UniProtKB - Q02597 (POLG_TUMVQ)
Genome polyprotein
Functioni
Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
An RNA-dependent RNA polymerase that plays an essential role in the virus replication.
Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity (By similarity).
By similarityHas helicase activity. It may be involved in replication (By similarity).
By similarityBoth 6K peptides are indispensable for virus replication.
By similarityHas RNA-binding and proteolytic activities.
Recruits the host translation initiation complex for viral genome translation by binding to host plant eIF4E/eIF(iso)4E and eIF4G/eIF(iso)4G proteins.
2 PublicationsCatalytic activityi
- EC:2.7.7.48PROSITE-ProRule annotation
- Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved. EC:3.4.22.44
- Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein. EC:3.4.22.45
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 270 | For P1 proteinase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 279 | For P1 proteinase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 313 | For P1 proteinase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 706 | For helper component proteinase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 779 | For helper component proteinase activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2161 | For nuclear inclusion protein A activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2196 | For nuclear inclusion protein A activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2266 | For nuclear inclusion protein A activityPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1313 – 1320 | ATPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- cysteine-type endopeptidase activity Source: InterPro
- helicase activity Source: UniProtKB-KW
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides Source: InterPro
- RNA binding Source: InterPro
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- serine-type peptidase activity Source: UniProtKB-KW
- structural molecule activity Source: InterPro
GO - Biological processi
- modulation by virus of host process Source: UniProtKB
- RNA-protein covalent cross-linking Source: UniProtKB-KW
- transcription, DNA-templated Source: InterPro
- viral RNA genome replication Source: InterPro
Keywordsi
Molecular function | Helicase, Hydrolase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Suppressor of RNA silencing, Thiol protease, Transferase |
Biological process | Host-virus interaction, Viral RNA replication |
Ligand | ATP-binding, Nucleotide-binding |
Protein family/group databases
MEROPSi | C04.001 |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved into the following 10 chains: P1 proteinase (EC:3.4.-.-) Alternative name(s): N-terminal protein Alternative name(s): VPg Alternative name(s): 49 kDa proteinase Short name: 49 kDa-Pro NIa-pro Alternative name(s): RNA-directed RNA polymerase Alternative name(s): Coat protein |
Organismi | Turnip mosaic virus (strain Quebec) (TuMV) |
Taxonomic identifieri | 36396 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Stelpaviricetes › Patatavirales › Potyviridae › Potyvirus › |
Virus hosti | Brassica [TaxID: 3705] |
Proteomesi |
|
Subcellular locationi
- Host nucleus By similarity Note: Binds to host plant eIF4E proteins in the host nucleus.By similarity
- Virion Curated
Keywords - Cellular componenti
Capsid protein, Helical capsid protein, Host nucleus, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000420030 | 1 – 3163 | Genome polyproteinAdd BLAST | 3163 | |
ChainiPRO_0000040473 | 1 – 362 | P1 proteinaseSequence analysisAdd BLAST | 362 | |
ChainiPRO_0000040474 | 363 – 820 | Helper component proteinaseSequence analysisAdd BLAST | 458 | |
ChainiPRO_0000040475 | 821 – 1175 | Protein P3By similarityAdd BLAST | 355 | |
ChainiPRO_0000040476 | 1176 – 1227 | 6 kDa protein 1By similarityAdd BLAST | 52 | |
ChainiPRO_0000040477 | 1228 – 1870 | Cytoplasmic inclusion proteinBy similarityAdd BLAST | 643 | |
ChainiPRO_0000040478 | 1871 – 1923 | 6 kDa protein 2By similarityAdd BLAST | 53 | |
ChainiPRO_0000040479 | 1924 – 2115 | Viral genome-linked proteinBy similarityAdd BLAST | 192 | |
ChainiPRO_0000040480 | 2116 – 2358 | Nuclear inclusion protein ABy similarityAdd BLAST | 243 | |
ChainiPRO_0000040481 | 2359 – 2875 | Nuclear inclusion protein BBy similarityAdd BLAST | 517 | |
ChainiPRO_0000040482 | 2876 – 3163 | Capsid proteinBy similarityAdd BLAST | 288 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1986 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 362 – 363 | Cleavage; by P1 proteinasePROSITE-ProRule annotation | 2 | |
Sitei | 820 – 821 | Cleavage; by autolysisPROSITE-ProRule annotation | 2 | |
Sitei | 1175 – 1176 | Cleavage; by NIa-proBy similarity | 2 | |
Sitei | 1227 – 1228 | Cleavage; by NIa-proBy similarity | 2 | |
Sitei | 1870 – 1871 | Cleavage; by NIa-proBy similarity | 2 | |
Sitei | 2115 – 2116 | Cleavage; by NIa-proBy similarity | 2 | |
Sitei | 2358 – 2359 | Cleavage; by NIa-proBy similarity | 2 | |
Sitei | 2875 – 2876 | Cleavage; by NIa-proBy similarity | 2 |
Keywords - PTMi
Covalent protein-RNA linkage, PhosphoproteinInteractioni
Subunit structurei
Interacts with host eIF4E proteins in the host nucleus; this interaction is possible in susceptible hosts but is impaired in resistant plants.
