UniProtKB - B9VUU3 (POLG_HE71)
Genome polyprotein
Functioni
Catalytic activityi
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H+ + phosphateBy similarityEC:3.6.1.15By similarity
- EC:2.7.7.48PROSITE-ProRule annotation
- Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.By similarity EC:3.4.22.29
- 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.PROSITE-ProRule annotation EC:3.4.22.28
Cofactori
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 883 | For protease 2A activityBy similarity | 1 | |
Active sitei | 901 | For protease 2A activityBy similarity | 1 | |
Metal bindingi | 918 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 920 | Zinc; structuralBy similarity | 1 | |
Active sitei | 972 | For protease 2A activityBy similarity | 1 | |
Metal bindingi | 978 | Zinc; structuralBy similarity | 1 | |
Metal bindingi | 980 | Zinc; via pros nitrogen; structuralBy similarity | 1 | |
Metal bindingi | 1381 | Zinc1 Publication | 1 | |
Metal bindingi | 1392 | Zinc1 Publication | 1 | |
Metal bindingi | 1393 | Zinc; via carbonyl oxygen1 Publication | 1 | |
Metal bindingi | 1397 | Zinc1 Publication | 1 | |
Active sitei | 1588 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1619 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1695 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Metal bindingi | 1964 | Magnesium 1; catalytic; for RdRp activityBy similarity | 1 | |
Metal bindingi | 1964 | Magnesium 2; catalytic; for RdRp activityBy similarity | 1 | |
Metal bindingi | 2060 | Magnesium 1; catalytic; for RdRp activityBy similarity | 1 | |
Metal bindingi | 2060 | Magnesium 2; catalytic; for RdRp activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1240 – 1247 | ATPPROSITE-ProRule annotation | 8 | |
Zinc fingeri | 1381 – 1397 | C4-type; degenerate1 PublicationAdd BLAST | 17 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- cysteine-type endopeptidase activity Source: UniProtKB-EC
- ion channel activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- RNA binding Source: UniProtKB-KW
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- RNA helicase activity Source: InterPro
- structural molecule activity Source: InterPro
GO - Biological processi
- clathrin-dependent endocytosis of virus by host cell Source: UniProtKB-KW
- DNA replication Source: UniProtKB-KW
- induction by virus of host autophagy Source: UniProtKB-KW
- pore formation by virus in membrane of host cell Source: UniProtKB-KW
- pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
- protein complex oligomerization Source: UniProtKB-KW
- RNA-protein covalent cross-linking Source: UniProtKB-KW
- suppression by virus of host gene expression Source: UniProtKB-KW
- suppression by virus of host MAVS activity Source: UniProtKB-KW
- suppression by virus of host MDA-5 activity Source: UniProtKB-KW
- suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
- suppression by virus of host RIG-I activity Source: UniProtKB-KW
- transcription, DNA-templated Source: InterPro
- viral RNA genome replication Source: InterPro
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Protein family/group databases
MEROPSi | C03.014 |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved into the following 17 chains: Alternative name(s): VP4-VP2 Alternative name(s): P1A Virion protein 4 Alternative name(s): P1B Virion protein 2 Alternative name(s): P1C Virion protein 3 Alternative name(s): P1D Virion protein 1 Alternative name(s): Picornain 2A Protein 2A Alternative name(s): Protein 3B Short name: P3B Protein 3CD (EC:3.4.22.28) Alternative name(s): Picornain 3CPROSITE-ProRule annotation Short name: P3CPROSITE-ProRule annotation RNA-directed RNA polymerasePROSITE-ProRule annotation (EC:2.7.7.48PROSITE-ProRule annotation) Short name: RdRp Alternative name(s): 3D polymerase Short name: 3Dpol Protein 3D Short name: 3D |
Organismi | Human enterovirus 71 (EV71) (EV-71) |
Taxonomic identifieri | 39054 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Picornavirales › Picornaviridae › Enterovirus › Enterovirus A |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Proteomesi |
|
Subcellular locationi
- Virion By similarity
- Host cytoplasm Curated
- Virion By similarity
- Host cytoplasm Curated
- Virion By similarity
- Host cytoplasm Curated
- 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.
- 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.
- 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.
- 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.
- Virion By similarity
- Host cytoplasm By similarity
- Host nucleus By similarity
- Host cytoplasm By similarity
- 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.
- 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.
