UniProtKB - A5LGW7 (POLG_HAVJ8)
Genome polyprotein
Functioni
Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these 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. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.
By similarityCapsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these 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. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.
By similarityCapsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these 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. The naked capsid interacts with the host receptor HAVCR1 to provide virion attachment to and probably entry into the target cell.
By similarityVP0 precursor is a component of the immature procapsids.
By similarityPlays a role in the assembly of the 12 pentamers into an icosahedral structure. Has not been detected in mature virions, supposedly owing to its small size.
By similarityPrecursor component of immature procapsids that corresponds to an extended form of the structural protein VP1. After maturation, possibly by the host Cathepsin L, the assembly signal 2A is cleaved to give rise to the mature VP1 protein.
By similarityFunctions as a viroporin. Affects membrane integrity and causes an increase in membrane permeability. Involved in host intracellular membrane rearrangements probably to give rise to the viral factories. Does not disrupt calcium homeostasis or glycoprotein trafficking. Antagonizes the innate immune response of the host by suppressing IFN-beta synthesis, which it achieves by interfering with the DDX58/IFIH1 (RIG-I/MDA5) pathway.
By similarityAffects membrane integrity and causes an increase in membrane permeability.
By similarityAssociates with and induces structural rearrangements of intracellular membranes. Displays RNA-binding activity.
By similarityThe precursor 3ABC is targeted to the mitochondrial membrane where protease 3C activity cleaves and inhibits the host antiviral protein MAVS, thereby disrupting activation of IRF3 through the IFIH1/MDA5 pathway. In vivo, the protease activity of 3ABC precursor is more efficient in cleaving the 2BC precursor than that of protein 3C. The 3ABC precursor may therefore play a role in the proteolytic processing of the polyprotein. Possible viroporin.
By similarityInteracts with the 3CD precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Since the 3AB precursor contains the hydrophobic domain 3A, it probably anchors the whole viral replicase complex to intracellular membranes on which viral RNA synthesis occurs.
By similarityMay serve as membrane anchor to the 3AB and 3ABC precursors via its hydrophobic domain. May interact with RNA.
By similarityActs as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome.
By similarityCysteine 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. Cleaves IKBKG/NEMO to impair innate immune signaling. Cleaves host PABPC1 which may participate in the switch of viral translation to RNA synthesis.
By similarityInteracts with the 3AB precursor and with RNA structures found at both the 5'- and 3'-termini of the viral genome. Disrupts TLR3 signaling by degrading the host adapter protein TICAM1/TRIF.
By similarityRNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.
By similarityMiscellaneous
Caution
Catalytic activityi
- a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)PROSITE-ProRule annotationBy similarityEC:2.7.7.48PROSITE-ProRule annotationBy similarity
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H+ + phosphateBy similarityEC:3.6.1.15By similarity
- 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
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 769 | Important for VP1 folding and capsid assemblyBy similarity | 1 | |
Active sitei | 1563 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1603 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1691 | For protease 3C activityPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1230 – 1237 | ATPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- cysteine-type endopeptidase activity Source: UniProtKB-EC
- ion channel activity Source: UniProtKB-KW
- nucleoside-triphosphatase activity Source: RHEA
- 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
- pore formation by virus in membrane of host cell Source: UniProtKB-KW
- protein complex oligomerization Source: UniProtKB-KW
- RNA-protein covalent cross-linking Source: UniProtKB-KW
- suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity Source: UniProtKB-KW
- transcription, DNA-templated Source: InterPro
- viral entry into host cell Source: UniProtKB-KW
- viral RNA genome replication Source: InterPro
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Protein family/group databases
MEROPSi | C03.005 |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved into the following 18 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): VPX Alternative name(s): P1D Virion protein 1 Alternative name(s): pXBy similarity Alternative name(s): Protein 3B Short name: P3B Alternative name(s): Picornain 3C |
Organismi | Human hepatitis A virus genotype IIIB (isolate HAJ85-1) (HHAV) (Human hepatitis A virus (isolate Human/Japan/HAJ85-1/1985)) |