By similarityStructurei
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 219 – 362 | Peptidase S30PROSITE-ProRule annotationAdd BLAST | 144 | |
Domaini | 698 – 820 | Peptidase C6PROSITE-ProRule annotationAdd BLAST | 123 | |
Domaini | 1300 – 1452 | Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST | 153 | |
Domaini | 1471 – 1630 | Helicase C-terminalPROSITE-ProRule annotationAdd BLAST | 160 | |
Domaini | 2116 – 2334 | Peptidase C4PROSITE-ProRule annotationAdd BLAST | 219 | |
Domaini | 2600 – 2724 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 125 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2883 – 2934 | DisorderedSequence analysisAdd BLAST | 52 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 414 – 417 | Involved in interaction with stylet and aphid transmissionBy similarity | 4 | |
Motifi | 672 – 674 | Involved in virions binding and aphid transmissionBy similarity | 3 | |
Motifi | 1402 – 1405 | DECH box | 4 | |
Motifi | 1964 – 1971 | Nuclear localization signalSequence analysis | 8 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 2883 – 2930 | Basic and acidic residuesSequence analysisAdd BLAST | 48 |
Domaini
Sequence similaritiesi
Family and domain databases
Gene3Di | 2.40.10.10, 2 hits 3.30.70.270, 1 hit 3.40.50.300, 2 hits 3.90.70.150, 1 hit |
InterProi | View protein in InterPro IPR011545, DEAD/DEAH_box_helicase_dom IPR043502, DNA/RNA_pol_sf IPR001456, HC-pro IPR031159, HC_PRO_CPD_dom IPR042308, HC_PRO_CPD_sf IPR014001, Helicase_ATP-bd IPR001650, Helicase_C IPR027417, P-loop_NTPase IPR002540, Pept_S30_P1_potyvir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001592, Poty_coat IPR001730, Potyv_NIa-pro_dom IPR039560, Potyvirid-P3 IPR013648, PP_Potyviridae IPR043128, Rev_trsase/Diguanyl_cyclase IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus |
Pfami | View protein in Pfam PF00270, DEAD, 1 hit PF00271, Helicase_C, 1 hit PF00863, Peptidase_C4, 1 hit PF00851, Peptidase_C6, 1 hit PF01577, Peptidase_S30, 1 hit PF00767, Poty_coat, 1 hit PF08440, Poty_PP, 1 hit PF13608, Potyvirid-P3, 1 hit PF00680, RdRP_1, 1 hit |
PRINTSi | PR00966, NIAPOTYPTASE |
SMARTi | View protein in SMART SM00487, DEXDc, 1 hit SM00490, HELICc, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 2 hits SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51744, HC_PRO_CPD, 1 hit PS51192, HELICASE_ATP_BIND_1, 1 hit PS51194, HELICASE_CTER, 1 hit PS51436, POTYVIRUS_NIA_PRO, 1 hit PS51871, PV_P1_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsiribosomal frameshifting. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MAAVTFASAI TNAITNKTTS TGMVQFGSFP PMPLRSTTVT TVATPVGQPK
