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Protein

Genome polyprotein

Gene
N/A
Organism
Papaya ringspot virus (strain P / mutant HA)
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.
Both 6K peptides are indispensable for virus replication.By similarity
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 sitei456 – 4561For P1 proteinase activityBy similarity
Active sitei465 – 4651For P1 proteinase activitySequence analysis
Active sitei499 – 4991For P1 proteinase activityBy similarity
Active sitei890 – 8901For helper component proteinase activityPROSITE-ProRule annotation
Active sitei963 – 9631For helper component proteinase activityPROSITE-ProRule annotation
Active sitei2327 – 23271For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2362 – 23621For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2431 – 24311For nuclear inclusion protein A activityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1486 – 14938ATPPROSITE-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

Protein family/group databases

MEROPSiC04.009.

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
OrganismiPapaya ringspot virus (strain P / mutant HA)
Taxonomic identifieri31731 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePotyviridaePotyvirus
Virus hostiCarica papaya (Papaya) [TaxID: 3649]
Proteomesi
  • UP000006688 Componenti: Chromosome
  • UP000007380 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 – 33443344Genome polyproteinPRO_0000420010Add
BLAST
Chaini1 – 547547P1 proteinaseBy similarityPRO_0000040361Add
BLAST
Chaini548 – 1004457Helper component proteinaseBy similarityPRO_0000040362Add
BLAST
Chaini1005 – 1349345Protein P3By similarityPRO_0000040363Add
BLAST
Chaini1350 – 1401526 kDa protein 1By similarityPRO_0000040364Add
BLAST
Chaini1402 – 2036635Cytoplasmic inclusion proteinBy similarityPRO_0000040365Add
BLAST
Chaini2037 – 2093576 kDa protein 2By similarityPRO_0000040366Add
BLAST
Chaini2094 – 2282189Viral genome-linked proteinBy similarityPRO_0000040367Add
BLAST
Chaini2283 – 2520238Nuclear inclusion protein ABy similarityPRO_0000040368Add
BLAST
Chaini2521 – 3057537Nuclear inclusion protein BBy similarityPRO_0000040369Add
BLAST
Chaini3058 – 3344287Capsid proteinBy similarityPRO_0000040370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2156 – 21561O-(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
Sitei547 – 5482Cleavage; by P1 proteinaseSequence analysis
Sitei1004 – 10052Cleavage; by autolysisPROSITE-ProRule annotation
Sitei1349 – 13502Cleavage; by NIa-proBy similarity
Sitei1401 – 14022Cleavage; by NIa-proBy similarity
Sitei2036 – 20372Cleavage; by NIa-proBy similarity
Sitei2093 – 20942Cleavage; by NIa-proBy similarity
Sitei2282 – 22832Cleavage; by NIa-proBy similarity
Sitei2520 – 25212Cleavage; by NIa-proBy similarity
Sitei3057 – 30582Cleavage; by NIa-proBy similarity

