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P12296

- POLG_ENMGO

UniProt

P12296 - POLG_ENMGO

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Protein

Genome polyprotein

Gene
N/A
Organism
Mengo encephalomyocarditis virus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity).By similarity
Protein VP0: VP0 precursor is a component of immature procapsids.By similarity
Protein 2B: Affects membrane integrity and cause an increase in membrane permeability.By similarity
Protein 2C: Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).By similarity
Protein 3A, via its hydrophobic domain, serves as membrane anchor.By similarity
Protease 3C: cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity).By similarity
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.PROSITE-ProRule annotation
Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function (By similarity).By similarity

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
NTP + H2O = NDP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei137 – 1382CleavageSequence Analysis
Sitei393 – 3942Cleavage; by protease 3CSequence Analysis
Sitei624 – 6252Cleavage; by protease 3CSequence Analysis
Sitei901 – 9022Cleavage; by protease 3CSequence Analysis
Sitei1044 – 10452Cleavage; by ribosomal skipSequence Analysis
Sitei1195 – 11962Cleavage; by protease 3CSequence Analysis
Sitei1520 – 15212Cleavage; by protease 3CSequence Analysis
Sitei1608 – 16092Cleavage; by protease 3CSequence Analysis
Sitei1628 – 16292Cleavage; by protease 3CSequence Analysis
Active sitei1674 – 16741For protease 3C activitySequence Analysis
Active sitei1706 – 17061For protease 3C activitySequence Analysis
Active sitei1787 – 17871For protease 3C activitySequence Analysis
Sitei1833 – 18342Cleavage; by protease 3CSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1314 – 13218ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. ion channel activity Source: UniProtKB-KW
  4. RNA binding Source: UniProtKB-KW
  5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  6. RNA helicase activity Source: InterPro
  7. structural molecule activity Source: InterPro

GO - Biological processi

  1. induction by virus of host autophagy Source: UniProtKB
  2. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  3. protein oligomerization Source: UniProtKB-KW
  4. RNA-protein covalent cross-linking Source: UniProtKB-KW
  5. suppression by virus of host gene expression Source: UniProtKB-KW
  6. suppression by virus of host mRNA export from nucleus Source: UniProtKB
  7. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  8. transcription, DNA-templated Source: InterPro
  9. viral entry into host cell Source: UniProtKB-KW
  10. viral RNA genome replication Source: InterPro
  11. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Transport, Viral attachment to host cell, Viral immunoevasion, Viral RNA replication, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiC03.009.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 13 chains:
Alternative name(s):
VP4-VP2
Alternative name(s):
P1A
Rho
Virion protein 4
Alternative name(s):
Beta
P1B
Virion protein 2
Alternative name(s):
Gamma
P1C
Virion protein 3
Alternative name(s):
Alpha
P1D
Virion protein 1
Protein 2A
Short name:
P2A
Alternative name(s):
G
Protein 2B
Short name:
I
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
C
Short name:
P2C
Protein 3A
Short name:
P3A
Protein 3B
Short name:
P3B
Alternative name(s):
H
VPg
Protease 3C (EC:3.4.22.28)
Short name:
P3C
Alternative name(s):
Picornain 3C
p22
RNA-directed RNA polymerase 3D-POL (EC:2.7.7.48)
Short name:
E
Short name:
P3D-POL
OrganismiMengo encephalomyocarditis virus
Taxonomic identifieri12107 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mus musculus (Mouse) [TaxID: 10090]
Oryctolagus cuniculus (Rabbit) [TaxID: 9986]
ProteomesiUP000008663: Genome