60 70 80 90 100
LYTVRFGSLD PVIVKGGAGS LAKATRQQPS VEIDVSLSEA AALEVAKPKS
110 120 130 140 150
SAVLRMHEEA NKERALFLDW EASLKRRSYG IAENEKVVMT TRGVSKIVPR
160 170 180 190 200
SSRAMKQKRA RERRRAQQPI ILKWEPKLSG FSIGGGFSAS AIEAEEVRTK
210 220 230 240 250
WPLHKTPSMK KRMVHKTCKM SDQGVDMLIR SLVKIFKAKS ANIEYIGKKP
260 270 280 290 300
IKVDFIRKER TKFARIQVAH LLGKRAQRDL LAGMEENHFI DILSEYSGNG
310 320 330 340 350
TTINPGVVCA GWSGIVVRNE TLTQKRSRSP SKAFVIRGEH EDKLYDARIK
360 370 380 390 400
ITKTMSLKIV HFSARGANFW KGFDRCFLAY RSDNREHTCY SGLDVTECGE
410 420 430 440 450
VAALMCLAMF PCGKITCPDC VIDSELSQGQ ASGPSMKHRL TQLRDVIKSS
460 470 480 490 500
YPRFKHAVQI LDRYEQSLSS ANENYQDFAE IQSISDGVEK AAFPHVNKLN
510 520 530 540 550
AILIKGATAT GEEFSQATKH LLEIARYLKN RTENIEKGSL KSFRNKVSQK
560 570 580 590 600
AHINPTLMCD NQLDKNGNFI WGERGYHAKR FFSNYFEIID PKKGYTQYET
610 620 630 640 650
RVVPNGSRKL AIGKLIVPTN FEVLREQMRG EPVEPYPVTV ECVSKSQGDF
660 670 680 690 700
VHACCCVTTE SGDPVLSEIK MPTKHHLVIG NSGDPKYIDL PEIEENKMYI
710 720 730 740 750
AKEGYCYINI FLAMLVNVKE SQAKEFTKVV RDKLVSELGK WPTLLDVATA
760 770 780 790 800
CYFLKVFYPD VANAELPRML VDHKTKIIHV VDSYGSLSTG YHVLKTNTVE
810 820 830 840 850
QLIKFTRCNL ESSLKHYRVG GTEWENAHGA DNIDNPQWCI KRLVKGVYRP
860 870 880 890 900
KQLKEDMLAN PFLPLYALLS PGVILAFYNS GSLEHLMNHY ISADSNVAVL
910 920 930 940 950
LVVLKSLAKK VSTSQSVLAQ LQIIERSLPE LIEAKANING PDDAATRACN
960 970 980 990 1000
RFMGMLLHMA EPNYELANGG YTFLRDHSIS ILEKSYLQIL DEAWNELSWS
1010 1020 1030 1040 1050
ERCVIRYYPS KQAIFTQKDL PMQSEADLGG RYSESVISSY EWSKQQAKGV
1060 1070 1080 1090 1100
KDSVVNKLRS SMSWTSSKVS NSVCRTINYL VPDVFKFMNV LVCISLLIKM
1110 1120 1130 1140 1150
TAEANHIITT QRRLKLDIEE TERKKIEWEL AFHHNILTHS ASQHPTLDEF
1160 1170 1180 1190 1200
TAYIAEKAPH LSEHIEPEEK EVVHQAKRQS EQELERVIAF VALVLMMFDA
1210 1220 1230 1240 1250
ERSDCVTKIL NKLKGLVATV EPTVYHQTLN EIEDDLNERN LFVDFELSSD
1260 1270 1280 1290 1300
SEMLQQLPAE KTFASWWSHQ LSRGFTIPHY RTEGKFMTFT RATATEVAGK
1310 1320 1330 1340 1350
IAHESDKDIL LMGAVGSGKS TGLPYHLSRK GNVLLLEPTR PLAENVHKQL
1360 1370 1380 1390 1400
SQAPFHQNTT LRMRGLTAFG SAPISVMTSG FALNYFANNR SRIEEFDFVI
1410 1420 1430 1440 1450
FDECHVHDAN AMAMRCLIHE CDYSGKIIKV SATPPGREVE FSTQYPVSIS
1460 1470 1480 1490 1500
TEDTLSFQDF VNAQGSGSNC DVISKGDNIL VYVASYNEVD TLSKLLIERD
1510 1520 1530 1540 1550
FKVTKVDGRT MKVGNIEITT SGTPSRKHFI VATNIIENGV TLDIDVVADF
1560 1570 1580 1590 1600