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 2 – 1503 | CytoplasmicSequence analysisAdd BLAST | 1502 | |
Intramembranei | 1504 – 1519 | Sequence analysisAdd BLAST | 16 | |
Topological domaini | 1520 – 2193 | CytoplasmicSequence analysisAdd BLAST | 674 |
Keywords - Cellular componenti
Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, T=pseudo3 icosahedral capsid protein, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1246 | K → A: 85% loss of protein 2C ATPase activity and complete loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1252 | I → R: 90% loss of protein 2C ATPase activity and complete loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1287 | D → N: Complete loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1381 | C → A: Complete loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1383 | E → C: 75% loss of protein 2C ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 1383 | E → H: 75% loss of protein 2C ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 1384 | N → A: 70% loss of protein 2C ATPase activity and 80% loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1385 | N → A: No effect on protein 2C ATPase activity and increased virion production. 1 Publication | 1 | |
Mutagenesisi | 1392 | C → A: Complete loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1393 | S → A: 50% loss of protein 2C ATPase activity and increased virion production. 1 Publication | 1 | |
Mutagenesisi | 1393 | S → R: 90% loss of protein 2C ATPase activity and complete loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1394 | P → A: 50% loss of protein 2C ATPase activity and 70% loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1397 | C → A: Complete loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1399 | K → A: 50% loss of protein 2C ATPase activity and 95% loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1436 | E → A: 70% loss of protein 2C ATPase activity and complete loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1438 | L → K: 90% loss of protein 2C ATPase activity and complete loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1439 | F → A or R: 95% loss of protein 2C ATPase activity and complete loss of virion production. 1 Publication | 1 | |
Mutagenesisi | 1439 | F → Y: 85% loss of protein 2C ATPase activity and complete loss of virion production. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostBy similarity | |||
ChainiPRO_0000449070 | 2 – 2193 | Genome polyproteinAdd BLAST | 2192 | |
ChainiPRO_0000449071 | 2 – 862 | P1Add BLAST | 861 | |
ChainiPRO_0000449072 | 2 – 323 | Capsid protein VP0Add BLAST | 322 | |
ChainiPRO_0000449073 | 2 – 69 | Capsid protein VP4Add BLAST | 68 | |
ChainiPRO_0000449074 | 70 – 323 | Capsid protein VP2Add BLAST | 254 | |
ChainiPRO_0000449075 | 324 – 565 | Capsid protein VP3Add BLAST | 242 | |
ChainiPRO_0000449076 | 566 – 862 | Capsid protein VP1Add BLAST | 297 | |
ChainiPRO_0000449077 | 863 – 1440 | P2Add BLAST | 578 | |
ChainiPRO_0000449078 | 863 – 1012 | Protease 2AAdd BLAST | 150 | |
ChainiPRO_0000449079 | 1013 – 1111 | Protein 2BAdd BLAST | 99 | |
ChainiPRO_0000449080 | 1112 – 1440 | Protein 2CAdd BLAST | 329 | |
ChainiPRO_0000449081 | 1441 – 2193 | P3Add BLAST | 753 | |
ChainiPRO_0000449082 | 1441 – 1548 | Protein 3ABAdd BLAST | 108 | |
ChainiPRO_0000449083 | 1441 – 1526 | Protein 3AAdd BLAST | 86 | |
ChainiPRO_0000449084 | 1527 – 1548 | Viral protein genome-linkedAdd BLAST | 22 | |
ChainiPRO_0000449085 | 1549 – 2193 | Protein 3CDAdd BLAST | 645 | |
ChainiPRO_0000449086 | 1549 – 1731 | Protease 3CAdd BLAST | 183 | |
ChainiPRO_0000449087 | 1732 – 2193 | RNA-directed RNA polymeraseAdd BLAST | 462 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine; by hostBy similarity | 1 | |
Modified residuei | 1529 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 69 – 70 | Cleavage; by autolysisBy similarity | 2 | |
Sitei | 323 – 324 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 862 – 863 | Cleavage; by autolysisBy similarity | 2 | |
Sitei | 1012 – 1013 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1111 – 1112 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1440 – 1441 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1526 – 1527 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1548 – 1549 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1731 – 1732 | Cleavage; by protease 3CBy similarity | 2 |
Keywords - PTMi
Autocatalytic cleavage, Covalent protein-RNA linkage, Lipoprotein, Myristate, PhosphoproteinInteractioni
Subunit structurei
Interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers.
By similarityInteracts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity).
Interacts with capsid protein VP2, capsid protein VP3 and capsid protein VP4 following cleavage of capsid protein VP0 (By similarity).
