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Protein

Genome polyprotein

Gene
N/A
Organism
Pea seed-borne mosaic virus (strain DPD1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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 sitei307 – 3071For P1 proteinase activityBy similarity
Active sitei316 – 3161For P1 proteinase activitySequence analysis
Active sitei348 – 3481For P1 proteinase activityBy similarity
Active sitei742 – 7421For helper component proteinase activityPROSITE-ProRule annotation
Active sitei815 – 8151For helper component proteinase activityPROSITE-ProRule annotation
Active sitei2195 – 21951For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2230 – 22301For nuclear inclusion protein A activityPROSITE-ProRule annotation
Active sitei2300 – 23001For nuclear inclusion protein A activityPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1351 – 13588ATPPROSITE-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

MEROPSiC04.010.

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
OrganismiPea seed-borne mosaic virus (strain DPD1)
Taxonomic identifieri31736 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePotyviridaePotyvirus
Virus hostiPisum sativum (Garden pea) [TaxID: 3888]
Proteomesi
  • UP000006689 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 – 32063206Genome polyproteinPRO_0000420013Add
BLAST
Chaini1 – 397397P1 proteinaseSequence analysisPRO_0000040375Add
BLAST
Chaini398 – 856459Helper component proteinaseSequence analysisPRO_0000040376Add
BLAST
Chaini857 – 1214358Protein P3By similarityPRO_0000040377Add
BLAST
Chaini1215 – 1266526 kDa protein 1By similarityPRO_0000040378Add
BLAST
Chaini1267 – 1902636Cytoplasmic inclusion proteinBy similarityPRO_0000040379Add
BLAST
Chaini1903 – 1955536 kDa protein 2By similarityPRO_0000040380Add
BLAST
Chaini1956 – 2149194Viral genome-linked proteinBy similarityPRO_0000040381Add
BLAST
Chaini2150 – 2395246Nuclear inclusion protein ABy similarityPRO_0000040382Add
BLAST
Chaini2396 – 2915520Nuclear inclusion protein BBy similarityPRO_0000040383Add
BLAST
Chaini2916 – 3206291Capsid proteinBy similarityPRO_0000040384Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2016 – 20161O-(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
Sitei397 – 3982Cleavage; by P1 proteinaseSequence analysis
Sitei856 – 8572Cleavage; by autolysisPROSITE-ProRule annotation
Sitei1214 – 12152Cleavage; by NIa-proBy similarity
Sitei1266 – 12672Cleavage; by NIa-proBy similarity
Sitei1902 – 19032Cleavage; by NIa-proBy similarity
Sitei1955 – 19562Cleavage; by NIa-proBy similarity
Sitei2149 – 21502Cleavage; by NIa-proBy similarity
Sitei2395 – 23962Cleavage; by NIa-proBy similarity
Sitei2915 – 29162Cleavage; by NIa-proBy similarity

Keywords - PTMi

Covalent protein-RNA linkage, Phosphoprotein

Proteomic databases

PRIDEiP29152.

Structurei

3D structure databases

ProteinModelPortaliP29152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini734 – 856123Peptidase C6PROSITE-ProRule annotationAdd
BLAST
Domaini1338 – 1490153Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1494 – 1668175Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini2150 – 2368219Peptidase C4PROSITE-ProRule annotationAdd
BLAST
Domaini2637 – 2761125RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi450 – 4534Involved in interaction with stylet and aphid transmissionBy similarity
Motifi708 – 7103Involved in virions binding and aphid transmissionBy similarity
Motifi1440 – 14434DECH box
Motifi1994 – 20018Nuclear 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: P29152-1) [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
MSTLVCQAVA APVWSNGART RRIRDADGEY RCTQCDMGFD SMTMARPVNH
60 70 80 90 100
CCDGIMIDEY NLYDDDPIMH LVDSKTPIKR GSQETEGDGM AAEAIKVTGA
110 120 130 140 150
EPVNCFMVGT IKCKINENSI VAKGVMAAIP RQLTQDEVFM RKARLQAAVA
160 170 180 190 200
KSTIEREEKE RQFAFSKLEE KLRARREKLK DGIVIKTRKG LEWREATPNQ
210 220 230 240 250
QRGKLQSTSF DASGGKTLTP HTIYCKTKSS KFSNGGVKCA TSKKMRTVRK
260 270 280 290 300
PQSLKMKTES IDVLIEQVMT IAGKHAKQVT LIDKQKTNRV WIRRVNGVRL
310 320 330 340 350
LQVETKHHKG IISQKDASLN NLTKRVARHF ARKTAYIHPS DSITHGHSGV
360 370 380 390 400
VFLRANISGS KSYSIDDLFV VRGKRNGKLM ESRNKVAWRK MFQIDHFSIV
410 420 430 440 450
GIKIWNAFDA EYVKLRDESV SDHDCVGGIT PEECGILAAQ ILRVFYPCWR
460 470 480 490 500
ITCTKCISNW LSKPTSEQIE HIYERGNLAI QDLNKRIPSA HHVTQMVELL
510 520 530 540 550
RQRIKNTTFD MGNNTKVHEL IGHRQDGVFR HLNRLNNSIL AANGSSTIEW
560 570 580 590 600
ESMNESLLEL ARWHNKRTES IASGGISSFR NKISAKAQIN FALMCDNQLD
610 620 630 640 650
TNGNFVWGER GYHAKRFFSE FFTKIDPKDG YSHHTVRATP TGVRHLAIGN
660 670 680 690 700
LIIPGDLQKL REKLEGVSIT AVGISEKCVS RRNGDFVYPC SCVTSENGKP
710 720 730 740 750
VLSDVILPTR NHLVIGNTGD PKLVDLPKTE TGRMWIAKEG YCYINIFFAM
760 770 780 790 800
LVNVSEKDAK DFTKFVRDEI MPQLGKWPTM MDVATACYKL AIIYPDVRDA
810 820 830 840 850
QLPRILVDHS EQIFHVIDSY GSMTTGYHIL KAGTVSQLIS FAHGALLGEM
860 870 880 890 900
KMYRVGGTQK MEINMCCCQR KNLLIKQLIR AIYRPKLLTE IIETEPFVLM
910 920 930 940 950
LAIVSPSILK AMFRSGTFNQ AIKFYMHRSK PTAQTLAFLE ALSERVSRSR
960 970 980 990 1000
VLSEQFNIID GALKELKSLA NMSMRTQHTY PIVQNQLDIM IERVSADAEL
1010 1020 1030 1040 1050
LRDGFVVSKG RVQALIEKNY QDDLRNSFTD LPYVQQLQQT MSFSRVKHGF
1060 1070 1080 1090 1100
GELCESKDLS FSKEAWMGHL SSFSAGGKQI IRLARTKSQQ MLASGGRRVT
1110 1120 1130 1140 1150
LAARNITMRM VTATFSEIMK FVNMLLVLSM IFKLWKQANT LLEEREKDKW
1160 1170 1180 1190 1200
EKFDRSQNEL RRQLRYTLWR FEAQEGRQVT REEFFDYLKY NEGIENRHEL
1210 1220 1230 1240 1250
INELIANQPL FSIQAKKHGE IRFEQTVALM ALLAMMFGSD RSDAVFSTLS
1260 1270 1280 1290 1300
KVRTIFTTMA QEVRCQSIDD IHDVFDEKKA TIDFELATDQ PAQVQMDKTF
1310 1320 1330 1340 1350
CEWWQNQMEQ NRTVPHYRTG GKFIEFTRSN AASVANEIAH TPDFSEYLIR
1360 1370 1380 1390 1400
GAVGSGKSTG LPCYLSAKGR VLLLEPTRPL TENVCAQLRG SPFHKSPSMS
1410 1420 1430 1440 1450
MRNGHTFGST PIHVMTTGYA LHFFCNNVER IREYDFVIFD ECHVIDSSAM
1460 1470 1480 1490 1500
SFYCALKEYS YQGKILKVSA TPPGREVEFK TQFPVTIATE DSLSFDQFVQ
1510 1520 1530 1540 1550
AQGSGANCDI LKKGHNILVY VSSYNEVDRL SKLLVDRGFK VTKVDGRTMK
1560 1570 1580 1590 1600
LGGVEINTSG TAEKPHFIVA TNIIENGVTL DIDVVVDFGV KVVAELDADA
1610 1620 1630 1640 1650
RTMRYNKQAI SYGERIQRLG RVGRLKDGHA LRIGHTEKGI TEIPVAIAVE
1660 1670 1680 1690 1700
SAFQCFAYGL PVMTSNVSTS IIGNCTVKQA RTMMNFELSP FFTVELVKYN
1710 1720 1730 1740 1750
GTMHPEIHKI LVPYKLRDSS MQLCKEAIPN SGVSRWHTAH EYISHGIVLE
1760 1770 1780 1790 1800