GTKVLPYLDT DNRMLSTTKT SINYGERIQR LGRVGRHKPG HALRIGHTER
1610 1620 1630 1640 1650
GLSEVPSCIA TEAALKCFTY GLPVITNNVS TSILGNVTVK QARTMSVFEI
1660 1670 1680 1690 1700
TPFYTSQVVR YDGSMHPQVH ALLKRFKLRD SEIVLTKLAI PNRGVNAGSQ
1710 1720 1730 1740 1750
PVSMHDSVQM LKIGVTLRIP FMCRDIPEKL HLDMWDVVVK FKGDAGFGRL
1760 1770 1780 1790 1800
SSSASKVAYT LQTDVNSIQR TVTIIDTLIA EERRKQEYFK TVTSNCVSSS
1810 1820 1830 1840 1850
NFSLQSITNA IKSRMMKDHP CENISVLEGA KSQLLEFRNL NSDHSFVTKT
1860 1870 1880 1890 1900
DGISRSFMRD YGALEAVNHQ STNEMSKFLQ LKGKWNKTLI TRDVLVICGV
1910 1920 1930 1940 1950
LGGGVWMVVQ HFRSKVSEPV THEAKGKKQR QKLKFRNARD NKMGREVYGD
1960 1970 1980 1990 2000
DDTIEHFFGD AYTKKGKSKG RTRGIGHKNR KFINMYGFDP EDFSAVRFVD
2010 2020 2030 2040 2050
PLTGATLDDN PFTDITLVQK HFGDIRMDLL GEDELDSNEI RMNKTIQAYY
2060 2070 2080 2090 2100
MNNKTGKALK VDLTPHIPLK VCDLHATIAG FPERENELRQ TGKAQPINID
2110 2120 2130 2140 2150
EVPRANNELV PVDHESNSMF RGLRDYNPIS NNICHLTNVS DGASNSLYGV
2160 2170 2180 2190 2200
GFGPLILTNR HLFERNNGEL IIKSRHGEFV IKNTTQLHLL PIPDRDLLLI
2210 2220 2230 2240 2250
RLPKDVPPFP QKLGFRQPEK GERICMVGSN FQTKSITSIV SETSTIMPVE
2260 2270 2280 2290 2300
NSQFWKHWIS TKDGQCGSPM VSTKDGKILG LHSLANFQNS INYFAAFPDD
2310 2320 2330 2340 2350
FTEKYLHTIE AHEWVKHWKY NTSAISWGSL NIQASQPVSL FKVSKLISDL
2360 2370 2380 2390 2400
DSTAVYAQTQ QNRWMFEQLT GNLKAIAHCP SQLVTKHTVK GKCQMFDLYL
2410 2420 2430 2440 2450
KLHDEAREYF QPMLGQYQKS KLNREAYAKD LLKYATPIEA GNIDCDLFEK
2460 2470 2480 2490 2500
TVEIVISDLR GYGFETCNYV TDENDIFEAL NMKSAVGALY KGKKKDYFAE
2510 2520 2530 2540 2550
FTPEVKEEIL KQSCERLFLG KMGVWNGSLK AELRPLEKVE ANKTRTFTAA
2560 2570 2580 2590 2600
PLDTLLGGKV CVDDFNNQFY DHNLRAPWDV GMTKFYCGWD RLLESLPDGW
2610 2620 2630 2640 2650
VYCDADGSQF DSSLSPYLIN AVLNIRLGFM EEWDVGEVML RNLYTEIVYT
2660 2670 2680 2690 2700
PISTPDGTLV KKFKGNNSGQ PSTVVDNTLM VILAVNYSLK KGGIPSELRD
2710 2720 2730 2740 2750
SIIRFFVNGD DLLLSVHPEY EYILDTMADN FRELGLKYTF DSRTREKGDL
2760 2770 2780 2790 2800
WFMSHQGHRR EGIWIPKLEP ERIVSILEWD RSKEPCHRLE AICAAMIESW
2810 2820 2830 2840 2850
GYDKLTHEIR KFYAWMIEQA PFSSLAQEGK APYIAETALR KLYLDKEPAQ
2860 2870 2880 2890 2900
EDLTQYLQAI FEDYEDGVEA CVYHQAGETL DADLTEEQKQ AEKEKKEREK
2910 2920 2930 2940 2950
AEKERERQKQ LAFKKGKDVA QEEGKRDKEV NAGTSGTFSV PRLKSLTSKM
2960 2970 2980 2990 3000
RVPRYEKRVA LNLDHLILYT PEQTDLSNTR STRKQFDTWF EGVMADYELT
3010 3020 3030 3040 3050
EDKMQIILNG LRVWCIENGT SPNINGMWVM MDGDDQVEFP IKPLIDHAKP
3060 3070 3080 3090 3100
TFRQIMAHFS DVAEAYIEKR NQDRPYMPRY GLQRNLTDMS LARYAFDFYE
3110 3120 3130 3140 3150
