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Protein

Genome polyprotein

Gene
N/A
Organism
Pepper mottle virus (isolate California) (PeMV) (PepMoV C)
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 sitei195 – 1951For P1 proteinase activityBy similarity
Active sitei204 – 2041For P1 proteinase activitySequence analysis
Active sitei238 – 2381For P1 proteinase activityBy similarity
Active sitei629 – 6291For helper component proteinase activityPROSITE-ProRule annotation
Active sitei702 – 7021For helper component proteinase activityPROSITE-ProRule annotation
Active sitei2076 – 20761For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2111 – 21111For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2181 – 21811For nuclear inclusion protein A activityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1241 – 12488ATPPROSITE-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

MEROPSiC04.002.

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
OrganismiPepper mottle virus (isolate California) (PeMV) (PepMoV C)
Taxonomic identifieri31737 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePotyviridaePotyvirus
Virus hostiCapsicum annuum (Bell pepper) [TaxID: 4072]
Datura inoxia (Downy thornapple) (Datura meteloides) [TaxID: 4075]
Solanum [TaxID: 4107]
Proteomesi
  • UP000008157 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 – 30683068Genome polyproteinPRO_0000420003Add
BLAST
Chaini1 – 287287P1 proteinaseSequence analysisPRO_0000040295Add
BLAST
Chaini288 – 743456Helper component proteinaseSequence analysisPRO_0000040296Add
BLAST
Chaini744 – 1104361Protein P3By similarityPRO_0000040297Add
BLAST
Chaini1105 – 1156526 kDa protein 1By similarityPRO_0000040298Add
BLAST
Chaini1157 – 1790634Cytoplasmic inclusion proteinBy similarityPRO_0000040299Add
BLAST
Chaini1791 – 1842526 kDa protein 2By similarityPRO_0000040300Add
BLAST
Chaini1843 – 2030188Viral genome-linked proteinBy similarityPRO_0000040301Add
BLAST
Chaini2031 – 2276246Nuclear inclusion protein ABy similarityPRO_0000040302Add
BLAST
Chaini2277 – 2795519Nuclear inclusion protein BBy similarityPRO_0000040303Add
BLAST
Chaini2796 – 3068273Capsid proteinBy similarityPRO_0000040304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1906 – 19061O-(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
Sitei287 – 2882Cleavage; by P1 proteinaseSequence analysis
Sitei743 – 7442Cleavage; by autolysisPROSITE-ProRule annotation
Sitei1104 – 11052Cleavage; by NIa-proBy similarity
Sitei1156 – 11572Cleavage; by NIa-proBy similarity
Sitei1790 – 17912Cleavage; by NIa-proBy similarity
Sitei1842 – 18432Cleavage; by NIa-proBy similarity
Sitei2030 – 20312Cleavage; by NIa-proBy similarity
Sitei2276 – 22772Cleavage; by NIa-proBy similarity
Sitei2795 – 27962Cleavage; by NIa-proBy similarity

Keywords - PTMi

Covalent protein-RNA linkage, Phosphoprotein

Proteomic databases

PRIDEiQ01500.