Subcellular locationi

Chain Protein 2B : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity
Chain Protein 2C : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity
Chain Protein 3A : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity
Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 15651565CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei1566 – 158419Sequence AnalysisAdd
BLAST
Topological domaini1585 – 2293709CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell cytoplasmic vesicle Source: UniProtKB-KW
  2. host cell nucleus Source: UniProtKB-KW
  3. icosahedral viral capsid Source: InterPro
  4. integral to membrane of host cell Source: UniProtKB-KW
  5. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6767Leader proteinSequence AnalysisPRO_5000141082Add
BLAST
Chaini68 – 393326Protein VP0Sequence AnalysisPRO_0000310965Add
BLAST
Chaini68 – 13770Protein VP4Sequence AnalysisPRO_5000141083Add
BLAST
Chaini138 – 393256Protein VP2Sequence AnalysisPRO_5000141084Add
BLAST
Chaini394 – 624231Protein VP3Sequence AnalysisPRO_5000141085Add
BLAST
Chaini625 – 901277Protein VP1Sequence AnalysisPRO_5000141086Add
BLAST
Chaini902 – 1044143Protein 2ASequence AnalysisPRO_5000141087Add
BLAST
Chaini1045 – 1195151Protein 2BSequence AnalysisPRO_5000141088Add
BLAST
Chaini1196 – 1520325Protein 2CSequence AnalysisPRO_5000141089Add
BLAST
Chaini1521 – 160888Protein 3ASequence AnalysisPRO_5000141090Add
BLAST
Chaini1609 – 162820Protein 3BSequence AnalysisPRO_5000141091Add
BLAST
Chaini1629 – 1833205Protease 3CSequence AnalysisPRO_5000141092Add
BLAST
Chaini1834 – 2293460RNA-directed RNA polymerase 3D-POLSequence AnalysisPRO_5000141093Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi68 – 681N-myristoyl glycine; by hostBy similarity
Modified residuei1611 – 16111O-(5'-phospho-RNA)-tyrosineBy similarity

Post-translational modificationi

Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle. The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond. This process would release the L-P1-2A peptide from the translational complex (By similarity).By similarity
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Structurei

Secondary structure

1
2293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Turni11 – 133Combined sources
Helixi16 – 183Combined sources
Helixi20 – 245Combined sources
Beta strandi32 – 343Combined sources
Beta strandi46 – 483Combined sources
Beta strandi60 – 623Combined sources
Turni63 – 653Combined sources
Beta strandi78 – 803Combined sources
Helixi94 – 974Combined sources
Beta strandi115 – 1173Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi133 – 1353Combined sources
Helixi148 – 1503Combined sources
Beta strandi152 – 1554Combined sources
Beta strandi160 – 1656Combined sources
Beta strandi169 – 1713Combined sources
Helixi172 – 1743Combined sources
Helixi194 – 1963Combined sources
Beta strandi200 – 2089Combined sources
Beta strandi216 – 2216Combined sources
Helixi223 – 2253Combined sources
Helixi228 – 2303Combined sources
Helixi231 – 2377Combined sources
Beta strandi240 – 25213Combined sources
Beta strandi260 – 26910Combined sources
Turni286 – 2905Combined sources
Helixi309 – 3146Combined sources
Beta strandi315 – 3217Combined sources
Turni322 – 3243Combined sources
Beta strandi326 – 3327Combined sources
Beta strandi337 – 3415Combined sources
Helixi343 – 3453Combined sources
Beta strandi349 – 36012Combined sources
Beta strandi368 – 38518Combined sources
Turni402 – 4054Combined sources
Helixi437 – 4393Combined sources
Turni440 – 4423Combined sources
Beta strandi455 – 4606Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi470 – 4767Combined sources
Helixi480 – 4823Combined sources
Helixi486 – 4916Combined sources
Beta strandi494 – 4996Combined sources
Beta strandi501 – 5077Combined sources
Beta strandi514 – 5229Combined sources
Beta strandi524 – 5263Combined sources
Helixi532 – 5354Combined sources
Beta strandi538 – 5447Combined sources
Beta strandi546 – 5483Combined sources
Beta strandi550 – 5556Combined sources
Beta strandi560 – 5678Combined sources
Turni573 – 5753Combined sources
Beta strandi579 – 58911Combined sources
Beta strandi598 – 6069Combined sources
Beta strandi611 – 6155Combined sources
Helixi629 – 6313Combined sources
Turni639 – 6424Combined sources
Beta strandi654 – 6563Combined sources
Helixi657 – 6615Combined sources
Beta strandi665 – 6706Combined sources
Helixi676 – 6783Combined sources
Beta strandi685 – 6884Combined sources
Beta strandi690 – 6945Combined sources
Helixi703 – 7053Combined sources
Beta strandi727 – 7293Combined sources
Beta strandi731 – 7333Combined sources
Helixi736 – 7405Combined sources
Beta strandi745 – 75814Combined sources
Beta strandi765 – 7706Combined sources
Beta strandi788 – 7903Combined sources
Beta strandi792 – 7943Combined sources
Beta strandi796 – 7994Combined sources
Beta strandi808 – 8125Combined sources
Beta strandi817 – 8248Combined sources
Beta strandi848 – 8547Combined sources
Beta strandi860 – 87314Combined sources
Beta strandi894 – 8963Combined sources
Beta strandi1836 – 18383Combined sources
Helixi1859 – 18624Combined sources
Beta strandi1865 – 18684Combined sources
Helixi1882 – 18854Combined sources
Helixi1886 – 18905Combined sources
Helixi1899 – 191618Combined sources
Helixi1925 – 19306Combined sources
Beta strandi1933 – 19353Combined sources
Beta strandi1940 – 19423Combined sources
Turni1946 – 19527Combined sources
Helixi1955 – 19584Combined sources
Turni1961 – 19644Combined sources
Helixi1968 – 197811Combined sources
Beta strandi1987 – 19915Combined sources
Beta strandi1994 – 19974Combined sources
Helixi1998 – 20025Combined sources
Beta strandi2008 – 20114Combined sources
Helixi2014 – 203118Combined sources
Turni2037 – 20404Combined sources
Helixi2047 – 205812Combined sources
Beta strandi2061 – 20688Combined sources
Turni2072 – 20754Combined sources
Helixi2078 – 208710Combined sources
Helixi2091 – 20933Combined sources
Helixi2099 – 21079Combined sources
Beta strandi2108 – 21136Combined sources
Beta strandi2116 – 21227Combined sources
Beta strandi2126 – 21283Combined sources
Helixi2131 – 215020Combined sources
Helixi2156 – 21583Combined sources
Beta strandi2160 – 21645Combined sources
Beta strandi2167 – 21748Combined sources
Helixi2178 – 21869Combined sources
Turni2187 – 21893Combined sources
Beta strandi2195 – 21973Combined sources
Turni2207 – 22093Combined sources
Beta strandi2215 – 22206Combined sources
Beta strandi2223 – 22286Combined sources
Helixi2230 – 22389Combined sources
Helixi2245 – 225612Combined sources
Helixi2257 – 22593Combined sources
Helixi2261 – 227313Combined sources
Helixi2281 – 229010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MECX-ray3.201625-898[»]
2138-393[»]
3394-624[»]
468-137[»]
2M7YNMR-A1-67[»]
2MEVX-ray3.001625-901[»]
2138-393[»]
3394-624[»]
468-137[»]
4NYZX-ray2.15A1834-2293[»]
4NZ0X-ray2.80A/B/C/D/E/F1834-2293[»]
ProteinModelPortaliP12296.
SMRiP12296. Positions 1-32, 76-892.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12296.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1282 – 1448167SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini2062 – 2180119RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 2 peptidase C3 domains.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProiIPR015031. Capsid_VP4_Picornavir.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR021573. Leader_pept_picornaV.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 2 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
PF11475. VP_N-CPKC. 1 hit.
[Graphical view]
PRINTSiPR00918. CALICVIRUSNS.
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

