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P12296

- POLG_ENMGO

UniProt

P12296 - POLG_ENMGO

Protein

Genome polyprotein

Gene
N/A
Organism
Mengo encephalomyocarditis virus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (20 Mar 2007)
      Previous versions | rss
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    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

    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

    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

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12296.

    Topological domain

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

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei1566 – 158419Sequence AnalysisAdd
    BLAST

    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

    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: October 1, 2014
    This is version 127 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