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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.
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.
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.
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.
Protein 2A: is involved in host translation shutoff. Nuclear localization is required for this function By similarity.

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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 – 1382Cleavage Reviewed prediction
Sitei393 – 3942Cleavage; by protease 3C Reviewed prediction
Sitei624 – 6252Cleavage; by protease 3C Reviewed prediction
Sitei901 – 9022Cleavage; by protease 3C Reviewed prediction
Sitei1044 – 10452Cleavage; by ribosomal skip Reviewed prediction
Sitei1195 – 11962Cleavage; by protease 3C Reviewed prediction
Sitei1520 – 15212Cleavage; by protease 3C Reviewed prediction
Sitei1608 – 16092Cleavage; by protease 3C Reviewed prediction
Sitei1628 – 16292Cleavage; by protease 3C Reviewed prediction
Active sitei1674 – 16741For protease 3C activity Reviewed prediction
Active sitei1706 – 17061For protease 3C activity Reviewed prediction
Active sitei1787 – 17871For protease 3C activity Reviewed prediction
Sitei1833 – 18342Cleavage; by protease 3C Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1314 – 13218ATP Reviewed prediction

GO - Molecular functioni

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

GO - Biological processi

  1. RNA-protein covalent cross-linking Source: UniProtKB-KW
  2. induction by virus of host autophagy Source: UniProtKB
  3. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  4. protein oligomerization Source: UniProtKB-KW
  5. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  6. suppression by virus of host mRNA export from nucleus Source: UniProtKB
  7. suppression by virus of host translation Source: UniProtKB-KW
  8. transcription, DNA-templated Source: InterPro
  9. viral RNA genome replication Source: InterPro
  10. viral entry into host cell Source: UniProtKB-KW
  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 VP2 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP3 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP1 : Virion. Host cytoplasm Reviewed prediction
Chain Protein 2B : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 2C : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3A : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3B : Virion Reviewed prediction
Chain Protease 3C : Host cytoplasm Reviewed prediction
Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 15651565Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1566 – 158419 Reviewed prediction
Add
BLAST
Topological domaini1585 – 2293709Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  2. host cell nucleus Source: UniProtKB-SubCell
  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 protein Reviewed prediction
PRO_5000141082Add
BLAST
Chaini68 – 393326Protein VP0 Reviewed prediction
PRO_0000310965Add
BLAST
Chaini68 – 13770Protein VP4 Reviewed prediction
PRO_5000141083Add
BLAST
Chaini138 – 393256Protein VP2 Reviewed prediction
PRO_5000141084Add
BLAST
Chaini394 – 624231Protein VP3 Reviewed prediction
PRO_5000141085Add
BLAST
Chaini625 – 901277Protein VP1 Reviewed prediction
PRO_5000141086Add
BLAST
Chaini902 – 1044143Protein 2A Reviewed prediction
PRO_5000141087Add
BLAST
Chaini1045 – 1195151Protein 2B Reviewed prediction
PRO_5000141088Add
BLAST
Chaini1196 – 1520325Protein 2C Reviewed prediction
PRO_5000141089Add
BLAST
Chaini1521 – 160888Protein 3A Reviewed prediction
PRO_5000141090Add
BLAST
Chaini1609 – 162820Protein 3B Reviewed prediction
PRO_5000141091Add
BLAST
Chaini1629 – 1833205Protease 3C Reviewed prediction
PRO_5000141092Add
BLAST
Chaini1834 – 2293460RNA-directed RNA polymerase 3D-POL Reviewed prediction
PRO_5000141093Add
BLAST

Amino acid modifications

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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP12296.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1282 – 1448167SF3 helicase
Add
BLAST
Domaini2062 – 2180119RdRp catalytic
Add
BLAST

Sequence similaritiesi

Contains 2 peptidase C3 domains.

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

MATTMEQEIC AHSMTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE     50
DDVFDPDLDM EVVFETQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI 100
DLSANATGSD PPKTYGQFSN LLSGAVNAFS NMLPLLADQN TEEMENLSDR 150
VSQDTAGNTV TNTQSTVGRL VGYGTVHDGE HPASCADTAS EKILAVERYY 200
TFKVNDWTST QKPFEYIRIP LPHVLSGEDG GVFGATLRRH YLVKTGWRVQ 250
VQCNASQFHA GSLLVFMAPE YPTLDVFAMD NRWSKDNLPN GTRTQTNRKG 300
PFAMDHQNFW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT 350
LVIAVVAPLT YSTGASTSLD ITASIQPVRP VFNGLRHEVL SRQSPIPVTI 400
REHAGTWYST LPDSTVPIYG KTPVAPANYM VGEYKDFLEI AQIPTFIGNK 450
VPNAVPYIEA SNTAVKTQPL AVYQVTLSCS CLANTFLAAL SRNFAQYRGS 500
LVYTFVFTGT AMMKGKFLIA YTPPGAGKPT SRDQAMQATY AIWDLGLNSS 550
YSFTVPFISP THFRMVGTDQ ANITNVDGWV TVWQLTPLTY PPGCPTSAKI 600
LTMVSAGKDF SLKMPISPAP WSPQGVENAE KGVTENTDAT ADFVAQPVYL 650
PENQTKVAFF YDRSSPIGAF AVKSGSLESG FAPFSNKACP NSVILTPGPQ 700
FDPAYDQLRP QRLTEIWGNG NEETSEVFPL KTKQDYSFCL FSPFVYYKCD 750
LEVTLSPHTS GAHGLLVRWC PTGTPTKPTT QVLHEVSSLS EGRTPQVYSA 800
GPGTSNQISF VVPYNSPLSV LPAVWYNGHK RFDNTGDLGI APNSDFGTLF 850
FAGTKPDIKF TVYLRYKNMR VFCPRPTVFF PWPTSGDKID MTPRAGVLML 900
ESPNPLDVSK TYPTLHILLQ FNHRGLEARI FRHGQLWAET HAEVVLRSKT 950
KQISFLSNGS YPSMDATTPL NPWKSTYQAV LRAEPHRVTM DVYHKRIRPF 1000
RLPLVQKEWR TCEENVFGLY HVFETHYAGY FSDLLIHDVE TNPGPFTFKP 1050
RQRPVFQTQG AAVSSMAQTL LPNDLASKAM GSAFTALLDA NEDAQKAMKI 1100
IKTLSSLSDA WENVKGTLNN PEFWKQLLSR CVQLIAGMTI AVMHPDPLTL 1150
LCLGVLTAAE ITSQTSLCEE IAAKFKTIFT TPPPRFPVIS LFQQQSPLKQ 1200
VNDVFSLAKN LDWAVKTVEK VVDWFGTWVA QEEREQTLDQ LLQRFPEHAK 1250
RISDLRNGMA AYVECKESFD FFEKLYNQAV KEKRTGIAAV CEKFRQKHDH 1300
ATARCEPVVI VLRGDAGQGK SLSSQIIAQA VSKTIFGRQS VYSLPPDSDF 1350
FDGYENQFAA IMDDLGQNPD GSDFTTFCQM VSTTNLLPNM ASLERKGTPF 1400
TSQLVVATTN LPEFRPVTIA HYPAVERRIT FDYSVSAGPV CSKTEAGCKV 1450
LDVERAFRPT GDAPLPCFQN NCLFLEKAGL QFRDNRSKEI LSLVDVIERA 1500
VTRIERKKKV LTAVQTLVAQ GPVDEVSFYS VVQQLKARQE ATDEQLEELQ 1550
EAFARVQERS SVFSDWMKIS AMLCAATLAL TQVVKMAKAV KQMVRPDLVR 1600
VQLDEQEQGP YNETTRIKPK TLQLLDVQGP NPTMDFEKFV AKFVTAPIGF 1650
VYPTGVSTQT CLLVKGRTLA VNRHMAESDW TSIVVRGVSH TRSSVKIIAI 1700
AKAGKETDVS FIRLSSGPLF RDNTSKFVKA SDVLPHSSSP LIGIMNVDIP 1750
MMYTGTFLKA GVSVPVETGQ TFNHCIHYKA NTRKGWCGSA ILADLGGSKK 1800
ILGFHSAGSM GVAAASIISQ EMIDAVVQAF EPQGALERLP DGPRIHVPRK 1850
TALRPTVARQ VFQPAFAPAV LSKFDPRTDA DVDEVAFSKH TSNQETLPPV 1900
FRMVAREYAN RVFALLGRDN GRLSVKQALD GLEGMDPMDK NTSPGLPYTT 1950
LGMRRTDVVD WETATLIPFA AERLEKMNNK DFSDIVYQTF LKDELRPIEK 2000
VQAAKTRIVD VPPFEHCILG RQLLGKFASK FQTQPGLELG SAIGCDPDVH 2050
WTAFGVAMQG FERVYDVDYS NFDSTHSVAV FRLLAEEFFS EENGFDPLVK 2100
DYLESLAISK HAYEEKRYLI TGGLPSGCAA TSMLNTIMNN IIIRAGLYLT 2150
YKNFEFDDVK VLSYGDDLLV ATNYQLNFDR VRTSLAKTGY KITPANKTST 2200
FPLESTLEDV VFLKRKFKKE GPLYRPVMNR EALEAMLSYY RPGTLSEKLT 2250
SITMLAVHSG KQEYDRLFAP FREVGVIVPT FESVEYRWRS LFW 2293

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
DQ294633 Genomic RNA. Translation: ABB97066.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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: July 9, 2014
This is version 126 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

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