Taxonomic identifieri | 474341 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Picornavirales › Picornaviridae › Hepatovirus › |
Virus hosti | Cercopithecus hamlyni (Owl-faced monkey) (Hamlyn's monkey) [TaxID: 9536] Homo sapiens (Human) [TaxID: 9606] Macaca (macaques) [TaxID: 9539] Pan troglodytes (Chimpanzee) [TaxID: 9598] |
Proteomesi |
|
Subcellular locationi
- Virion By similarity
- host multivesicular body By similarity Note: The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies.By similarity
- Virion By similarity
- host multivesicular body By similarity Note: The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies.By similarity
- Virion By similarity
- host multivesicular body By similarity Note: The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies.By similarity
- Virion By similarity Note: Present in the full mature virion. The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies.By similarity
- Host membrane By similarity; Peripheral membrane protein By similarity Note: Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication.By similarity
- Host membrane By similarity; Single-pass membrane protein By similarity Note: Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. May associate with membranes through a N-terminal amphipathic helix.By similarity
- Host membrane By similarity; Single-pass membrane protein Sequence analysis
- Host mitochondrion outer membrane By similarity; Single-pass membrane protein By similarity Note: Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication.By similarity
- Host membrane By similarity; Single-pass membrane protein Sequence analysis Note: Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication.By similarity
- Host membrane By similarity; Single-pass membrane protein Sequence analysis Note: Probably localizes to intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication.By similarity
- Virion By similarity
- Host cytoplasm By similarity
- Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity Note: Interacts with membranes in a complex with viral protein 3AB. 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 1011 – 1031 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 1462 – 1482 | HelicalSequence analysisAdd BLAST | 21 |
Keywords - Cellular componenti
Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host endosome, Host membrane, Host mitochondrion, Host mitochondrion outer membrane, Membrane, T=pseudo3 icosahedral capsid protein, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000310636 | 1 – 2228 | Genome polyproteinAdd BLAST | 2228 | |
ChainiPRO_0000310637 | 1 – 245 | Capsid protein VP0Add BLAST | 245 | |
ChainiPRO_0000310638 | 1 – 23 | Capsid protein VP4Add BLAST | 23 | |
ChainiPRO_0000310639 | 24 – 245 | Capsid protein VP2Add BLAST | 222 | |
ChainiPRO_0000310640 | 246 – 491 | Capsid protein VP3Add BLAST | 246 | |
ChainiPRO_0000310641 | 492 – 836 | Protein VP1-2AAdd BLAST | 345 | |
ChainiPRO_0000310642 | 492 – 765 | Capsid protein VP1Add BLAST | 274 | |
ChainiPRO_0000310643 | 766 – 836 | Assembly signal 2AAdd BLAST | 71 | |
ChainiPRO_0000310644 | 837 – 1422 | Protein 2BCAdd BLAST | 586 | |
ChainiPRO_0000310645 | 837 – 1087 | Protein 2BAdd BLAST | 251 | |
ChainiPRO_0000310646 | 1088 – 1422 | Protein 2CAdd BLAST | 335 | |
ChainiPRO_0000310647 | 1423 – 2228 | Protein 3ABCDAdd BLAST | 806 | |
ChainiPRO_0000310648 | 1423 – 1739 | Protein 3ABCAdd BLAST | 317 | |
ChainiPRO_0000310649 | 1423 – 1519 | Protein 3ABAdd BLAST | 97 | |
ChainiPRO_0000310650 | 1423 – 1496 | Protein 3AAdd BLAST | 74 | |
ChainiPRO_0000310651 | 1497 – 1519 | Viral protein genome-linkedAdd BLAST | 23 | |
ChainiPRO_0000310652 | 1520 – 2228 | Protein 3CDAdd BLAST | 709 | |
ChainiPRO_0000310653 | 1520 – 1739 | Protease 3CAdd BLAST | 220 | |
ChainiPRO_0000310654 | 1740 – 2228 | RNA-directed RNA polymerase 3D-POLAdd BLAST | 489 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1499 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 | |
Disulfide bondi | 1543 | InterchainBy similarity |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 23 – 24 | CleavageSequence analysis | 2 | |
Sitei | 245 – 246 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 491 – 492 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 765 – 766 | Cleavage; partial; by hostBy similarity | 2 | |
Sitei | 836 – 837 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1087 – 1088 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1422 – 1423 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1496 – 1497 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1519 – 1520 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1739 – 1740 | Cleavage; by protease 3CBy similarity | 2 |
Keywords - PTMi
Covalent protein-RNA linkage, Disulfide bond, PhosphoproteinInteractioni
Subunit structurei
Homodimer. Homomultimer; probably interacts with membranes in a multimeric form. Seems to assemble into amyloid-like fibers.
By similarityInteracts with capsid protein VP2.
Interacts with capsid protein VP3.
By similarityInteracts with capsid protein VP1.
Interacts with capsid protein VP3.
By similarityInteracts with capsid protein VP1.
Interacts with capsid protein VP2.
By similarityFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1204 – 1366 | SF3 helicasePROSITE-ProRule annotationAdd BLAST | 163 | |
Domaini | 1514 – 1728 | Peptidase C3PROSITE-ProRule annotationAdd BLAST | 215 | |
Domaini | 1977 – 2098 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 122 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 56 – 76 | DisorderedSequence analysisAdd BLAST | 21 | |
Regioni | 766 – 836 | Involved in P1-2A pentamerizationBy similarityAdd BLAST | 71 | |
Regioni | 1043 – 1070 | Membrane-penetrating abilityBy similarityAdd BLAST | 28 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 1127 – 1152 | Sequence analysisAdd BLAST | 26 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 167 – 171 | (L)YPX(n)L motifBy similarity | 5 | |
Motifi | 200 – 205 | (L)YPX(n)L motifBy similarity | 6 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Coiled coil, Transmembrane, Transmembrane helixFamily and domain databases
CDDi | cd00205, rhv_like, 2 hits |
Gene3Di | 2.40.10.10, 2 hits 2.60.120.20, 3 hits 3.30.70.270, 1 hit |
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR004004, Helic/Pol/Pept_Calicivir-typ IPR000605, Helicase_SF3_ssDNA/RNA_vir IPR014759, Helicase_SF3_ssRNA_vir IPR024354, Hepatitis_A_VP1-2A IPR044067, PCV_3C_PRO IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin 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 PF12944, HAV_VP, 1 hit PF00548, Peptidase_C3, 1 hit PF00680, RdRP_1, 1 hit PF00073, Rhv, 2 hits PF00910, RNA_helicase, 1 hit |
PRINTSi | PR00918, CALICVIRUSNS |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF56672, SSF56672, 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
MNMSRQGIFQ TVGSGLDHIL SLADVEEEQM IQSVDRTAVT GASYFTSVDQ
60 70 80 90 100
SSVHTAEVGA HQSEPLKTSV DKPGSKRTQG EKFFLIHSAD WLTTHALFHE
110 120 130 140 150
VAKLDVVKLL YNEQFAVQGL LRYHTYARFG IEIQVQINPT PFQQGGLICA
160 170 180 190 200
MVPGDQSYGS IASLTVYPHG LLNCNINNVV RIKVPFIYTR GAYHFKDPQY
210 220 230 240 250
PVWELTIRVW SELNIGTGTS AYTSLNVLAR FTDLELHGLT PLSTQMMRNE
260 270 280 290 300
FRVSTTENVV NLSNYEDARA KMSFALDQED WKSDASQGGG IKITHFTTWT
310 320 330 340 350
SIPTLAAQFP FNASDSVGQQ IKVIPVDPYF FQMTNTNPEQ KCITALASIC
360 370 380 390 400
QMFCFWRGDL VFDFQVFPTK YHSGRLLFCF VPGNELIDVS HITLKQATTA
410 420 430 440 450
PCAVMDITGV QSTLRFRVPW ISDTPYRVNR YTKSSHQKGE YTAIGKLIVY
460 470 480 490 500
CYNRLTSPSN VASHVRVNVY LSAINLECFA PLYHAMDVTT QVGDDSGGFS
510 520 530 540 550
TTVSTKQNVP DPQVGITTVR DLKGKANQGK MDVSGVQAPV GAITTIEDPV
560 570 580 590 600
LAKKVPETFP ELKPGESRHT SDHMSIYKFM GRSHFLCTFT FNSNNKEYTF
610 620 630 640 650
PITLSSTSNP PHGLPSTLRW FFNLFQLYRG PLDLTIIITG ATDVDGMAWF
660 670 680 690 700
TPVGLAVDTP WVEKESALSI DYKTALGAVR FNTRRTGNIQ IRLPWYSYLY
710 720 730 740 750
AVSGALDGLG DKTDSTFGLV SIQIANYNHS DEYLSFSCYL SVTEQSEFYF
760 770 780 790 800
PRAPLNTNAM MSSETMLDRI ALGDLESSVD DPRSEEDRKF ESHIEKRKPY
810 820 830 840 850
KELRLEVGKQ RLKYAQEELS NEVLPPPRKI KGVFSQAKIS LFYTEDHEIM
860 870 880 890 900
KFSWKGITAD TRALRRFGFS LAAGRSVWTL EMDAGVLTGR LVRVNDEKWT
910 920 930 940 950
EMKDDKIVSL VEKFTSNKHW SKINFPHGML DLEEIAANSK EFPNMSETDL
960 970 980 990 1000
CFLLHWLNPK KINLADRMLG MSGIQEIKEK GVGLIGECRA FLDSITTTLK
1010 1020 1030 1040 1050
SMMFGFHHSV TVEIINTVLC FVKSGILLYV IQQLNQEEHS HIIGLLRVMN
