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Protein

Genome polyprotein

Gene
N/A
Organism
Plum pox potyvirus (isolate NAT) (PPV)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Capsid protein: involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication.
Helper component proteinase: 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 similarity
Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication.
Nuclear inclusion protein A: has RNA-binding and proteolytic activities.

Catalytic activityi

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.
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei216 – 2161For P1 proteinase activityBy similarity
Active sitei225 – 2251For P1 proteinase activitySequence analysis
Active sitei259 – 2591For P1 proteinase activityBy similarity
Active sitei652 – 6521For helper component proteinase activityPROSITE-ProRule annotation
Active sitei725 – 7251For helper component proteinase activityPROSITE-ProRule annotation
Active sitei2095 – 20951For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2130 – 21301For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2200 – 22001For nuclear inclusion protein A activityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1253 – 12608ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Suppressor of RNA silencing, Thiol protease, Transferase

Keywords - Biological processi

Viral RNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.4.22.45. 4919.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 10 chains:
Alternative name(s):
N-terminal protein
Helper component proteinase (EC:3.4.22.45)
Short name:
HC-pro
6 kDa protein 1
Short name:
6K1
6 kDa protein 2
Short name:
6K2
Alternative name(s):
VPg
Nuclear inclusion protein A (EC:3.4.22.44)
Short name:
NI-a
Short name:
NIa
Alternative name(s):
49 kDa proteinase
Short name:
49 kDa-Pro
NIa-pro
Nuclear inclusion protein B (EC:2.7.7.48)
Short name:
NI-b
Short name:
NIb
Alternative name(s):
RNA-directed RNA polymerase
Capsid protein
Short name:
CP
Alternative name(s):
Coat protein
OrganismiPlum pox potyvirus (isolate NAT) (PPV)
Taxonomic identifieri12213 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePotyviridaePotyvirus
Virus hostiPrunus armeniaca (Apricot) (Armeniaca vulgaris) [TaxID: 36596]
Prunus cerasifera (cherry plum) [TaxID: 36595]
Prunus domestica (Garden plum) [TaxID: 3758]
Prunus glandulosa [TaxID: 105665]
Prunus persica (Peach) (Amygdalus persica) [TaxID: 3760]
Prunus salicina [TaxID: 88123]
Prunus spinosa (Blackthorn) (Prunus domestica var. spinosa) [TaxID: 114937]
Proteomesi
  • UP000006685 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Helical capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31253125Genome polyproteinPRO_0000420007Add
BLAST
Chaini1 – 308308P1 proteinaseSequence analysisPRO_0000040331Add
BLAST
Chaini309 – 766458Helper component proteinaseSequence analysisPRO_0000040332Add
BLAST
Chaini767 – 1116350Protein P3By similarityPRO_0000040333Add
BLAST
Chaini1117 – 1168526 kDa protein 1By similarityPRO_0000040334Add
BLAST
Chaini1169 – 1803635Cytoplasmic inclusion proteinBy similarityPRO_0000040335Add
BLAST
Chaini1804 – 1856536 kDa protein 2By similarityPRO_0000040336Add
BLAST
Chaini1857 – 2049193Viral genome-linked proteinBy similarityPRO_0000040337Add
BLAST
Chaini2050 – 2292243Nuclear inclusion protein ABy similarityPRO_0000040338Add
BLAST
Chaini2293 – 2810518Nuclear inclusion protein BBy similarityPRO_0000040339Add
BLAST
Chaini2811 – 3125315Capsid proteinBy similarityPRO_0000040340Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1919 – 19191O-(5'-phospho-RNA)-tyrosineBy similarity

Post-translational modificationi

VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).By similarity
Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO polyprotein is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei308 – 3092Cleavage; by P1 proteinaseSequence analysis
Sitei766 – 7672Cleavage; by autolysisPROSITE-ProRule annotation
Sitei1116 – 11172Cleavage; by NIa-proBy similarity
Sitei1168 – 11692Cleavage; by NIa-proBy similarity
Sitei1803 – 18042Cleavage; by NIa-proBy similarity
Sitei1856 – 18572Cleavage; by NIa-proBy similarity
Sitei2049 – 20502Cleavage; by NIa-proBy similarity
Sitei2292 – 22932Cleavage; by NIa-proBy similarity
Sitei2810 – 28112Cleavage; by NIa-proBy similarity

Keywords - PTMi

Covalent protein-RNA linkage, Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliP17766.
SMRiP17766. Positions 2058-2271.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini644 – 766123Peptidase C6PROSITE-ProRule annotationAdd
BLAST
Domaini1240 – 1392153Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1411 – 1570160Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2050 – 2268219Peptidase C4PROSITE-ProRule annotationAdd
BLAST
Domaini2534 – 2658125RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi360 – 3634Involved in interaction with stylet and aphid transmissionBy similarity
Motifi618 – 6203Involved in virions binding and aphid transmissionBy similarity
Motifi1342 – 13454DECH box
Motifi1897 – 19048Nuclear localization signalSequence analysis

Domaini

The N-terminus of helper component proteinase is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus.

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 peptidase C4 domain.PROSITE-ProRule annotation
Contains 1 peptidase C6 domain.PROSITE-ProRule annotationCurated
Contains 1 peptidase S30 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR001456. HC-pro.
IPR031159. HC_PRO_CPD_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR002540. Pept_S30_P1_potyvir.
IPR009003. Peptidase_S1_PA.
IPR001592. Poty_coat.
IPR001730. Potyv_NIa-pro_dom.
IPR013648. PP_Potyviridae.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
[Graphical view]
PfamiPF07652. Flavi_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.
PF00680. RdRP_1. 1 hit.
[Graphical view]
PRINTSiPR00966. NIAPOTYPTASE.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51744. HC_PRO_CPD. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51436. POTYVIRUS_NIA_PRO. 1 hit.
PS50507. RDRP_SSRNA_POS. 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: P17766-1) [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
MSTIVFGSFT CHLDAAIHQD NADRLAKAWT RPENRQVSNA HLLCRRAAES
60 70 80 90 100
LINTYESATA SAWKGLEEKL QPMFAKREFS KTVTKRKGLR CFKESSEKFI
110 120 130 140 150
EKKLRKQYQE ERERLQFLNG PDAIVNQISV DKCEASVRVP SPHIIEKPSF
160 170 180 190 200
VTPSMKKKVV FKKVRMSEAS LQLFMRRVAA NAKANGQKVE IIGRKRVVGN
210 220 230 240 250
YTTKSRLTYF RTHVRHLDGS KPRYDLVLDE ATKKILQLFA NTSGFHHVHK
260 270 280 290 300
KGEVTPGMSG FVVNPMNLSD PMQVYDTDLF IVRGKHNSIL VDSRCKVSKK
310 320 330 340 350
QSNEIIHYSD PGKQFSDGFT NSFMQCKLRE TDHQCTSDLD VKECGYVAAL
360 370 380 390 400
VCQAIIPCGK ITCLQCAQKY SYMSQQEIRD RFSTVIEQHE KTVMDNYPQF
410 420 430 440 450
SHVLAFLKRY RELMRVENQN YEAFKDITHM IGERKEAPFS HLNKINELII
460 470 480 490 500
KGGMMSAQDY IEASDHLREL ARYQKNRTEN IRSGSIKAFR NKISSKAHVN
510 520 530 540 550
MQLMCDNQLD TNGNFVWGQR EYHAKRFFRN YFDVIDVSEG YRRHIVRENP
560 570 580 590 600
RGIRKLAIGN LVMSTNLAAL RKQLLGEECI HFEVSKECTS KRGENFVYQC
610 620 630 640 650
CCVTHEDGTP LESEIISPTK NHLVVGNSGD SKYVDLPTAK GGAMFIAKAG
660 670 680 690 700
YCYINIFLAM LININEDEAK SFTKTVRDTL VPKLGTWPSM MDLATACHFL
710 720 730 740 750
AVLYPETRNA ELPRILVDHE AKIFHVVDSF GSLSTGMHVL KANTINQLIS
760 770 780 790 800
FASDTLDSNM KTYLVGGLEV DKCDEFKNVK LLIRSIYKPQ IMEQVLKEEP
810 820 830 840 850
YLLLMSVLSP GVLMALFNSG SLEKATQYWI TRSHSLAAIT SMLSALAAKV
860 870 880 890 900
SLASTLNAQM SVIDEHAAVL YDSVFVGTQP YASYMMAVKT LERMKARTES
910 920 930 940 950
DHTLNDLGFS VLRQATPHLV EKSYLQELEQ AWKELSWSEK FSAILESQRW
960 970 980 990 1000
RKHIPKPFIP KDGADLGGRY DISVRSLLGN QYKRLRDVVR WKRDDVVCYT
1010 1020 1030 1040 1050
YQSMGKLFCK AIGISPSFLP STLKMLDMLI VFSLLLSIGA TCNSMVNEHK
1060 1070 1080 1090 1100
HLKQLAADRE DKKRFKRLQV LYTRLSEKVG CTPTADEFLE YVGDENPDLL
1110 1120 1130 1140 1150
KHAEDLIGDG QVVVHQSKRD SQANLERVVA FVALVMMLFD SERSDGVYKI
1160 1170 1180 1190 1200
LNKLKGIMGS VDRAVHHQSL DDIEDILDEK KLTVDFVLQS NEVAPTVPFD
1210 1220 1230 1240 1250
STFEKWWMNQ LETGNVIPHY RTEGHFLEFT RENAAHIANE VMHGSHQDIL
1260 1270 1280 1290 1300
IRGAVGSGKS TGLPFHLSKK GHVLLIEPTR PLAENVCKQL RGQPFNVNPT
1310 1320 1330 1340 1350
LRMRGMSTFG STPITVMTSG YALHFLANNP TYLDNYKCII FDECHVHDAS
1360 1370 1380 1390 1400
AMAFRCLLSE YSYPGKILKV SATPPGHEVE FKTQKEVKVI VEESLSFQQF
1410 1420 1430 1440 1450
VSNLGTGCNS DILKHGVNVL VYVASYNEVD TLSKLLTDRS FKVSKVDGRT
1460 1470 1480 1490 1500
MKVGNVEIPT SGTQAKPHFV VATNIIENGV TLDIDVVVDF GLKVVPVLDI
1510 1520 1530 1540 1550
DNRLVRYTKK SISYGERIQR LGRVGRNKPG AALRIGFTEK GLTQIPPIIA
1560 1570 1580 1590 1600
TEAAFLCFTY GLPVMTNGVS TSLLAMCTVK QARTMQQFEL SPFYTVALVR
1610 1620 1630 1640 1650
FDGTMHQEIF RLLKSYRLRD SEVILNKLAI PNSNVCGWMS VRDYKRQGCN
1660 1670 1680 1690 1700
LDLDENIRVP FYVKDIPETL HERIWQAVET HKSDAGFGRI CSSSACKIAY
1710 1720 1730 1740 1750
TLQTDIHSIP RTIKIIDALL EQERTKQAHF RAMTSQSCSS SNFSLSSITS
1760 1770 1780 1790 1800
AIRSKYAKDH TEENIGVLQM AKSQLLEFKN LNIDPSYPEL IRNFGALECV
1810 1820 1830 1840 1850
HHQTKEGVSK ALQLKGHWNK RLITRDATLM LGVLGGGAWM IFSYLRDSFK
1860 1870 1880 1890 1900
EEVIHQGFNR RQRQKLKFRQ ARDNRMAREV YGDDSTMEAY FGSAYSKKGK
1910 1920 1930 1940 1950
SKGKTRGMGT KTRKFVNMYG YDPTDYNFVR FVDPLTGHTL DESPLMDINL
1960 1970 1980 1990 2000
VQEHFSQIRN DYIGDDKITM QHIMSNPGIV AYYIKDATQK ALKVDLTPHN
2010 2020 2030 2040 2050
PLRVCDKTAT IAGFPEREFE LRQTGHPVFV EPNAIPKINE EGDEEVDHES
2060 2070 2080 2090 2100
KSLFRGLRDY NPIASSICQL NNSSGARQSE MFGLGFGGLI VTNQHLFKRN
2110 2120 2130 2140 2150
DGELTIRSHH GEFVVKDTKT LKLLPCKGRD IVIIRLPKDF PPFPRRLQFR
2160 2170 2180 2190 2200
TPTTEDRVCL IGSNFQTKSI SSTMSETSAT YPVDNSHFWK HWISTKDGHC
2210 2220 2230 2240 2250
GLPIVSTRDG SILGLHSLAN STNTQNFYAA FPDNFETTYL SNQDNDNWIK
2260 2270 2280 2290 2300
QWRYNPDEVC WGSLQLKRDI PQSPFTICKL LTDLDGEFVY TQSKTTHWLR
2310 2320 2330 2340 2350
DRLEGNLKAV GACPGQLVTK HVVKGKCTLF ETYLLTHPEE HEFFRPLMGA
2360 2370 2380 2390 2400
YQKSALNKDA YVKDLMKYSK PIVVGAVDCD QFERAVDVVI SMLISKGFEE
2410 2420 2430 2440 2450
CNYVTDPDDI FSALNMKAAV GALYSGKKRD YFENVSDQDK ESFVRASCKR
2460 2470 2480 2490 2500
LFMGKKGVWN GSLKAELRPK EKVEANKTRS FTAAPIDTLL GGKVCVDDFN
2510 2520 2530 2540 2550
NQFYSLNLHC PWSVGMTKFR GGWDKLLKAL PEGWIYCDAD GSQFDSSLSP
2560 2570 2580 2590 2600
YLINAVLNIR LAFMEEWDIG EQMLSNLYTE IVYTPIATPD GTIVKKFKGN
2610 2620 2630 2640 2650
NSGQPSTVVD NTLMVILAMT YSLLKLGHHP DTHDCICRYF VNGDDLVLAV
2660 2670 2680 2690 2700
HPAYESIYDE LQEHFSQLGL NYTFTTKTEN KEELWFMSHK GVLYDDMYIP
2710 2720 2730 2740 2750
KLEPERIVSI LEWDRSNEPI HRLEAICASM VEAWGYKELL REIRKFYSWV
2760 2770 2780 2790 2800
LEQAPYNALS KDGKAPYIAE TALKKLYTDT EASETEIERY LEAFYDNIND
2810 2820 2830 2840 2850
DGESNVVVHQ ADEREDEEEV DALQPPPVIQ PAPRTTAPML NPIFTPATTQ
2860 2870 2880 2890 2900
PATKPVSQVS GPQLQTFGTY SHEDASPSNS NALVNTNRDR DVDAGSTGTF
2910 2920 2930 2940 2950
TVPRLKAMTS KLSLPKVKGK AIMNLNHLAH YSPAQVDLSN TRAPQSCFQT
2960 2970 2980 2990 3000
WYEGVKRDYD VTDDEMSIIL NGLMVWCIEN GTSPNINGMW VMMDGETQVE
3010 3020 3030 3040 3050
YPIKPLLDHA KPTFRQIMAH FSNVAEAYIE KRNYEKAYMP RYGIQRNLTD
3060 3070 3080 3090 3100
YSLARYAFDF YEMTSTTPVR AREAHIQMKA AALRNVQNRL FGLDGNVGTQ
3110 3120
EEDTERHTAG DVNRNMHNLL GMRGV
Note: Produced by conventional translation.
Length:3,125
Mass (Da):354,266
Last modified:August 1, 1990 - v1
Checksum:iED0DD33C439CB712
GO
Isoform P3N-PIPO polyprotein (identifier: P0CK02-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry P0CK02.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshifting in P3 ORF.
Length:1,020
Mass (Da):116,033
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13751 Genomic RNA. Translation: BAA02898.1.
PIRiJQ0003. GNVSPP.
RefSeqiNP_040807.1. NC_001445.1.