TLKSDVRIPF YLKGVPEKVY EKIWNAVCVF KSDSGFGRMS TASACNVAYT
1810 1820 1830 1840 1850
LKTDPLSITR TIAHIDALLI EEQEKKSQFD LMSSHVTNSS SISLAGLVNR
1860 1870 1880 1890 1900
LRSKWMVDHS GENIVKLQNA RSQLLEFRGM DINLDDVESF RKFGCAETVR
1910 1920 1930 1940 1950
CQSKSEVSKT LQLKGKWNKP LITSDFFVVC MVSIGCVVLM YQIFMAKWNE
1960 1970 1980 1990 2000
PVKLEGKSKA KTLRFRQARD NNAKYEVFAD EDTKRHYFGE AYTKKGKKSG
2010 2020 2030 2040 2050
KARGMGVKTK KFVNVYGFDP CEYSLVRFVD PLTGLTYDRH PMEHMMDVQE
2060 2070 2080 2090 2100
TIGDDRREAM WNDELDKQLF VTRPTIEAYY IKDKTTPALK IDLNPHNPMR
2110 2120 2130 2140 2150
VCDKAETIAG FPEREFELRQ SGSATLVPYS EVPVQNEKQE FDEEHVRTEA
2160 2170 2180 2190 2200
ASLHFGLRDY NPIAQAVCRI TNTGVDYDRS IFGIGFGQFL ITNAHCFKLN
2210 2220 2230 2240 2250
EGETRIVSRH GQFTIEKTHS LPIHQVKDKD MVIVRLPKDF PPFPQRLQFR
2260 2270 2280 2290 2300
APQEREKICL VGSNFQEKSI QSVITESCMT FKHNGGKYWK HWITTKEGHC
2310 2320 2330 2340 2350
GLPAVALKDG HIVGIHNLGG ENTNINYFTP FDADILDKYL LNAEALQWTK
2360 2370 2380 2390 2400
GWKYNKNKVC WGGLELLDDN EPEESGLFRM VKLLKSLEED GVRTQSRDDA
2410 2420 2430 2440 2450
WLEKEIKGSL KVVARCPGQL VTKHVVKGPC AMFQLYLELH EDAKSFFTPR
2460 2470 2480 2490 2500
MGSYGKSRLS KGAFIKDIMK YSSNTVVGNV DCDVFENAID NVEKILWKAG
2510 2520 2530 2540 2550
MMQCEYVTDA EAIFQSLNMN AAVGAMYQGK KKDYFEDFTA ADRELIVKQS
2560 2570 2580 2590 2600
CERLFLGKKG VWNGSLKAEL RPIEKVHENK TRTFTAAPLD TLLGGKVCVD
2610 2620 2630 2640 2650
DFNNFFYSCH LRGPWTVGIT KFYAGWNEFL SKLPDGWLYC DADGSRFDSS
2660 2670 2680 2690 2700
LTPYLINAVL ELRLRFMEEW DAGEQMLKNL YTEIIYTPIA TPDGSVIKKT
2710 2720 2730 2740 2750
KGNNSGQPST VVDNTLMVIL AMQYSLQLLG VDFETQDEVV RYFANGDDLL
2760 2770 2780 2790 2800
IAVRPDCEFV LKGLEIHFSN LGLNYNFSAR HHDKKDVWFM STRGILRDGI
2810 2820 2830 2840 2850
LIPKLEEERI VAILEWDRSR EFSHRLDAIC AAMIEAWGYD ELLQHIRKFY
2860 2870 2880 2890 2900
YWLLEQEPYR SIAQEGKAPY IAETALRHLY TNAMATQSEL EKYTEAINQH
2910 2920 2930 2940 2950
YNDEGGDGSI KVRLQAGDET KDDERRRKEE EDRKKREESI DASQFGSNRD
2960 2970 2980 2990 3000
NKKNKNKESD TPNKLIVKSD RDVDAGSSGT ITVPRLEKIS AKIRMPKHKG
3010 3020 3030 3040 3050
GVAISLQHLV DYNPAQVDIS NTRATQSQFD NWWRAVSQEY GVGDNEMQVL
3060 3070 3080 3090 3100
ASGLMVWCIE NGTSPNINGM WTMMDGEEQV EYPLKPVMDN ARPTFRQIMA
3110 3120 3130 3140 3150
HFSDVAEAYI EKRNSTEVYI PRYALQRNLR DPSLARYGFD FYEITAKTPV
3160 3170 3180 3190 3200
RAREAHFQMK AAAIRGKSNS LFGLDGNVGT QEENTERHTA EDVNQNMHNL

LGMRAM
Note: Produced by conventional translation.
Length:3,206
Mass (Da):364,276
Last modified:December 1, 1992 - v1
Checksum:i42A3D921BE9A0CBF
GO
Isoform P3N-PIPO polyprotein (identifier: P0CJ99-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P0CJ99.
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:1,096
Mass (Da):124,210
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10930 mRNA. Translation: BAA01726.1.
PIRiJQ1331. GNVSPV.
RefSeqiNP_056765.1. NC_001671.1.

Genome annotation databases

GeneIDi1494045.
KEGGivg:1494045.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10930 mRNA. Translation: BAA01726.1.
PIRiJQ1331. GNVSPV.
RefSeqiNP_056765.1. NC_001671.1.

3D structure databases

ProteinModelPortaliP29152.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC04.010.

Proteomic databases

PRIDEiP29152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1494045.
KEGGivg:1494045.

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...

Entry informationi

Entry nameiPOLG_PSBMV
AccessioniPrimary (citable) accession number: P29152
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: September 7, 2016
This is version 133 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.