Interacts with host SCARB2 (By similarity).
By similarityInteracts with capsid protein VP1 and capsid protein VP3 in the mature capsid (By similarity).
Interacts with host SCARB2 (By similarity).
By similarityInteracts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers (By similarity). Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid (By similarity).
Interacts with capsid protein VP4 in the mature capsid (By similarity).
Interacts with protein 2C; this interaction may be important for virion morphogenesis (By similarity).
By similarityInteracts with host BAX; this interaction activates the mitochondrial apoptotic pathway.
By similarityHomohexamer; forms a hexameric ring structure with 6-fold symmetry characteristic of AAA+ ATPases (Probable).
Interacts (via N-terminus) with host RTN3 (via reticulon domain); this interaction is important for viral replication (By similarity).
Interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity).
By similarity1 PublicationHomodimer (By similarity).
Interacts with host GBF1 (By similarity).
Interacts (via GOLD domain) with host ACBD3 (via GOLD domain); this interaction allows the formation of a viral protein 3A/ACBD3 heterotetramer with a 2:2 stoichiometry, which will stimulate the recruitment of host PI4KB in order to synthesize PI4P at the viral RNA replication sites (By similarity).
By similarityInteracts with host IFIH1/MDA5; this interaction inhibits host IFIH1 (By similarity).
Interacts with host DDX58 (By similarity).
By similarityInteracts with Viral protein genome-linked and with protein 3CD.
By similarityProtein-protein interaction databases
IntActi | B9VUU3, 1 interactor |
Structurei
Secondary structure
3D structure databases
SMRi | B9VUU3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1216 – 1374 | SF3 helicasePROSITE-ProRule annotationAdd BLAST | 159 | |
Domaini | 1549 – 1727 | Peptidase C3PROSITE-ProRule annotationAdd BLAST | 179 | |
Domaini | 1958 – 2073 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 116 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 566 – 588 | Amphipatic alpha-helixSequence analysisAdd BLAST | 23 | |
Regioni | 568 – 588 | Amphipatic alpha-helixSequence analysisAdd BLAST | 21 | |
Regioni | 1112 – 1250 | OligomerizationBy similarityAdd BLAST | 139 | |
Regioni | 1112 – 1184 | Membrane-bindingBy similarityAdd BLAST | 73 | |
Regioni | 1133 – 1137 | RNA-bindingBy similarity | 5 | |
Regioni | 1424 – 1431 | RNA-bindingBy similarity | 8 | |
Regioni | 1435 – 1440 | OligomerizationBy similarity | 6 | |
Regioni | 1441 – 1463 | DisorderedSequence analysisAdd BLAST | 23 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 1381 – 1397 | C4-type; degenerate1 PublicationAdd BLAST | 17 |
Keywords - Domaini
Repeat, Zinc-fingerFamily and domain databases
CDDi | cd00205, rhv_like, 3 hits |
Gene3Di | 1.10.10.870, 1 hit 2.40.10.10, 4 hits 2.60.120.20, 3 hits 3.30.70.270, 1 hit |
