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Protein

Genome polyprotein

Gene
N/A
Organism
Mengo encephalomyocarditis virus
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei1674For protease 3C activitySequence analysis1
Active sitei1706For protease 3C activitySequence analysis1
Active sitei1787For protease 3C activitySequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1314 – 1321ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

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 virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeCardiovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Mus musculus (Mouse) [TaxID: 10090]
Oryctolagus cuniculus (Rabbit) [TaxID: 9986]
Proteomesi
  • UP000008663 Componenti: Genome

Subcellular locationi

Protein 2A :
Protein 2B :
Protein 2C :
Protein 3A :
Protein 3B :
RNA-directed RNA polymerase 3D-POL :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 1565CytoplasmicSequence analysisAdd BLAST1565
Intramembranei1566 – 1584Sequence analysisAdd BLAST19
Topological domaini1585 – 2293CytoplasmicSequence analysisAdd BLAST709

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
ChainiPRO_50001410821 – 67Leader proteinSequence analysisAdd BLAST67
ChainiPRO_000031096568 – 393Protein VP0Sequence analysisAdd BLAST326
ChainiPRO_500014108368 – 137Protein VP4Sequence analysisAdd BLAST70
ChainiPRO_5000141084138 – 393Protein VP2Sequence analysisAdd BLAST256
ChainiPRO_5000141085394 – 624Protein VP3Sequence analysisAdd BLAST231
ChainiPRO_5000141086625 – 901Protein VP1Sequence analysisAdd BLAST277
ChainiPRO_5000141087902 – 1044Protein 2ASequence analysisAdd BLAST143
ChainiPRO_50001410881045 – 1195Protein 2BSequence analysisAdd BLAST151
ChainiPRO_50001410891196 – 1520Protein 2CSequence analysisAdd BLAST325
ChainiPRO_50001410901521 – 1608Protein 3ASequence analysisAdd BLAST88
ChainiPRO_50001410911609 – 1628Protein 3BSequence analysisAdd BLAST20
ChainiPRO_50001410921629 – 1833Protease 3CSequence analysisAdd BLAST205
ChainiPRO_50001410931834 – 2293RNA-directed RNA polymerase 3D-POLSequence analysisAdd BLAST460

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi68N-myristoyl glycine; by hostBy similarity1
Modified residuei1611O-(5'-phospho-RNA)-tyrosineBy similarity1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei137 – 138CleavageSequence analysis2
Sitei393 – 394Cleavage; by protease 3CSequence analysis2
Sitei624 – 625Cleavage; by protease 3CSequence analysis2
Sitei901 – 902Cleavage; by protease 3CSequence analysis2
Sitei1044 – 1045Cleavage; by ribosomal skipSequence analysis2
Sitei1195 – 1196Cleavage; by protease 3CSequence analysis2
Sitei1520 – 1521Cleavage; by protease 3CSequence analysis2
Sitei1608 – 1609Cleavage; by protease 3CSequence analysis2
Sitei1628 – 1629Cleavage; by protease 3CSequence analysis2
Sitei1833 – 1834Cleavage; by protease 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRIDEiP12296.