Isoform Genome polyprotein (identifier: P12296-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATTMEQEIC AHSMTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE
60 70 80 90 100
DDVFDPDLDM EVVFETQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI
110 120 130 140 150
DLSANATGSD PPKTYGQFSN LLSGAVNAFS NMLPLLADQN TEEMENLSDR
160 170 180 190 200
VSQDTAGNTV TNTQSTVGRL VGYGTVHDGE HPASCADTAS EKILAVERYY
210 220 230 240 250
TFKVNDWTST QKPFEYIRIP LPHVLSGEDG GVFGATLRRH YLVKTGWRVQ
260 270 280 290 300
VQCNASQFHA GSLLVFMAPE YPTLDVFAMD NRWSKDNLPN GTRTQTNRKG
310 320 330 340 350
PFAMDHQNFW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT
360 370 380 390 400
LVIAVVAPLT YSTGASTSLD ITASIQPVRP VFNGLRHEVL SRQSPIPVTI
410 420 430 440 450
REHAGTWYST LPDSTVPIYG KTPVAPANYM VGEYKDFLEI AQIPTFIGNK
460 470 480 490 500
VPNAVPYIEA SNTAVKTQPL AVYQVTLSCS CLANTFLAAL SRNFAQYRGS
510 520 530 540 550
LVYTFVFTGT AMMKGKFLIA YTPPGAGKPT SRDQAMQATY AIWDLGLNSS
560 570 580 590 600
YSFTVPFISP THFRMVGTDQ ANITNVDGWV TVWQLTPLTY PPGCPTSAKI
610 620 630 640 650
LTMVSAGKDF SLKMPISPAP WSPQGVENAE KGVTENTDAT ADFVAQPVYL
660 670 680 690 700
PENQTKVAFF YDRSSPIGAF AVKSGSLESG FAPFSNKACP NSVILTPGPQ
710 720 730 740 750
FDPAYDQLRP QRLTEIWGNG NEETSEVFPL KTKQDYSFCL FSPFVYYKCD
760 770 780 790 800
LEVTLSPHTS GAHGLLVRWC PTGTPTKPTT QVLHEVSSLS EGRTPQVYSA
810 820 830 840 850
GPGTSNQISF VVPYNSPLSV LPAVWYNGHK RFDNTGDLGI APNSDFGTLF
860 870 880 890 900
FAGTKPDIKF TVYLRYKNMR VFCPRPTVFF PWPTSGDKID MTPRAGVLML
910 920 930 940 950
ESPNPLDVSK TYPTLHILLQ FNHRGLEARI FRHGQLWAET HAEVVLRSKT
960 970 980 990 1000
KQISFLSNGS YPSMDATTPL NPWKSTYQAV LRAEPHRVTM DVYHKRIRPF
1010 1020 1030 1040 1050
RLPLVQKEWR TCEENVFGLY HVFETHYAGY FSDLLIHDVE TNPGPFTFKP
1060 1070 1080 1090 1100
RQRPVFQTQG AAVSSMAQTL LPNDLASKAM GSAFTALLDA NEDAQKAMKI
1110 1120 1130 1140 1150
IKTLSSLSDA WENVKGTLNN PEFWKQLLSR CVQLIAGMTI AVMHPDPLTL
1160 1170 1180 1190 1200
LCLGVLTAAE ITSQTSLCEE IAAKFKTIFT TPPPRFPVIS LFQQQSPLKQ
1210 1220 1230 1240 1250
VNDVFSLAKN LDWAVKTVEK VVDWFGTWVA QEEREQTLDQ LLQRFPEHAK
1260 1270 1280 1290 1300
RISDLRNGMA AYVECKESFD FFEKLYNQAV KEKRTGIAAV CEKFRQKHDH
1310 1320 1330 1340 1350
ATARCEPVVI VLRGDAGQGK SLSSQIIAQA VSKTIFGRQS VYSLPPDSDF
1360 1370 1380 1390 1400
FDGYENQFAA IMDDLGQNPD GSDFTTFCQM VSTTNLLPNM ASLERKGTPF
1410 1420 1430 1440 1450
TSQLVVATTN LPEFRPVTIA HYPAVERRIT FDYSVSAGPV CSKTEAGCKV
1460 1470 1480 1490 1500
LDVERAFRPT GDAPLPCFQN NCLFLEKAGL QFRDNRSKEI LSLVDVIERA
1510 1520 1530 1540 1550
VTRIERKKKV LTAVQTLVAQ GPVDEVSFYS VVQQLKARQE ATDEQLEELQ
1560 1570 1580 1590 1600
EAFARVQERS SVFSDWMKIS AMLCAATLAL TQVVKMAKAV KQMVRPDLVR
1610 1620 1630 1640 1650
VQLDEQEQGP YNETTRIKPK TLQLLDVQGP NPTMDFEKFV AKFVTAPIGF
1660 1670 1680 1690 1700
VYPTGVSTQT CLLVKGRTLA VNRHMAESDW TSIVVRGVSH TRSSVKIIAI
1710 1720 1730 1740 1750
AKAGKETDVS FIRLSSGPLF RDNTSKFVKA SDVLPHSSSP LIGIMNVDIP
1760 1770 1780 1790 1800
MMYTGTFLKA GVSVPVETGQ TFNHCIHYKA NTRKGWCGSA ILADLGGSKK
1810 1820 1830 1840 1850
ILGFHSAGSM GVAAASIISQ EMIDAVVQAF EPQGALERLP DGPRIHVPRK
1860 1870 1880 1890 1900
TALRPTVARQ VFQPAFAPAV LSKFDPRTDA DVDEVAFSKH TSNQETLPPV
1910 1920 1930 1940 1950
FRMVAREYAN RVFALLGRDN GRLSVKQALD GLEGMDPMDK NTSPGLPYTT
1960 1970 1980 1990 2000
LGMRRTDVVD WETATLIPFA AERLEKMNNK DFSDIVYQTF LKDELRPIEK
2010 2020 2030 2040 2050
VQAAKTRIVD VPPFEHCILG RQLLGKFASK FQTQPGLELG SAIGCDPDVH
2060 2070 2080 2090 2100
WTAFGVAMQG FERVYDVDYS NFDSTHSVAV FRLLAEEFFS EENGFDPLVK
2110 2120 2130 2140 2150
DYLESLAISK HAYEEKRYLI TGGLPSGCAA TSMLNTIMNN IIIRAGLYLT
2160 2170 2180 2190 2200
YKNFEFDDVK VLSYGDDLLV ATNYQLNFDR VRTSLAKTGY KITPANKTST
2210 2220 2230 2240 2250
FPLESTLEDV VFLKRKFKKE GPLYRPVMNR EALEAMLSYY RPGTLSEKLT
2260 2270 2280 2290
SITMLAVHSG KQEYDRLFAP FREVGVIVPT FESVEYRWRS LFW