Structurei

3D structure databases

ProteinModelPortaliQ01500.
SMRiQ01500. Positions 2039-2252.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini621 – 743123Peptidase C6PROSITE-ProRule annotationAdd
BLAST
Domaini1228 – 1380153Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1399 – 1558160Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2031 – 2249219Peptidase C4PROSITE-ProRule annotationAdd
BLAST
Domaini2518 – 2642125RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi337 – 3404Involved in interaction with stylet and aphid transmissionBy similarity
Motifi595 – 5973Involved in virions binding and aphid transmissionBy similarity
Motifi1330 – 13334DECH box
Motifi1884 – 18918Nuclear 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.
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.
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: Q01500-1) [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
MATSVIQFGS FVCNLPKSQP LCTTVHCPKQ SMSTNIVRPS DPFAELEKHL
60 70 80 90 100
EPYLQKRMDA TIRQTKGGTL VYKHMSEAKR ARKLRKKQRE EEEVRLFMNA
110 120 130 140 150
APYIVSNITI GGGEVPSKME EVSIKRPLNK TPSRKIKKSL TPVTFRDGHM
160 170 180 190 200
NKFLRELRDC ATRNSMTVHL IGKRKTELAF KRRASLNAVY ATLHHMRGVD
210 220 230 240 250
RKRDIVLEEW MNDYVLNLSK VSTWGSLFHA ESLKRGDSGL ILNARALRGK
260 270 280 290 300
FGRCSRGFFI VRGKSDGVVL DARSKLSMAT VTHMEQYSTP EAFWSGLEKK
310 320 330 340 350
WSVVRKPTAH TCKPTYSVSN CGEVAAIIAQ ALFPCHKLTC GECSKEICDL
360 370 380 390 400
TSNECVQELY KNTSLALERM NNLHPEFQHI VKVLSVVRQL TEASNHGTET
410 420 430 440 450
FDEIFKMIGS KTQSPFTHLN KLNEFMLKGN ENTSGEWLTA RQHLRELVRF
460 470 480 490 500
QKNRTDNIKK GDLASFRNKL SARAQYNLYL SCDNQLDKNA SFLWGQREYH
510 520 530 540 550
ARRFFLNFFQ QIDPSKGYLA YEDRTIPNGS RKLAIGNLIV PLDLAEFRKR
560 570 580 590 600
MNGIDTQQPP IGKYCTSQLD GNFVYPCCCT TLDDGQPIRS AVYAPTKKHL
610 620 630 640 650
VVGNTGDTKY INLPKGDTEM LYIALDGYCY INIYLAMLVN ISEEEAKDFT
660 670 680 690 700
KKVRDIFMPK LGKWPTLMDL ATTCAQLRIF HPDVHDAELP RILVDHNTQT
710 720 730 740 750
CHVVDSYGSI STGYHILKAA TVSQLVLFAD DNLESEIKHY RVGGIVENHK
760 770 780 790 800
VQIDNQPSRC GVSEFHAIRM LIKGIYRPSV MYELLSEEPY LLVFSILSPS
810 820 830 840 850
ILIAMYNDRA FELAVQIWLE KEQSIPLIAT ILTNLAAKVS VATTLVQQLQ
860 870 880 890 900
LIELSADQLL NVTCDGFRVS FAYQSALTLL TRMRDQAKAN SELISGGFNE
910 920 930 940 950
YDQDLAWTLE KNYQGLLHDQ WKELSSLEKF RYYWSSRKRK TRLRSNIKSR
960 970 980 990 1000
SSPVASAISS LSLKPFMGKV FSHMKAGAVC TKQGTKNFID ARCLGISTYF
1010 1020 1030 1040 1050
VGSLMRKFPS AKVLLSSLFV LGALLNITHA ANRIIIDNRI SREHAAALEL
1060 1070 1080 1090 1100
YRKEDTCHEL YTALERKLGE KPTWDEYCSY VAKINPAMLE FIKDSYDEKQ
1110 1120 1130 1140 1150
VVHQRSTEDL KKVEHIIAFV TLAIMLFDSE RSDCVFKTLN KFKGVVCSLG
1160 1170 1180 1190 1200
SGVRHQSLDD FVSTMDEKNF VVDFELNDSV QRKNLTTEIT FESWWDEQVA
1210 1220 1230 1240 1250
RGFTIPHYRT EGRFMEFTRA TAAKVASDIS ISSERDFLIR GAVGSGKSTG
1260 1270 1280 1290 1300
LPHHLSTYGR VLLIEPTRPL AENVFKQLSG GPFFLKPTMR MRGNSVFGSS
1310 1320 1330 1340 1350
PISVMTSGFA LHFFANNITQ LQEIQFIIID ECHVMDASSM AFRSLIHTYH
1360 1370 1380 1390 1400
TNCKVLKVSA TPPGREVEFT TQFPVKLVVE DSLSFKTFVE SQGTGSNCDM
1410 1420 1430 1440 1450
IQYGNNLLVY VASYNEVDQL SKLLVAREFN VTKVDGRTMK HGELEIVTRG
1460 1470 1480 1490 1500
TKSKPHFVVA TNIIENGVTL DIDVVIDFGM KVSPFLDVDN RSVAYNKVSI
1510 1520 1530 1540 1550
SYGERIQRLG RVGRIQKGTA LRIGHTEKGL IEIPQMISTE AALYCFAYNL
1560 1570 1580 1590 1600
PVMSSGVSTS MIKNCTIPQV RTMHTFELSP FFMYNFVSHD GTMHPVVHET
1610 1620 1630 1640 1650
LKRYKLRDSV IPLSESSIPY RASSDWITAG DYRRIGVKLD IPDETRIAFH
1660 1670 1680 1690 1700
IKTFHRKFTN NLWESVLKYK ASAAFPTLRS SSITKIAYTL STDLYAIPRT
1710 1720 1730 1740 1750
LAVVESLLED ERTKQYQFKS LIDNGCSSMF SVVGISNALR AKYSKDHTVE
1760 1770 1780 1790 1800
NINKLETVKA QLKEFHNLNG SGDELNLIKR FESLQFVHHQ SKSSLAKALG