1060 1070 1080 1090 1100
YADIGCSVIS CGKVFSKMLE TVFNWQMDSR MMELRTQSIS NWLRDICSGI
1110 1120 1130 1140 1150
TIFKSFKDAI YWLYTRIREY YDVNYGNKKD VLNILKDNQQ KIERAIEEAD
1160 1170 1180 1190 1200
NFCVLQIQDV EKFEQYQKGV DLIQKLRTVH SMAQVDPGLT VHLAPLRDCI
1210 1220 1230 1240 1250
ARVHQKLKNL GSINQAMVTR CEPVVCYLYG KRGGGKSLTS IALATKICKH
1260 1270 1280 1290 1300
YGVEPEKNIY TKPVASDYWD GYSGQLVCII DDIGQNTTDE DWSDFCQLVS
1310 1320 1330 1340 1350
GCPMRLNMAS LEEKGRHFSS PFIIATSNWS NPSPKTVYVK EAIDRRLHFK
1360 1370 1380 1390 1400
VEVKPASFFK NPHNDMLNVN LAKTNDAIKD MSCVDLVMDS HNISLSELLS
1410 1420 1430 1440 1450
SLVMTVEIRK QNMSEFMELW SQGMSDDDND SAVAEFFQSF PSGEPSGSKL
1460 1470 1480 1490 1500
SRFFQSVTNH KWVAVGAAVG VLGVLVGGWY VYKHFTKKKE EPIPSEGVYH
1510 1520 1530 1540 1550
GVTKPKQVIK LDADPVESQS TLEIAGLVRK NLVQFGVGEK NGCVRWVMNA
1560 1570 1580 1590 1600
LGIKDDWLLV PSHAYKFEKD YEMMEFYFNR GGTYYSISAG NVVIQSLDVG
1610 1620 1630 1640 1650
FQDVVLMKVP TIPKFRDITE HFIKKSDVPR ALNRLATLVT TVNGTPMLIS
1660 1670 1680 1690 1700
EGPLKMEEKA TYVHKKNDGT TIDLTVDQAW RGKGEGLPGM CGGALISSNQ
1710 1720 1730 1740 1750
SIQNAILGIH VAGGNSILVA KLVTQEMFQN IDKKIVESQR IMKVEFTQCS
1760 1770 1780 1790 1800
MNVVSKTLFK KSPIHHHIDK NMINFPAVMP FSRAEIDPMA VMLSKYSLPI
1810 1820 1830 1840 1850
VDEPEDYKDV SVFFQNKILG KSPLVDDFLD IEMAITGAPG IDAINMDSSP
1860 1870 1880 1890 1900
GYPYVQEKLT KRDLIWLDDN GMFLGVHPRL AQRILFNTTM MENCSDLDVV
1910 1920 1930 1940 1950
FTTCPKDELR PLDKVLESKT RAIDSCPLDY TILCRMYWGP AISYFHLNPG
1960 1970 1980 1990 2000
FHTGVAIGID PDRQWDQLFK TMIRFGDVGL DLDFSAFDAS LSPFMIREAG
2010 2020 2030 2040 2050
RILTEMSGAP NHFGEALINT IIYSKHLLYN CCYHVYGSMP SGSPCTALLN
2060 2070 2080 2090 2100
SIINNVNLYY VFSKIFKKSP VFFCDAIRIL CYGDDVLIVF SRQVQFDNLD
2110 2120 2130 2140 2150
SIGQRIVDEF RKLGMTATSA DKSVPQLKPV SELTFLKRSF NLVDDRIRPA
2160 2170 2180 2190 2200
IAEKTIWSLV AWQRSNAEFE QNLENAQWFA FMHGYEFYQD FYHFVQSCLE
2210 2220
KEMIEYRLKS YDWWRMKFND QCFVCDLS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB279735 Genomic RNA Translation: BAF63623.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB279735 Genomic RNA Translation: BAF63623.1 |
3D structure databases
BMRBi | A5LGW7 |
SMRi | A5LGW7 |
ModBasei | Search... |
Protein family/group databases
MEROPSi | C03.005 |
Family and domain databases
CDDi | cd00205, rhv_like, 2 hits |
Gene3Di | 2.40.10.10, 2 hits 2.60.120.20, 3 hits 3.30.70.270, 1 hit |
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR004004, Helic/Pol/Pept_Calicivir-typ IPR000605, Helicase_SF3_ssDNA/RNA_vir IPR014759, Helicase_SF3_ssRNA_vir IPR024354, Hepatitis_A_VP1-2A IPR044067, PCV_3C_PRO IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin 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 PF12944, HAV_VP, 1 hit PF00548, Peptidase_C3, 1 hit PF00680, RdRP_1, 1 hit PF00073, Rhv, 2 hits PF00910, RNA_helicase, 1 hit |
PRINTSi | PR00918, CALICVIRUSNS |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF56672, SSF56672, 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | POLG_HAVJ8 | |
Accessioni | A5LGW7Primary (citable) accession number: A5LGW7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 13, 2007 |
Last sequence update: | July 10, 2007 | |
Last modified: | February 23, 2022 | |
This is version 88 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |