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Protein

Genome polyprotein

Gene
N/A
Organism
Blackberry virus Y (isolate Blackberry plant/USA:Arkansas/C3ARK/2005) (BVY)
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.By similarity
Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication.By similarity
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 (By similarity).By similarity
Both 6K peptides are indispensable for virus replication.By similarity
Nuclear inclusion protein A: has RNA-binding and proteolytic activities.By similarity

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.

Cofactori

Fe2+PROSITE-ProRule annotationNote: Binds 1 Fe2+ ion per subunit.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi201 – 2011IronPROSITE-ProRule annotation
Metal bindingi203 – 2031IronPROSITE-ProRule annotation
Metal bindingi259 – 2591IronPROSITE-ProRule annotation
Binding sitei268 – 26812-oxoglutaratePROSITE-ProRule annotation
Active sitei956 – 9561For helper component proteinase activityPROSITE-ProRule annotation
Active sitei1029 – 10291For helper component proteinase activityPROSITE-ProRule annotation
Active sitei2400 – 24001For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2435 – 24351For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2504 – 25041For nuclear inclusion protein A activityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1553 – 15608ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Viral RNA replication

Keywords - Ligandi

ATP-binding, Iron, Metal-binding, Nucleotide-binding

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
OrganismiBlackberry virus Y (isolate Blackberry plant/USA:Arkansas/C3ARK/2005) (BVY)
Taxonomic identifieri686949 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePotyviridaeBrambyvirus
Virus hostiRubus plicatus [TaxID: 211815]
Proteomesi
  • UP000006703 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 – 34913491Genome polyproteinPRO_0000419995Add
BLAST
Chaini1 – 745745P1 proteinasePRO_5000147981Add
BLAST
Chaini746 – 1070325Helper component proteinasePRO_5000147982Add
BLAST
Chaini1071 – 1420350Protein P3PRO_5000147983Add
BLAST
Chaini1421 – 1476566 kDa protein 1PRO_5000147984Add
BLAST
Chaini1477 – 2096620Cytoplasmic inclusion proteinPRO_5000147985Add
BLAST
Chaini2097 – 2163676 kDa protein 2PRO_5000147986Add
BLAST
Chaini2164 – 2353190Viral genome-linked proteinPRO_5000147987Add
BLAST
Chaini2354 – 2590237Nuclear inclusion protein APRO_5000147988Add
BLAST
Chaini2591 – 3143553Nuclear inclusion protein BPRO_5000147989Add
BLAST
Chaini3144 – 3491348Capsid proteinPRO_5000147990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2238 – 22381O-(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
Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten 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
Sitei745 – 7462Cleavage; by P1 proteinaseSequence analysis
Sitei1070 – 10712Cleavage; by autolysisPROSITE-ProRule annotation
Sitei1420 – 14212Cleavage; by NIa-proBy similarity
Sitei1476 – 14772Cleavage; by NIa-proBy similarity
Sitei2096 – 20972Cleavage; by NIa-proBy similarity
Sitei2163 – 21642Cleavage; by NIa-proBy similarity
Sitei2353 – 23542Cleavage; by NIa-proBy similarity
Sitei2590 – 25912Cleavage; by NIa-proBy similarity
Sitei3143 – 31442Cleavage; by NIa-proBy similarity

Keywords - PTMi

Covalent protein-RNA linkage, Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliA0AUJ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 27795Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST
Domaini948 – 1070123Peptidase C6PROSITE-ProRule annotationAdd
BLAST
Domaini1540 – 1692153Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1696 – 1869174Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2354 – 2570217Peptidase C4PROSITE-ProRule annotationAdd
BLAST
Domaini2850 – 2974125RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1642 – 16454DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2594 – 25974Poly-Thr
Compositional biasi3166 – 31705Poly-Gln

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 (By similarity).By similarity

Sequence similaritiesi

Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation
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 RdRp catalytic domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR027450. AlkB-like.
IPR001456. HC-pro.
IPR031159. HC_PRO_CPD_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
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]
PfamiPF13532. 2OG-FeII_Oxy_2. 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. 1 hit.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
PS51744. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A0AUJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTRYRGADR YGNLGYDKVL QSKADAAKRR GLLFDHGSET YECPRCGEIW
60 70 80 90 100
RNLDDYMAEG GKMHPKKCLP EECDSDEEQI SSCNAALIHE KWGDLDSDTS
110 120 130 140 150
SKLSEFYKEP SILTYTTRTH CVVEKMRSMT APQCIEDIVG VRLHGRTAWF
160 170 180 190 200
FSKDPTLQYG HHPIYYDTHP WNDELDKYLG GAKYNTALVQ VYDGTRDLPY
210 220 230 240 250
HKDDEPCYDI TNNPIRTVNV TGTGDLCISK DKRRLYETIP MTSGTVITFP
260 270 280 290 300
ATMQENFYHA VRNPSAGRIS ITFRNQIRTV ERQVAHSANK RWVPIVEARV
310 320 330 340 350
TTNESRRGDN KQFQEAQSKL QTKTTINFGE FAAEVDGYYP TLSQDHKPAL
360 370 380 390 400
PKIIPELGLP TVDFIYVGNM RVPIDFKKNN VPAIVDTARH VAKIIDSQAL
410 420 430 440 450
TSEPIKVFTE QREVVGNVVT CTGTGFSVAD AKEAKALLNG LMYNRASNLF
460 470 480 490 500
ICPSCSDAAV LPEALLTLEH KRSCELASMK KISLARNMQV HVKQEAVARL
510 520 530 540 550
ISQQNSISVP IATLSSCVRG SADTTQVSLH IDEEDSIVDA IHLPNDFITC
560 570 580 590 600
DHEHAFETDS ASDNDVETMK KSEKRRKRRK RNPPPVRQVI TRAPVSNIIC
610 620 630 640 650
DVILTCLETQ IPVEFIGKSC ITFKPVRVGP VHTVGIQLKH QLHKTGFEVD
660 670 680 690 700
DLPDRETTSD IILAATRALR RLRHAHSNAQ QVHNSDITFG TSGAILPWSW
710 720 730 740 750
LAHDVIVEGP VQDSLVVRGR NVVSGHVTNA LNLQQDCLAD DYLQYSEELQ
760 770 780 790 800
PLHDDLSELK PLNVINNELI RQNMHITTLY SNMSKLQNDA LATKAEMKLP
810 820 830 840 850
LFGVAQLVVN QLKYNTTTHE WGERGDYVRK FVGKFFADFP TTQVPKQYMT
860 870 880 890 900
RTTNGHIRIT AYKALSLTSD PEIMMSRRMT QPMLTTAKQA DCVFQSTTGA
910 920 930 940 950
TCTSASCTTN SSGVVLSNKC ADPAPNTLRV RTMWDDIIIE LPLQGGRVHV
960 970 980 990 1000
PLEGLCFSTI FLHMYLLVPD ESVKLFHRTV TERAMPSLGQ WPTLRHLATW
1010 1020 1030 1040 1050
VLNLVAMFPV LSTTPMPEIL VHHESQSVHI PDCLGTATSG YHRLNIVTPY
1060 1070 1080 1090 1100
DFIIFATEIG RNGCQEYRVG GFAHDIKYTV SLMQDKRKLL HELMLTPTWA
1110 1120 1130 1140 1150
FYALSSPTLL KILYRSGALK RTYEHAVMAN HNAVDLVHEL NFLPERVSRA
1160 1170 1180 1190 1200
QTLQDEITAW EANVGRVLQQ VDGYLTRNHD PPLQRWYADA SARLQHLKID
1210 1220 1230 1240 1250
VDLLKNGFRS SQREHVEKKE QLLCDSFERL YNEQNSSLES LKTRCGMGSA
1260 1270 1280 1290 1300
RALIKPSGKC ESPEPAKQLS CKDLICSTKD KYALMLYTQA DALKRKIVAG
1310 1320 1330 1340 1350
SQSAFTTVCA GVAYRATKVM LRTPFNLLNA LNTYSLLIAA VNVMVLVQNY
1360 1370 1380 1390 1400
RRDQRKRAQY VNNLETQSMI RHYFAHLEQY IVNYVPRDEQ FEVIKAKFDE
1410 1420 1430 1440 1450
EFPEYNVMFK EVYKERIQFQ SADEGKNMCK IFASAILVMM VFDAHRADLM
1460 1470 1480 1490 1500
YKSFSQVRAL FNTLYDSGNP FNIIFQAERT IAPTMDVIIQ EPKPAIPSTS
1510 1520 1530 1540 1550
SCTFETWFRN CVNANNVIPV IPECDLLDFT RDTASSVVAT LTSSVKREFV
1560 1570 1580 1590 1600
IRGFVGSGKS TYLPHLLTKH GKVLLCEPVR VLASNVFEAL SGSPFYQSPT
1610 1620 1630 1640 1650
LLMRGTTKFG SGKITVATSG YAANYYNANR HRLNEFAYII FDESHQHTAH
1660 1670 1680 1690 1700
NFLLRSILDV IGYEGTVLHV SATPIGKEIP FRTMHPVEVV NMSTLSFEDF
1710 1720 1730 1740 1750
AIGQRKQVRC DVFNKGANIL VYVASYNDVD RMSTLLLERG LRVKKIDART
1760 1770 1780 1790 1800
VANVNNITCD GSDGEPLYLV ATNIVENGVT LNVDVVVDFG LCVKPVINAL
1810 1820 1830 1840 1850
QRRVDYVKTP ITWGQRIQRN GRVGRYKNGF CLNVGDVYKT PPIISEDVAL
1860 1870 1880 1890 1900
ESALMCFAAN VPPIFDNVDP ALFGQVTRPQ VQTAQMFELP IYITTPMISD
1910 1920 1930 1940 1950
AGALQSDIYQ VIKKFVLREG SIQLTQDATY LSNMSNWKTI ADYFPDISDT
1960 1970 1980 1990 2000
HAMRHEKVPF FVKDFGENSY IALAEAIRKA RNKSLGARGK LYGDVDATAL
2010 2020 2030 2040 2050
LLQTDPGSLD RSIMIVETEL VAQRSKLEDL NHHVHESTGM FQRYVSHLNH
2060 2070 2080 2090 2100
CLRGRYQTDQ IQKNIEVLSN MRSTLVGYRQ VVDKVEPEEI PHFVQQNPNI
2110 2120 2130 2140 2150
TMIIDFQSDR TKADGFVKHG INGIYNYTKI ASDTFSLLLI ACVVIYYVVQ
2160 2170 2180 2190 2200
YFFREMKSHI TFEASGSRRN RLHLRDNKLI KGGYTWAGPS DDMEREFGPE
2210 2220 2230 2240 2250
YALKRDKFSE KKARKHMRER IQPRTNMGVK LAPFQVFYGF DVADYDVLQL
2260 2270 2280 2290 2300
FDPITGVKID MDPRATAKEI TEEVEDTPFN KEVWSDTHMP EKIQATFVKK
2310 2320 2330 2340 2350
GGVNREDVLK QVRVDMTTHN PTMVTGSGGI MGYPEHKGDF RQTGPPKFSI
2360 2370 2380 2390 2400
VPEGRSTIKS GNNIAPFISA MGTIKNVYMN GDFDTLACTQ IGNKLVVNAH
2410 2420 2430 2440 2450
IFMEPVKKQE LILQHGVYEL PNNGTINIKH VPGIDMVIQT LPMDVPLARQ
2460 2470 2480 2490 2500
IKAYRGPIPG ELIRLLKIER NTKTNSTSLS DPGTARVGPG TIWYHNITTK
2510 2520 2530 2540 2550
HGDCGSLVLS EKDNKIVGIH TGQQDGTNLN LFAPITKDAI VAIETVLPGE
2560 2570 2580 2590 2600
LNDWVFTPDM LDVGSNNAIR KQASDPFPVV KKLLEGITFQ NNRTTTTDSV
2610 2620 2630 2640 2650
SNTAILPARK YWVASDLPVN IKYQCDMPTF FNTRHTYEGE SQPFMAYLRE
2660 2670 2680 2690 2700
CGDAETFFRP LLSHYIPSNL NGDAFKKDFF KYGKPVPVGL VHGPSFKIAS
2710 2720 2730 2740 2750
DRVIKRFERV GYERHSIPFE FDAEAIRDDL NKHAAMGAQY VGKKEQHLDG
2760 2770 2780 2790 2800
ISEEQFCDEF VASCCRLANN CDGVWKGSLK AELRSKEKVQ ENKTRVFTSA
2810 2820 2830 2840 2850
PYDVLLGGKA CVMHFNKKFY ANNTKGPWTV GINKLGLGWH RLLKSLPEGF
2860 2870 2880 2890 2900
VYGTGDGSQF DSSLTPLLIN EVCRIRMYFM QDDELGQAML RGLYRQIIWT
2910 2920 2930 2940 2950
LISMPDGSVV RKAKGNPSGQ PSTVDDNTIM VMLAVEYVFA YLGITQEEMD
2960 2970 2980 2990 3000
TIFKYYANGD DLIFAIHPDR ESILNEFTHL FAHLGLNYIF EDRTRNRAEL
3010 3020 3030 3040 3050
EYMSLTGIER EGFYIPKLSR ERISSIVQWR RKGDTRAMFD ALNAAILESW
3060 3070 3080 3090 3100
GYDDLTYWLR KYYEWLIINR YDIDLPEGEK LPYHTETAVE TLYTCDDNTT
3110 3120 3130 3140 3150
VYDGRYDFEV PTDASGGVFI IDFQSSSGTD TPPVIPPATS EPALQPVLTR
3160 3170 3180 3190 3200
QTSRPPTPPN TILTGQQQQQ LMPKSSQPYQ LEPLLAPTGV QQPTFGTFGM
3210 3220 3230 3240 3250
PQAQQTTTEP VVAAARVRGK QKEGDTSLSQ VRDHRRLSPE RIVRHDDDLA
3260 3270 3280 3290 3300
PPNESTSGES SHYDELTLPD VPRDKRKGLG ARLKGKPIIT QTQIYNYRPA
3310 3320 3330 3340 3350
FGSIHNNKAT DIELEAWKKQ IADYFQVDDV STLILGFMAY VIENGTSPEI
3360 3370 3380 3390 3400
FTNQKFVMAT SSGEQREYPL APFRSRSVEL RKIMRRFSEE AIDYIQIQRE
3410 3420 3430 3440 3450
HNPQYVPRQA VVRNVKRAIY FPYCFDFIDE TILTPDALEI VHQMKAAALE
3460 3470 3480 3490
SASSKVLGLD GGSARAIDTE RHTTEDATAR THNLRGAAMM A
Length:3,491
Mass (Da):393,838
Last modified:November 28, 2006 - v1
Checksum:iE548F95E522B9155
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY994084 Genomic RNA. Translation: AAX87001.1.
RefSeqiYP_851006.1. NC_008558.1.

Genome annotation databases

GeneIDi5076635.
KEGGivg:5076635.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY994084 Genomic RNA. Translation: AAX87001.1.
RefSeqiYP_851006.1. NC_008558.1.

3D structure databases

ProteinModelPortaliA0AUJ5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5076635.
KEGGivg:5076635.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR027450. AlkB-like.
IPR001456. HC-pro.
IPR031159. HC_PRO_CPD_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
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]
PfamiPF13532. 2OG-FeII_Oxy_2. 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. 1 hit.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
PS51744. 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. "A member of a new genus in the Potyviridae infects Rubus."
    Susaimuthu J., Tzanetakis I.E., Gergerich R.C., Martin R.R.
    Virus Res. 131:145-151(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiPOLG_BVY3
AccessioniPrimary (citable) accession number: A0AUJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: November 28, 2006
Last modified: December 9, 2015
This is version 74 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, Reference 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.