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Q6XW15

- POLG_BTMV

UniProt

Q6XW15 - POLG_BTMV

Protein

Genome polyprotein

Gene
N/A
Organism
Beet mosaic virus (BtMV)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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 By similarity.By similarity
    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
    Sitei313 – 3142Cleavage; by P1 proteinaseSequence Analysis
    Active sitei656 – 6561For helper component proteinase activityBy similarity
    Active sitei729 – 7291For helper component proteinase activityBy similarity
    Sitei770 – 7712Cleavage; by HC-proSequence Analysis
    Sitei1117 – 11182Cleavage; by NIa-proBy similarity
    Sitei1169 – 11702Cleavage; by NIa-proBy similarity
    Sitei1803 – 18042Cleavage; by NIa-proBy similarity
    Sitei1855 – 18562Cleavage; by NIa-proBy similarity
    Sitei2046 – 20472Cleavage; by NIa-proBy similarity
    Active sitei2092 – 20921For nuclear inclusion protein A activityPROSITE-ProRule annotation
    Active sitei2127 – 21271For nuclear inclusion protein A activityPROSITE-ProRule annotation
    Active sitei2198 – 21981For nuclear inclusion protein A activityPROSITE-ProRule annotation
    Sitei2293 – 22942Cleavage; by NIa-proBy similarity
    Sitei2809 – 28102Cleavage; by NIa-proBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1254 – 12618ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activity Source: InterPro
    3. helicase activity Source: UniProtKB-KW
    4. RNA binding Source: InterPro
    5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    6. structural molecule activity Source: InterPro

    GO - Biological processi

    1. RNA-protein covalent cross-linking Source: UniProtKB-KW
    2. transcription, DNA-templated Source: InterPro
    3. viral RNA genome replication Source: InterPro

    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

    MEROPSiS30.001.

    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
    OrganismiBeet mosaic virus (BtMV)
    Taxonomic identifieri114921 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePotyviridaePotyvirus
    Virus hostiAmaranthus retroflexus (Redroot amaranth) (Redroot pigweed) [TaxID: 124763]
    Beta vulgaris subsp. maritima (Sea beet) (Beta maritima) [TaxID: 350892]
    Beta vulgaris subsp. vulgaris (sugar beet) [TaxID: 3555]
    Chenopodium album (Lamb's-quarters) [TaxID: 3559]
    Melilotus indicus (Sourclover) (Yellow sweet clover) [TaxID: 200951]
    Sonchus arvensis (Perennial sowthistle) [TaxID: 50192]
    Spinacia oleracea (Spinach) [TaxID: 3562]
    Trifolium incarnatum (Crimson clover) [TaxID: 60916]
    ProteomesiUP000007617: Genome

    Subcellular locationi

    GO - Cellular componenti

    1. helical viral capsid Source: UniProtKB-KW

    Keywords - Cellular componenti

    Capsid protein, Helical capsid protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 30853085Genome polyproteinPRO_0000419994Add
    BLAST
    Chaini1 – 313313P1 proteinaseSequence AnalysisPRO_0000040246Add
    BLAST
    Chaini314 – 770457Helper component proteinaseSequence AnalysisPRO_0000040247Add
    BLAST
    Chaini771 – 1117347Protein P3Sequence AnalysisPRO_0000040248Add
    BLAST
    Chaini1118 – 1169526 kDa protein 1By similarityPRO_0000040249Add
    BLAST
    Chaini1170 – 1803634Cytoplasmic inclusion proteinBy similarityPRO_0000040250Add
    BLAST
    Chaini1804 – 1855526 kDa protein 2By similarityPRO_0000040251Add
    BLAST
    Chaini1856 – 2046191Viral genome-linked proteinBy similarityPRO_0000040252Add
    BLAST
    Chaini2047 – 2293247Nuclear inclusion protein ABy similarityPRO_0000040253Add
    BLAST
    Chaini2294 – 2809516Nuclear inclusion protein BBy similarityPRO_0000040254Add
    BLAST
    Chaini2810 – 3085276Capsid proteinPRO_0000040255Add
    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
    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

    Keywords - PTMi

    Covalent protein-RNA linkage, Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ6XW15.
    SMRiQ6XW15. Positions 2055-2269.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1241 – 1393153Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1412 – 1571160Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini2047 – 2266220Peptidase C4PROSITE-ProRule annotationAdd
    BLAST
    Domaini2535 – 2659125RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi365 – 3684Involved in interaction with stylet and aphid transmissionBy similarity
    Motifi622 – 6243Involved in virions binding and aphid transmissionBy similarity
    Motifi1343 – 13464DESH box
    Motifi1895 – 190410Nuclear 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.Curated
    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. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR002540. Pept_S30_P1_potyvir.
    IPR001456. Peptidase_C6.
    IPR001592. Poty_coat.
    IPR001730. Potyv_NIa-pro_dom.
    IPR013648. PP_Potyviridae.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    [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.
    PROSITEiPS51192. 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. Align

