYTKGGPGHE 2650 2660 2670 2680 2690 2700 EPMLMQSYGW NIVTMKSGVD VFYKPSEISD TLLCDIGESS PSAEIEEQRT LRILEMVSDW 2710 2720 2730 2740 2750 2760 LSRGPKEFCI KILCPYMPKV IEKLESLQRR FGGGLVRVPL SRNSNHEMYW VSGASGNIVH 2770 2780 2790 2800 2810 2820 AVNMTSQVLI GRMDKKIWKG PKYEEDVNLG SGTRAVGKGV QHTDYKRIKS RIEKLKEEYA 2830 2840 2850 2860 2870 2880 ATWHTDDNHP YRTWTYHGSY EVKPSGSAST LVNGVVRLLS KPWDAITGVT TMAMTDTTPF 2890 2900 2910 2920 2930 2940 GQQRVFKEKV DTKAPEPPQG VKTVMDETTN WLWAYLARNK KARLCTREEF VKKVNSHAAL 2950 2960 2970 2980 2990 3000 GAMFEEQNQW KNAREAVEDP KFWEMVDEER ECHLRGECRT CIYNMMGKRE KKPGEFGKAK 3010 3020 3030 3040 3050 3060 GSRAIWFMWL GARFLEFEAL GFLNEDHWMS RENSGGGVEG AGIQKLGYIL RDVAQKPGGK 3070 3080 3090 3100 3110 3120 IYADDTAGWD TRITQADLEN EAKVLELMEG EQRTLARAII ELTYRHKVVK VMRPAAGGKT 3130 3140 3150 3160 3170 3180 VMDVISREDQ RGSGQVVTYA LNTFTNIAVQ LVRLMEAEAV IGPDDIESIE RKKKFAVRTW 3190 3200 3210 3220 3230 3240 LFENAEERVQ RMAVSGDDCV VKPLDDRFST ALHFLNAMSK VRKDIQEWKP SQGWYDWQQV 3250 3260 3270 3280 3290 3300 PFCSNHFQEV IMKDGRTLVV PCRGQDELIG RARISPGSGW NVRDTACLAK AYAQMWLVLY 3310 3320 3330 3340 3350 3360 FHRRDLRLMA NAICSSVPVD WVPTGRTTWS IHGKGEWMTT EDMLSVWNRV WILENEWMED 3370 3380 3390 3400 3410 3420 KTTVSDWTEV PYVGKREDIW CGSLIGTRTR ATWAENIYAA INQVRSVIGK EKYVDYVQSL 3430 RRYEETHVSE DRVL

References

[1]	"Characterization of infectious Murray Valley encephalitis virus derived from a stably cloned genomic-length cDNA." Hurrelbrink R.J., Nestorowicz A., McMinn P.C. J. Gen. Virol. 80:3115-3125(1999) [PubMed: 10567642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Partial nucleotide sequence of the Murray Valley encephalitis virus genome. Comparison of the encoded polypeptides with yellow fever virus structural and non-structural proteins." Dalgarno L., Trent D.W., Strauss J.H., Rice C.M. J. Mol. Biol. 187:309-323(1986) [PubMed: 3009829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-1780.
[3]	"Sequence of the 3' half of the Murray Valley encephalitis virus genome and mapping of the nonstructural proteins NS1, NS3, and NS5." Lee E., Fernon C., Simpson R., Weir R.C., Rice C.M., Dalgarno L. Virus Genes 4:197-213(1990) [PubMed: 1702914] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1773-3434, PROTEIN SEQUENCE OF 794-807; 1504-1519 AND 2530-2537.
[4]	"Determination of the intramolecular disulfide bond arrangement and biochemical identification of the glycosylation sites of the nonstructural protein NS1 of Murray Valley encephalitis virus." Blitvich B.J., Scanlon D., Shiell B.J., Mackenzie J.S., Pham K., Hall R.A. J. Gen. Virol. 82:2251-2256(2001) [PubMed: 11514736] [Abstract] Cited for: GLYCOSYLATION OF NS1, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF161266 Genomic RNA. Translation: AAF05296.1.
X03467 Unassigned RNA. Translation: CAA27184.1.

PIR

GNWVMV. A24635.

RefSeq

NP_051124.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PX2	X-ray	2.00	A/B	2530-2798	[»]
2PX4	X-ray	2.20	A	2530-2798	[»]
2PX5	X-ray	2.30	A/B	2530-2798	[»]
2PX8	X-ray	2.20	A/B	2530-2798	[»]
2PXA	X-ray	2.30	A/B	2530-2798	[»]
2PXC	X-ray	2.80	A	2530-2798	[»]
2V8O	X-ray	1.90	A	1681-2122	[»]
2WV9	X-ray	2.75	A	1421-2122	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S07.001.

Genome annotation databases

GeneID

1489715.

Family and domain databases

InterPro

IPR014001. DEAD-like_N.
IPR001650. DNA/RNA_helicase_C.
IPR000069. Env_glycoprot_M_flavivir.
IPR013756. Flav_glyE_cen_dom_subdom2.
IPR013754. Flav_glyE_dim.
IPR001122. Flavi_capsidC.
IPR001157. Flavi_NS1.
IPR000752. Flavi_NS2A.
IPR000487. Flavi_NS2B.
IPR000404. Flavi_NS4A.
IPR001528. Flavi_NS4B.
IPR002535. Flavi_propep.
IPR000336. Flv_glyE_Ig-like.
IPR014412. Gen_Poly_FLV.
IPR011999. GlycoprotE_cen/dimer_Flavivir.
IPR011998. GlycoprotE_cen/dimer_vir.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR014756. Ig_E-set.
IPR001850. Peptidase_S7.
IPR000208. RNA-dir_pol_flavivirus.
IPR007094. RNA-dir_pol_PSvirus.
IPR002877. rRNA_MeTrfase_RrmJ/FtsJ.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]

Gene3D

G3DSA:3.30.67.10. Flav_glyE_cen_2. 1 hit.
G3DSA:2.60.98.10. Flav_glyE_dim. 1 hit.
G3DSA:2.60.40.350. Flv_glyE_Ig-like. 1 hit.

Pfam

PF01003. Flavi_capsid. 1 hit.
PF02832. Flavi_glycop_C. 1 hit.
PF00869. Flavi_glycoprot. 1 hit.
PF01004. Flavi_M. 1 hit.
PF00948. Flavi_NS1. 1 hit.
PF01005. Flavi_NS2A. 1 hit.
PF01002. Flavi_NS2B. 1 hit.
PF01350. Flavi_NS4A. 1 hit.
PF01349. Flavi_NS4B. 1 hit.
PF00972. Flavi_NS5. 1 hit.
PF01570. Flavi_propep. 1 hit.
PF01728. FtsJ. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00949. Peptidase_S7. 1 hit.
[Graphical view]

PIRSF

PIRSF003817. Gen_Poly_FLV. 1 hit.

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

PROSITE

PS00690. DEAH_ATP_HELICASE. False negative.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

POLG_MVEV5

Accession

Primary (citable) accession number: P05769
Secondary accession number(s): Q9Q9F7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	December 21, 2004
Last modified:	February 9, 2010
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)