MTSRTPIRAR EAHIQMKAAA LRGANNNLFG LDGNVGTTVE NTERHTTEDV
3160
NRNMHNLLGV QGL
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 2862 | E → G in BAA01452 (PubMed:2254757).Curated | 1 |
Polymorphismi
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural varianti | 2039 | E → Q in TuMV-E116Q. 1 Publication | 1 | |
Natural varianti | 2086 | N → Y in TuMV-N163Y. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10927 Genomic RNA Translation: BAA01725.1 D10601 Genomic RNA Translation: BAA01452.1 |
PIRi | JQ1895 |
Keywords - Coding sequence diversityi
Ribosomal frameshiftingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10927 Genomic RNA Translation: BAA01725.1 D10601 Genomic RNA Translation: BAA01452.1 |
PIRi | JQ1895 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein family/group databases
MEROPSi | C04.001 |
Family and domain databases
Gene3Di | 2.40.10.10, 2 hits 3.30.70.270, 1 hit 3.40.50.300, 2 hits 3.90.70.150, 1 hit |
InterProi | View protein in InterPro IPR011545, DEAD/DEAH_box_helicase_dom IPR043502, DNA/RNA_pol_sf IPR001456, HC-pro IPR031159, HC_PRO_CPD_dom IPR042308, HC_PRO_CPD_sf IPR014001, Helicase_ATP-bd IPR001650, Helicase_C IPR027417, P-loop_NTPase IPR002540, Pept_S30_P1_potyvir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001592, Poty_coat IPR001730, Potyv_NIa-pro_dom IPR039560, Potyvirid-P3 IPR013648, PP_Potyviridae IPR043128, Rev_trsase/Diguanyl_cyclase IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus |
Pfami | View protein in Pfam PF00270, DEAD, 1 hit PF00271, Helicase_C, 1 hit PF00863, Peptidase_C4, 1 hit PF00851, Peptidase_C6, 1 hit PF01577, Peptidase_S30, 1 hit PF00767, Poty_coat, 1 hit PF08440, Poty_PP, 1 hit PF13608, Potyvirid-P3, 1 hit PF00680, RdRP_1, 1 hit |
PRINTSi | PR00966, NIAPOTYPTASE |
SMARTi | View protein in SMART SM00487, DEXDc, 1 hit SM00490, HELICc, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 2 hits SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51744, HC_PRO_CPD, 1 hit PS51192, HELICASE_ATP_BIND_1, 1 hit PS51194, HELICASE_CTER, 1 hit PS51436, POTYVIRUS_NIA_PRO, 1 hit PS51871, PV_P1_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | POLG_TUMVQ | |
Accessioni | Q02597Primary (citable) accession number: Q02597 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
Last sequence update: | June 1, 1994 | |
Last modified: | February 23, 2022 | |
This is version 158 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- SIMILARITY comments
Index of protein domains and families