Keywords - PTMi

Covalent protein-RNA linkage, Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ01901.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini882 – 1004123Peptidase C6PROSITE-ProRule annotationAdd
BLAST
Domaini1473 – 1625153Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1644 – 1803160Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2283 – 2499217Peptidase C4PROSITE-ProRule annotationAdd
BLAST
Domaini2761 – 2885125RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi598 – 6014Involved in interaction with stylet and aphid transmissionBy similarity
Motifi856 – 8583Involved in virions binding and aphid transmissionBy similarity
Motifi1575 – 15784DECH box
Motifi2134 – 21418Nuclear 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.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR022199. DUF3725.
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]
PfamiPF00270. DEAD. 1 hit.
PF12523. DUF3725. 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: Q01901-1) [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
MSSLYTLRAA AQYDRRLESK KGSGWVEHKL ERKGERGNTH YCSEFDISKG
60 70 80 90 100
AKILQLVQIG NTEVGRTFLE GNRFVRANIF EIIRKTMVGR LGYDFESELW
110 120 130 140 150
VCRNCDKTSE KYFKKCDCGE TYYYSERNLM RTMNDLMYQF DMTPSEINSV
160 170 180 190 200
DLEYLANAVD YAEQLVKRSQ VPEPVELAMM EPIVASGEGI LMVSEPEVMP
210 220 230 240 250
VTTKVEEAWT IQIGEIPVPL VVIKETPVIS GVEGTLNSTG FSLEADITKL
260 270 280 290 300
VEKEILQEEV KEAVHLALEV GNEIAEKKPE LKLIPYWSAS LELHKRIRKH
310 320 330 340 350
KEHAKIAAIQ VQKEREKDQK VFSALELRLN LKSRRRNQAV VCDKRGTLKW
360 370 380 390 400
ETQRGHKKSK LMQQASDFVV TQIHCDFGCK TQYSEPHIPG IKQSTSKKIC
410 420 430 440 450
KPRKHSRIVG NSKINYIMKN LCDTIIERGI PVELVTKRCK RRILQKEGRS
460 470 480 490 500
YVQLRHMNGI RARQDVSSSP DMELLFTQFC KFLVGHKPLK SKNLTFGSSG
510 520 530 540 550
LIFKPKFADN VGRYFGDYFV VRGRLGGKLF DGRSKLARSV YAKMDQYNDV
560 570 580 590 600
AEKFWLGFNR AFLRHRKPTD HTCTSDMDVT MCGEVAALAT IILFPCHKIT
610 620 630 640 650
CNTCMSKVKG RVIDEVGEDL NCELERLRET LSAYGGSFGH VSTLLDQLNR
660 670 680 690 700
VLNARNMNDG AFKEIAKKID EKKESPWTHM TTINNTLYKG SLATGYEFER
710 720 730 740 750
ASNSLREIVR WHLKRTESIK AGSVESFRNK RSGKAHFNPA LTCDNQLDKN
760 770 780 790 800
GNFLWGERQY HAKRFFANYF EKIDHSKGYE YYSQRQNPNG IRKIAIGNLV
810 820 830 840 850
FSTNLERFRQ QMVEHHIDQG PITRECIALR NNNYVHVCSC VTLDDGTPAT
860 870 880 890 900
SELKTPTKNH IVLGNSGDPK YVDLPTLESD SMYIAKKGYC YMNIFLAMLI
910 920 930 940 950
NIPENEAKDF TKRVRDLVGS KLGEWPTMLD VATCANQLVV FHPDAANAEL
960 970 980 990 1000
PQILVDHRQK TMHVIDSFGS VDSGYHILKA NTVNQLIQFA RDPLDSEMKH
1010 1020 1030 1040 1050
YIVGGEFDPT TNCLHQLIRV IYKPHELRSL LRNEPYLIVI ALMSPSVLLT
1060 1070 1080 1090 1100
LFNSGAVEHA LNYWIKRDQD VVEVIVLVEQ LCRKVTLART ILEQFNEIRQ
1110 1120 1130 1140 1150
NARDLHELMD RNNKPWISYD RSLELLSVYA NSQLTDEGLL KQGFSTLDPR
1160 1170 1180 1190 1200
LREAVEKTYA TLLQEEWRAL SLFQKLHLRY FAFKSQPSFS EYLKPKGRAD
1210 1220 1230 1240 1250
LKIVYDFSPK YCVHEVGKAF LLPVKAGAKI ASRIINGCGA FIRKSAAKGC
1260 1270 1280 1290 1300
AYIFKDLFQF VHVVLVLSIL LQIFRSAQGI ATEHLQLKQA KAEVERQKDF
1310 1320 1330 1340 1350
DRLEALYAEL CVKSGEQPTT EEFLDFVMER EPRLKDQAYN LIYIPVIHQA
1360 1370 1380 1390 1400
KSDNEKKLEQ VIAFITLILM MIDVDKSDCV YRILNKFKGV INSSNTNVYH
1410 1420 1430 1440 1450
QSLDDIRDFY EDKQLTIDFD ITGENQINRG PIDVTFEKWW DNQLSNNNTI
1460 1470 1480 1490 1500
GHYRIGGTFV EFSRVNAATV ASEIAHSPER EFLVRGAVGS GKSTNLPFLL
1510 1520 1530 1540 1550
SKHGSVLLIE PTRPLCENVC KQLRGEPFHC NPTIRMRGLT AFGSTNITIM
1560 1570 1580 1590 1600
TSGFALHYYA HNIQQLRLFD FIIFDECHVI DSQAMAFYCL MEGNAIEKKI
1610 1620 1630 1640 1650
LKVSATPPGR EVEFSTQFPT KIVTEQSISF KQLVDNFGTG ANSDVTAFAD
1660 1670 1680 1690 1700
NILVYVASYN EVDQLSKLLS DKGYLVTKID GRTMKVGKTE ISTSGTKFKK
1710 1720 1730 1740 1750
HFIVATNIIE NGVTLDIEAV IDFGMKVVPE MDSDNRMIRY SKQAISFGER
1760 1770 1780 1790 1800
IQRLGRVGRH KEGIALRIGH TEKGIQEIPE MAATEAAFLS FTYGLPVMTH
1810 1820 1830 1840 1850
NVGLSLLKNC TVRQARTMQQ YELSPFFTQN LVNFDGTVHP KIDVLLRPYK
1860 1870 1880 1890 1900
LRDCEVRLSE AAIPHGVQSI WLSARDYEAV GGRLCLEGDV RIPFLIKDVP
1910 1920 1930 1940 1950
ERLYKELWDI VQTYKRDFTF GRINSVSAGK IAYTLRTDVY SIPRTLITID
1960 1970 1980 1990 2000
KLIESENMKH AHFKAMTSCT GLNSSFSLLG VINTIQSRYL VDHSVENIRK
2010 2020 2030 2040 2050
LQLAKAQIQQ LEAHMQENNV ENLIQSLGAV RAVYHQSVDG FKHIKRELGL
2060 2070 2080 2090 2100
KGVWDGSLMI KDAIVCGFTM AGGAMLLYQH FRDKFTNVHV FHQGFSARQR
2110 2120 2130 2140 2150
QKLRFKSAAN AKLGREVYGD DGTIEHYFGE AYTKKGNKKG KMHGMGVKTR
2160 2170 2180 2190 2200
KFVATYGFKP EDYSYVRYLD PLTGETLDES PQTDISMVQD HFSDIRRKYM
2210 2220 2230 2240 2250
DSDSFDRQAL IANNTIKAYY VRNSAKAALE VDLTPHNPLK VCDNKLTIAG
2260 2270 2280 2290 2300
FPDREAELRQ TGPPRTIQVD QVPPPSKSVH HEGKSLCQGM RNYNGIASVV
2310 2320 2330 2340 2350
CHLKNTSGKG KSLFGIGYNS FIITNRHLFK ENNGELIVKS QHGKFIVKNT
2360 2370 2380 2390 2400
TTLQIAPVGK TDLLIIRMPK DFPPFHSRAR FRAMKAGDKV CMIGVDYQEN
2410 2420 2430 2440 2450
HIASKVSETS IISEGTGDFG CHWISTNDGD CGNPLVSVSD GFIVGLHSLS
2460 2470 2480 2490 2500
TSTGDQNFFA KIPAQFEEKV LRKIDDLTWS KHWSYNINEL SWGALKVWES
2510 2520 2530 2540 2550
RPEAIFNAQK EVNQLNVFEQ SGGRWLFDKL HGNLKGVSSA PSNLVTKHVV
2560 2570 2580 2590 2600
KGICPLFRNY LECDEEAKAF FSPLMGHYMK SVLSKEAYIK DLLKYSSDIV
2610 2620 2630 2640 2650
VGEVNHDVFE DSVAQVIELL NDHECPELEY ITDSEVIIQA LNMDAAVGAL
2660 2670 2680 2690 2700