InterProi | View protein in InterPro IPR003593, AAA+_ATPase IPR043502, DNA/RNA_pol_sf IPR000605, Helicase_SF3_ssDNA/RNA_vir IPR014759, Helicase_SF3_ssRNA_vir IPR027417, P-loop_NTPase IPR014838, P3A IPR036203, P3A_soluble_dom IPR044067, PCV_3C_PRO IPR000081, Peptidase_C3 IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR003138, Pico_P1A IPR002527, Pico_P2B IPR001676, Picornavirus_capsid IPR043128, Rev_trsase/Diguanyl_cyclase IPR033703, Rhv-like IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR029053, Viral_coat |
Pfami | View protein in Pfam PF08727, P3A, 1 hit PF00548, Peptidase_C3, 1 hit PF02226, Pico_P1A, 1 hit PF00947, Pico_P2A, 1 hit PF01552, Pico_P2B, 1 hit PF00680, RdRP_1, 1 hit PF00073, Rhv, 3 hits PF00910, RNA_helicase, 1 hit |
SMARTi | View protein in SMART SM00382, AAA, 1 hit |
SUPFAMi | SSF50494, SSF50494, 2 hits SSF52540, SSF52540, 1 hit SSF56672, SSF56672, 1 hit SSF89043, SSF89043, 1 hit |
PROSITEi | View protein in PROSITE PS51874, PCV_3C_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit PS51218, SF3_HELICASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MGSQVSTQRS GSHENSNSAT EGSTINYTTI NYYKDSYAAT AGKQSLKQDP
60 70 80 90 100
DKFANPVKDI FTEMAAPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI
110 120 130 140 150
IVGYGEWPSY CSDSDATAVD KPTRPDVSVN RFYTLDTKLW EKSSKGWYWK
160 170 180 190 200
FPDVLTETGV FGQNAQFHYL YRSGFCIHVQ CNASKFHQGA LLVAVLPEYV
210 220 230 240 250
IGTVAGGTGT EDSHPPYKQT QPGADGFELQ HPYVLDAGIP ISQLTVCPHQ
260 270 280 290 300
WINLRTNNCA TIIVPYINAL PFDSALNHCN FGLLVVPISP LDYDQGATPV
310 320 330 340 350
IPITITLAPM CSEFAGLRQA VTQGFPTELK PGTNQFLTTD DGVSAPILPN
360 370 380 390 400
FHPTPCIHIP GEVRNLLELC QVETILEVNN VPTNATSLME RLRFPVSAQA
410 420 430 440 450
GKGELCAVFR ADPGRNGPWQ STLLGQLCGY YTQWSGSLEV TFMFTGSFMA
460 470 480 490 500
TGKMLIAYTP PGGPLPKDRA TAMLGTHVIW DFGLQSSVTL VIPWISNTHY
510 520 530 540 550
RAHARDGVFD YYTTGLVSIW YQTNYVVPIG APNTAYIIAL AAAQKNFTMK
560 570 580 590 600
LCKDASDILQ TGTIQGDRVA DVIESSIGDS VSRALTQALP APTGQNTQVS
610 620 630 640 650
SHRLDTGKVP ALQAAEIGAS SNASDESMIE TRCVLNSHST AETTLDSFFS
660 670 680 690 700
RAGLVGEIDL PLEGTTNPNG YANWDIDITG YAQMRRKVEL FTYMRFDAEF
710 720 730 740 750
TFVACTPTGE VVPQLLQYMF VPPGAPKPDS RESLAWQTAT NPSVFVKLSD
760 770 780 790 800
PPAQVSVPFM SPASAYQWFY DGYPTFGEHK QEKDLEYGAC PNNMMGTFSV
810 820 830 840 850
RTVGTSKSKY PLVVRIYMRM KHVRAWIPRP MRNQNYLFKA NPNYAGNSIK
860 870 880 890 900
PTGTSRTAIT TLGKFGQQSG AIYVGNFRVV NRHLATHNDW ANLVWEDSSR
910 920 930 940 950
DLLVSSTTAQ GCDTIARCNC QTGVYYCNSR RKHYPVSFSK PSLIYVEASE
960 970 980 990 1000
YYPARYQSHL MLAQGHSEPG DCGGILRCQH GVVGIVSTGG NGLVGFADVR
1010 1020 1030 1040 1050
DLLWLDEEAM EQGVSDYIKG LGDAFGTGFT DAVSREVEAL KSYLIGSEGA
1060 1070 1080 1090 1100
VEKILKNLIK LISALVIVIR SDYDMVTLTA TLALIGCHGS PWAWIKAKTA
1110 1120 1130 1140 1150
SILGIPIAQK QSASWLKKFN DMANAAKGLE WVSNKISKFI DWLKEKIVPA
1160 1170 1180 1190 1200
AKEKVEFLNN LKQLPLLENQ ISNLEQSAAS QEDLEVMFGN VSYLAHFCRK
1210 1220 1230 1240 1250
FQPLYATEAK RVYALEKRMN NYMQFKSKHR IEPVCLIIRG SPGTGKSLAT
1260 1270 1280 1290 1300
GIIARAIADK YHSSVYSLPP DPDHFDGYKQ QVVTVMDDLC QNPDGKDMSL
1310 1320 1330 1340 1350
FCQMVSTVDF IPPMASLEEK GVSFTSKFVI ASTNATNIIV PTVSDSDAIR
1360 1370 1380 1390 1400
RRFYMDCDIE VTDSYKTDLG RLDAGRAAKL CSENNTANFK RCSPLVCGKA
1410 1420 1430 1440 1450
IQLRDRKSKV RYSVDTVVSE LIREYSNRSA IGNTIEALFQ GPPKFRPIRI
1460 1470 1480 1490 1500
GLEEKPAPDA ISDLLASVDS EEVRQYCRDQ GWIIPETPTN VERHLNRAVL
1510 1520 1530 1540 1550
VMQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPKQVLKKP ALRTATVQGP
1560 1570 1580 1590 1600
SLDFALSLLR RNVRQVQTDQ GHFTMLGVRD RLAVLPRHSQ PGKTIWIEHK
1610 1620 1630 1640 1650
LVNVLDAVEL VDEQGVNLEL TLITLDTNEK FRDITKFIPE NISTASDATL
1660 1670 1680 1690 1700
VINTEHMPSM FVPVGDVVQY GFLNLSGKPT HRTMMYNFPT KAGQCGGVVT
1710 1720 1730 1740 1750
SVGKVIGIHI GGNGRQGFCA GLKRSYFASE QGEIQWVKPN KETGRLNING
1760 1770 1780 1790 1800
PTRTKLEPSV FHDVFEGSKE PAVLHSKDPR LEVDFEQALF SKYVGNTLHV
1810 1820 1830 1840 1850
PDEYIREAAL HYANQLKQLD IDTTQMSMEE ACYGTDNLEA IDLHTSAGYP
1860 1870 1880 1890 1900
YSALGIKKRD ILDPTTRDVS KMKFYMDKYG LDLPYSTYVK DELRSIDKIK
1910 1920 1930 1940 1950
KGKSRLIEAS SLNDSVYLRM AFGHLYETFH ANPGTVTGSA VGCNPDVFWS
1960 1970 1980 1990 2000
KLPILLPGSL FAFDYSGYDA SLSPVWFRAL ELVLREIGYS EEAVSLIEGI
2010 2020 2030 2040 2050
NHTHHVYRNK TYCVLGGMPS GCSGTSIFNT MINNIIIRAL LIKTFKGIDL
2060 2070 2080 2090 2100
DELNMVAYGD DVLASYPFPI DCLELAKTGK EYGLTMTPAD KSPCFNEVNW
2110 2120 2130 2140 2150
ENATFLKRGF LPDEQFPFLI HPTMPMKEIH ESIRWTKDAR NTQDHVRSLC
2160 2170 2180 2190
LLAWHNGKQE YEKFVSSIRS VPIGKALAIP NYENLRRNWL ELF
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | FJ606450 Genomic RNA Translation: ACM62759.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | FJ606450 Genomic RNA Translation: ACM62759.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
5GQ1 | X-ray | 2.49 | A/B/C/D/E/F | 1227-1440 | [»] | |
5GRB | X-ray | 2.80 | A/B/C/D/E/F | 1227-1440 | [»] | |
SMRi | B9VUU3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | B9VUU3, 1 interactor |
Protein family/group databases
MEROPSi | C03.014 |
Family and domain databases
CDDi | cd00205, rhv_like, 3 hits |
Gene3Di | 1.10.10.870, 1 hit 2.40.10.10, 4 hits 2.60.120.20, 3 hits 3.30.70.270, 1 hit |
InterProi | View protein in InterPro IPR003593, AAA+_ATPase IPR043502, DNA/RNA_pol_sf IPR000605, Helicase_SF3_ssDNA/RNA_vir IPR014759, Helicase_SF3_ssRNA_vir IPR027417, P-loop_NTPase IPR014838, P3A IPR036203, P3A_soluble_dom IPR044067, PCV_3C_PRO IPR000081, Peptidase_C3 IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR003138, Pico_P1A IPR002527, Pico_P2B IPR001676, Picornavirus_capsid IPR043128, Rev_trsase/Diguanyl_cyclase IPR033703, Rhv-like IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR029053, Viral_coat |
Pfami | View protein in Pfam PF08727, P3A, 1 hit PF00548, Peptidase_C3, 1 hit PF02226, Pico_P1A, 1 hit PF00947, Pico_P2A, 1 hit PF01552, Pico_P2B, 1 hit PF00680, RdRP_1, 1 hit PF00073, Rhv, 3 hits PF00910, RNA_helicase, 1 hit |
SMARTi | View protein in SMART SM00382, AAA, 1 hit |
SUPFAMi | SSF50494, SSF50494, 2 hits SSF52540, SSF52540, 1 hit SSF56672, SSF56672, 1 hit SSF89043, SSF89043, 1 hit |
PROSITEi | View protein in PROSITE PS51874, PCV_3C_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit PS51218, SF3_HELICASE_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | POLG_HE71 | |
Accessioni | B9VUU3Primary (citable) accession number: B9VUU3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 26, 2020 |
Last sequence update: | March 24, 2009 | |
Last modified: | April 7, 2021 | |
This is version 93 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families