Note: Produced by conventional translation.

Length:2,293
Mass (Da):255,528
Last modified:March 20, 2007 - v3
Checksum:i0394484E477B94E7
GO
Isoform 2B* (identifier: P0DJX8-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry P0DJX8.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by -1 ribosomal frameshifting.

Length:129
Mass (Da):14,191
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ294633 Genomic RNA. Translation: ABB97066.1.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ294633 Genomic RNA. Translation: ABB97066.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MEC X-ray 3.20 1 625-898 [» ]
2 138-393 [» ]
3 394-624 [» ]
4 68-137 [» ]
2M7Y NMR - A 1-67 [» ]
2MEV X-ray 3.00 1 625-901 [» ]
2 138-393 [» ]
3 394-624 [» ]
4 68-137 [» ]
4NYZ X-ray 2.15 A 1834-2293 [» ]
4NZ0 X-ray 2.80 A/B/C/D/E/F 1834-2293 [» ]
ProteinModelPortali P12296.
SMRi P12296. Positions 1-32, 76-892.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P12296.

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
4.10.90.10. 1 hit.
InterProi IPR015031. Capsid_VP4_Picornavir.
IPR004004. Helic/Pol/Pept_Calicivir-typ.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR021573. Leader_pept_picornaV.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view ]
Pfami PF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 2 hits.
PF00910. RNA_helicase. 1 hit.
PF08935. VP4_2. 1 hit.
PF11475. VP_N-CPKC. 1 hit.
[Graphical view ]
PRINTSi PR00918. CALICVIRUSNS.
SUPFAMi SSF50494. SSF50494. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Dipyridamole reversibly inhibits mengovirus RNA replication."
    Fata-Hartley C.L., Palmenberg A.C.
    J. Virol. 79:11062-11070(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Medium plague.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-901.
  3. "Structural refinement and analysis of Mengo virus."
    Krishnaswamy S., Rossmann M.G.
    J. Mol. Biol. 211:803-844(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SEQUENCE REVISION TO 451 AND 669.

Entry informationi

Entry nameiPOLG_ENMGO
AccessioniPrimary (citable) accession number: P12296
Secondary accession number(s): Q2V6G9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: March 20, 2007
Last modified: November 26, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3