YTGKKRKYFE GSTVEHRQAL VRKSCERLYE GRMGVWNGSL KAELRPAEKV
2710 2720 2730 2740 2750
LAKKTRSFTA APLDTLLGAK VCVDDFNNWF YSKNMECPWT VGMTKFYKGW
2760 2770 2780 2790 2800
DEFLKKFPDG WVYCDADGSQ FDSSLTPYLL NAVLSIRLWA MEDWDIGEQM
2810 2820 2830 2840 2850
LKNLYGEITY TPILTPDGTI VKKFKGNNSG QPSTVVDNTL MVLITMYYAL
2860 2870 2880 2890 2900
RKAGYDTKTQ EDMCVFYING DDLCIAIHPD HEHVLDSFSS SFAELGLKYD
2910 2920 2930 2940 2950
FAQRHRNKQN LWFMSHRGIL IDDIYIPKLE PERIVAILEW DKSKLPEHRL
2960 2970 2980 2990 3000
EAITAAMIES WGYGDLTHQI RRFYQWVLEQ APFNELAKQG RAPYVSEVGL
3010 3020 3030 3040 3050
RRLYTSERGS MDELEAYIDK YFERERGDSP ELLVYHESRG TDDYQLVCSN
3060 3070 3080 3090 3100
NTHVFHQSKN EAVDAGLNEK LKEKEKQKEK EKEKQKEKEK DGASDGNDVS
3110 3120 3130 3140 3150
TSTKTGERDR DVNVGTSGTF TVPRIKSFTD KMVLPRIKGK TVLNLNHLLQ
3160 3170 3180 3190 3200
YNPQQIDISN TRATHSQFEK WYEGVRNDYG LNDNEMQVML NGLMVWCIEN
3210 3220 3230 3240 3250
GTSPDISGVW VMMDGETQVD YPIKPLIEHA TPSFRQIMAH FSNAAEAYIA
3260 3270 3280 3290 3300
KRNATERYMP RYGIKRNLTD ISLARYAFDF YEVNSKTPDR AREAHMQMKA
3310 3320 3330 3340
AALRNTSRRM FGMDGSVSNK EENTERHTVE DVNRDMHSLL GMRN
Note: Produced by conventional translation.
Length:3,344
Mass (Da):381,046
Last modified:October 1, 1996 - v2
Checksum:iE90CD7523AC5243D
GO
Isoform P3N-PIPO polyprotein (identifier: P0CJ98-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0CJ98.
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:1,228
Mass (Da):140,607
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67673 Genomic RNA. Translation: CAA47905.1.
S46722 Genomic RNA. Translation: AAB23789.1.
X67672 Genomic RNA. Translation: CAA47904.1.
PIRiJQ1899.
RefSeqiNP_056758.1. NC_001785.1.

Genome annotation databases

GeneIDi1494043.
KEGGivg:1494043.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67673 Genomic RNA. Translation: CAA47905.1.
S46722 Genomic RNA. Translation: AAB23789.1.
X67672 Genomic RNA. Translation: CAA47904.1.
PIRiJQ1899.
RefSeqiNP_056758.1. NC_001785.1.

3D structure databases

ProteinModelPortaliQ01901.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC04.009.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1494043.
KEGGivg:1494043.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR022199. DUF3725.
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]
PfamiPF00270. DEAD. 1 hit.
PF12523. DUF3725. 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...

Entry informationi

Entry nameiPOLG_PRSVH
AccessioniPrimary (citable) accession number: Q01901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: September 7, 2016
This is version 131 of the entry and version 2 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.