Structurei

Secondary structure

12293
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 3Combined sources3
Beta strandi8 – 10Combined sources3
Turni11 – 13Combined sources3
Helixi16 – 18Combined sources3
Helixi20 – 24Combined sources5
Turni26 – 30Combined sources5
Beta strandi32 – 34Combined sources3
Beta strandi36 – 40Combined sources5
Helixi41 – 45Combined sources5
Beta strandi46 – 48Combined sources3
Turni54 – 57Combined sources4
Beta strandi60 – 62Combined sources3
Turni63 – 65Combined sources3
Beta strandi78 – 80Combined sources3
Helixi94 – 97Combined sources4
Beta strandi115 – 117Combined sources3
Beta strandi124 – 126Combined sources3
Beta strandi133 – 135Combined sources3
Helixi148 – 150Combined sources3
Beta strandi152 – 155Combined sources4
Beta strandi160 – 165Combined sources6
Beta strandi169 – 171Combined sources3
Helixi172 – 174Combined sources3
Helixi194 – 196Combined sources3
Beta strandi200 – 208Combined sources9
Beta strandi216 – 221Combined sources6
Helixi223 – 225Combined sources3
Helixi228 – 230Combined sources3
Helixi231 – 237Combined sources7
Beta strandi240 – 252Combined sources13
Beta strandi260 – 269Combined sources10
Turni286 – 290Combined sources5
Helixi309 – 314Combined sources6
Beta strandi315 – 321Combined sources7
Turni322 – 324Combined sources3
Beta strandi326 – 332Combined sources7
Beta strandi337 – 341Combined sources5
Helixi343 – 345Combined sources3
Beta strandi349 – 360Combined sources12
Beta strandi368 – 385Combined sources18
Turni402 – 405Combined sources4
Helixi437 – 439Combined sources3
Turni440 – 442Combined sources3
Beta strandi455 – 460Combined sources6
Beta strandi466 – 468Combined sources3
Beta strandi470 – 476Combined sources7
Helixi480 – 482Combined sources3
Helixi486 – 491Combined sources6
Beta strandi494 – 499Combined sources6
Beta strandi501 – 507Combined sources7
Beta strandi514 – 522Combined sources9
Beta strandi524 – 526Combined sources3
Helixi532 – 535Combined sources4
Beta strandi538 – 544Combined sources7
Beta strandi546 – 548Combined sources3
Beta strandi550 – 555Combined sources6
Beta strandi560 – 567Combined sources8
Turni573 – 575Combined sources3
Beta strandi579 – 589Combined sources11
Beta strandi598 – 606Combined sources9
Beta strandi611 – 615Combined sources5
Helixi629 – 631Combined sources3
Turni639 – 642Combined sources4
Beta strandi654 – 656Combined sources3
Helixi657 – 661Combined sources5
Beta strandi665 – 670Combined sources6
Helixi676 – 678Combined sources3
Beta strandi685 – 688Combined sources4
Beta strandi690 – 694Combined sources5
Helixi703 – 705Combined sources3
Beta strandi727 – 729Combined sources3
Beta strandi731 – 733Combined sources3
Helixi736 – 740Combined sources5
Beta strandi745 – 758Combined sources14
Beta strandi765 – 770Combined sources6
Beta strandi788 – 790Combined sources3
Beta strandi792 – 794Combined sources3
Beta strandi796 – 799Combined sources4
Beta strandi808 – 812Combined sources5
Beta strandi817 – 824Combined sources8
Beta strandi848 – 854Combined sources7
Beta strandi860 – 873Combined sources14
Beta strandi894 – 896Combined sources3
Beta strandi1836 – 1838Combined sources3
Helixi1859 – 1862Combined sources4
Beta strandi1865 – 1868Combined sources4
Helixi1882 – 1885Combined sources4
Helixi1886 – 1890Combined sources5
Helixi1899 – 1916Combined sources18
Helixi1925 – 1930Combined sources6
Beta strandi1933 – 1935Combined sources3
Beta strandi1940 – 1942Combined sources3
Turni1946 – 1952Combined sources7
Helixi1955 – 1958Combined sources4
Turni1961 – 1964Combined sources4
Helixi1968 – 1978Combined sources11
Beta strandi1987 – 1991Combined sources5
Beta strandi1994 – 1997Combined sources4
Helixi1998 – 2002Combined sources5
Beta strandi2008 – 2011Combined sources4
Helixi2014 – 2031Combined sources18
Turni2037 – 2040Combined sources4
Helixi2047 – 2058Combined sources12
Beta strandi2061 – 2068Combined sources8
Turni2072 – 2075Combined sources4
Helixi2078 – 2087Combined sources10
Helixi2091 – 2093Combined sources3
Helixi2099 – 2107Combined sources9
Beta strandi2108 – 2113Combined sources6
Beta strandi2116 – 2122Combined sources7
Beta strandi2126 – 2128Combined sources3
Helixi2131 – 2150Combined sources20
Helixi2156 – 2158Combined sources3
Beta strandi2160 – 2164Combined sources5
Beta strandi2167 – 2174Combined sources8
Helixi2178 – 2186Combined sources9
Turni2187 – 2189Combined sources3
Beta strandi2195 – 2197Combined sources3
Turni2207 – 2209Combined sources3
Beta strandi2215 – 2220Combined sources6
Beta strandi2223 – 2228Combined sources6
Helixi2230 – 2238Combined sources9
Helixi2245 – 2256Combined sources12
Helixi2257 – 2259Combined sources3
Helixi2261 – 2273Combined sources13
Helixi2281 – 2290Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2MMHNMR-A1-67[»]
2MMINMR-A1-67[»]
2MMKNMR-A1-67[»]
2MMLNMR-A1-67[»]
4NYZX-ray2.15A1834-2293[»]
4NZ0X-ray2.80A/B/C/D/E/F1834-2293[»]
4Y2CX-ray2.20A1834-2293[»]
4Y3CX-ray3.20A/B/C/D/E/F1834-2293[»]
ProteinModelPortaliP12296.
SMRiP12296.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12296.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1282 – 1448SF3 helicasePROSITE-ProRule annotationAdd BLAST167
Domaini2062 – 2180RdRp catalyticPROSITE-ProRule annotationAdd BLAST119

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

CDDicd00205. rhv_like. 3 hits.
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.
IPR009003. Peptidase_S1_PA.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
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. AlignAdd to basket

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
PDB 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[»]
2MMHNMR-A1-67[»]
2MMINMR-A1-67[»]
2MMKNMR-A1-67[»]
2MMLNMR-A1-67[»]
4NYZX-ray2.15A1834-2293[»]
4NZ0X-ray2.80A/B/C/D/E/F1834-2293[»]
4Y2CX-ray2.20A1834-2293[»]
4Y3CX-ray3.20A/B/C/D/E/F1834-2293[»]
ProteinModelPortaliP12296.
SMRiP12296.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC03.009.

Proteomic databases

PRIDEiP12296.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP12296.

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
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.
IPR009003. Peptidase_S1_PA.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
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]
ProtoNetiSearch...

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 30, 2016
This is version 139 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.