1810 1820 1830 1840 1850
LRGVWNKSLI VRDAIIAAGV ACGGAWLLYT WFTAKMSEVS HQGRSKTKRI
1860 1870 1880 1890 1900
QALKFRKARD KRAGFEIDNN EDTIEEYFGS AYTKKGKGKG TTVGMGRTNR
1910 1920 1930 1940 1950
RFINMYGFEP GQFSYIKFVD PLTGAQMEEN VYADIVDVQE KFGDIRRQMI
1960 1970 1980 1990 2000
LDDELDRRQT DVHNTIHAYL IKDWSNKALK VDLTPHNPLR VSDKASAIMK
2010 2020 2030 2040 2050
FPEREGELRQ TGQAVEVDVC DIPKEVVKHE AKTLMRGLRD YNPIAQTVCK
2060 2070 2080 2090 2100
LTVKSELGET STYGLGFGGL IIANHHLFKS FNGSLEVKSH HGVFRVPNLM
2110 2120 2130 2140 2150
AISVLPLKGR DMIIIKMPKD FPVFPQRLKF REPASTDRVC LIGSNFQERY
2160 2170 2180 2190 2200
ISTTVSEISA THPVPRSTFW KHWISTDDGH CGLPIVSTTD GFILGLHSLA
2210 2220 2230 2240 2250
NNRNSENYYT AFDSDFEMKI LRSGENTEWV KNWKYNPDTV LWGPLQLTKG
2260 2270 2280 2290 2300
TPSGMFKTTK MIEDLLAFKS ESVREQAHTS SWMLEVLKEN LKAIAYMKSQ
2310 2320 2330 2340 2350
LVTKHVVKGE CMMFKQYLQE NPRANEFFQP KMWAYGKSML NKEAYIKDIM
2360 2370 2380 2390 2400
KYSKVIDVGV VDCDRHLRKL SLELLYTQIH GFRKCSYITD EEEIFKALNI
2410 2420 2430 2440 2450
TTAVGAMYGG KKKEYFEKFT TEDKAEILRQ SCLRLYTGKL GVWEWALKAE
2460 2470 2480 2490 2500
LRSKEKIEAN KTRTFTAAPI DTLLGGKVCV DDLNNQFYSK NIECCWTVGM
2510 2520 2530 2540 2550
TKFYGGWDKL LTALPAGWIY CDADGSQFDS SLTPYLINAV LTIRYAFMED
2560 2570 2580 2590 2600
WDIGYKMLQN LYTEIIYTPI STPDGTIVKK FRGNNSGQPS TVVDNSLMVV
2610 2620 2630 2640 2650
LAMHYAFVRE GIAFEEIDSI CKFFVNGDDL LIAVNPERES LLDTLSNHFS
2660 2670 2680 2690 2700
DLGLNYDFSS RTRNKSELWF MSHCGISVEG TYIPKLEEER IVSILQWDRA
2710 2720 2730 2740 2750
ELPEYRLEAI CAAMIESWGY PQLTHEIRRF YSWLIEKNPY ADLASEGKAP
2760 2770 2780 2790 2800
YISELALKKL YLNQDVQMMS FRSYLKYFAD ADEEFECGTY EVRHQSSSRS
2810 2820 2830 2840 2850
DTLDAGEEKK KNKEVATVSD GMGKKEVEST RDSDVNAGTV GTFTIPRIKS
2860 2870 2880 2890 2900
ITEKMRMPKQ KRKGVLNLAH LLEYKPSQVD ISNTRSTQAQ FDNWYCEVMK
2910 2920 2930 2940 2950
AYDLQEEAMG TVMNGLMVWC IENGTSPNIS GTWTMMDGDE QVEFPLKPVI
2960 2970 2980 2990 3000
ENAKPTFRQI MAHFSDVAEA YIEMRNKQEP YMPRYGLVRN LRDMGLARYA
3010 3020 3030 3040 3050
FDFYEVTSRT STRAREAHIQ MKAAALKSAQ TRLFGLDGGI GTQGENTERH
3060
TTEDVSPDMH TLLGVREM
Note: Produced by conventional translation.
Length:3,068
Mass (Da):348,656
Last modified:October 1, 1993 - v1
Checksum:iFD3458B837FDA7C2
GO
Isoform P3N-PIPO polyprotein (identifier: P0CK01-1) [UniParc]FASTAAdd to basket

The sequence of this isoform can be found in the external entry P0CK01.
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:985
Mass (Da):112,002
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96425 Genomic RNA. Translation: AAA46903.1.
PIRiA44062.
RefSeqiNP_041276.1. NC_001517.1.

Genome annotation databases

GeneIDi1494047.
KEGGivg:1494047.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96425 Genomic RNA. Translation: AAA46903.1.
PIRiA44062.
RefSeqiNP_041276.1. NC_001517.1.

3D structure databases

ProteinModelPortaliQ01500.
SMRiQ01500. Positions 2039-2252.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC04.002.

Proteomic databases

PRIDEiQ01500.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1494047.
KEGGivg:1494047.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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.
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 pepper mottle virus genomic RNA: comparison of the encoded polyprotein with those of other sequenced potyviruses."
    Vance V.B., Moore D., Turpen T.H., Bracker A., Hollowell V.C.
    Virology 191:19-30(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Cited for: REVIEW.

Entry informationi

Entry nameiPOLG_PEMVC
AccessioniPrimary (citable) accession number: Q01500
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 14, 2015
This is version 131 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.