Genome annotation databases

GeneIDi1494049.
KEGGivg:1494049.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13751 Genomic RNA. Translation: BAA02898.1.
PIRiJQ0003. GNVSPP.
RefSeqiNP_040807.1. NC_001445.1.

3D structure databases

ProteinModelPortaliP17766.
SMRiP17766. Positions 2058-2271.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1494049.
KEGGivg:1494049.

Enzyme and pathway databases

BRENDAi3.4.22.45. 4919.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011492. DEAD_Flavivir.
IPR001456. HC-pro.
IPR031159. HC_PRO_CPD_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR002540. Pept_S30_P1_potyvir.
IPR009003. Peptidase_S1_PA.
IPR001592. Poty_coat.
IPR001730. Potyv_NIa-pro_dom.
IPR013648. PP_Potyviridae.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
[Graphical view]
PfamiPF07652. Flavi_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.
PF00680. RdRP_1. 1 hit.
[Graphical view]
PRINTSiPR00966. NIAPOTYPTASE.
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51744. HC_PRO_CPD. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51436. POTYVIRUS_NIA_PRO. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete nucleotide sequence of plum pox virus RNA."
    Maiss E., Timpe U., Brisske A., Jelkmann W., Casper R., Himmler G., Mattanovich D., Katinger H.W.D.
    J. Gen. Virol. 70:513-524(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Cited for: REVIEW.

Entry informationi

Entry nameiPOLG_PPVNA
AccessioniPrimary (citable) accession number: P17766
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: October 14, 2015
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.