    Isoform Genome polyprotein (identifier: Q6XW15-1) [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

    MATMMHFGQF PSNIPLRAAT CCTKVHSTLV TKEMMASSVK PAESSSVARP     50
    IIYSSAATDG YEKAQRAFEA SFREKYSGKL EAMKYGKMVK KGGLTYVKRA 100
    GPQAIAKGIE MDAAIEKFNT AFNAGELENV TLEGDITAGI SVARGESVWL 150
    RSVFWSRSLK KQARKKTPKL VAKSDFDDLF NKVLKVASLG NIPVEIVGKK 200
    ANKILRCGYR RVNTSTIPYF HLPHHNSNYI CRELHPQRVR WLVPLLVRHR 250
    KIRDQFSDSM IARGWSGLIL PKYIASTCGR RYDEVIVRGR LYGRVEDART 300
    KLPAGDVGRT MHYSSGEERF FAGWKEGFEK LVPAQKEHIC KIVQDNKFCG 350
    KLAASIVQIA FPCHKMACDV CRNKFNEMTP EAYSELIDKH IDQRMNEINE 400
    AIVRFPGLKQ VVSNFRSKHI ASTNIKDNLE VAKLTQGHKA NQMMQLARIN 450
    SILIKGNTAT PSEISDASGL LLEITRWFNN HLSVIDKGSL RAFRNKRSSK 500
    ALVNPSLLCD NQRDKNGNFI WGERGYHSKR FFASHFDEVT PGDGYKEYII 550
    RKGPQGQRKL AIGNLIVSFD LEKTRQALKG EEVEKLPLSN SCVSKRNGNY 600
    VYTSCCVTLD DGTPLYSNIK NPTKRHLVVG TTGDPKIVDL PATDTDKMYI 650
    AKEGYCYLNI FLAMLINVNE NEAKAFTKMV RDIIIPMLGT WPTMQDLATA 700
    CFMMTAFFPE TSSAELPRIL VDHTNQTMHV IDSFGSLTTG YHVLKAGTAA 750
    QLIDFASTEL EGEMKWYRVG GHGLPVKEKM ISALITSIFR PKKLVYLIEE 800
    DPYVLIMAMC SPRLIISLFN NGALELAAKH WISRDKNVSA IFAMLMDLST 850
    EMSKAELLIE QHRMINECAK RVHDTQNYLD EVGPHQQEVR TFLALISDEL 900
    EADKELHKTG FANFSERFHS LTEKMYVDAL EEEWRGLSLL DRFSYATFVY 950
    KHKPRSTSVL PPKKSEDIDA KFVISPSWFV GKTKEHLSGG RKYVTSQITQ 1000
    FTSYIKRATL DRAMRIMCSC LKDLAYFMNV ALVTHLLISM IAAVYNMLND 1050
    HRIAKRRLYI LEMQETNTAI WHLYDTWKTV NQRDPTHEEF RKYVAKVNKN 1100
    LLRHLPEEED KAEVEYQANK VYEKKLEKAV ALMALFTMIF DTEKSGAVFS 1150
    ILRNIKSVFS TLGEEVKYQS LDEIQSIEDE KKLTIDFDLD TEITAEHTTM 1200
    DVQFEKWWDK QLSQNRVVPH YRVGGTFIEF TRHTAASVCN TICASSEQEF 1250
    VVRGAVGSGK STGLPSHLSR KGRVLLLEPT RPLAENVCKQ LRKEPFHLSP 1300
    TLRMRGLTTF GSSNISVMTS GYALHFHANN PQRLEEFDFI MIDESHTMDS 1350
    STMAFYCLLR EYEFKGKILK VSATPPGREC EFKTQHDVLI KIEESLSYNS 1400
    FVTAQGTGSN ADVVQNGDNI LVYVPSYNDV DQLSKGLMEK GHLVTKVDGR 1450
    TMKMGNVEIP TKGTSSKKHF IVATNIIENG VTLDIDVVVD FGLKVVAELD 1500
    SDSRCMRYKK VSISYGERLQ RLGRVGRVKQ GTALRIGHTE TGMTEIPVAI 1550
    ATEAAFICFA YNLPVMTHNV TSSLLSRCTN RQARTMMQYE LSPFFMVELV 1600
    HFNGCVHPQI ESKLKAYKLR DSETQLSTLA IPNSGTSRWK TVGEYKKLGV 1650
    RIEADDNVRV PFAANGVPDR LYADLWETIQ QHKSDAGFGR LTSACASKIS 1700
    YTLTTQPNAI PRTLAIIEHL LREEQQKKAY FESLNDTLCA TSFSLAGMVN 1750
    NIRRRYLKDH SAHNINVLQN AKSQLNEFNS KAIDPERVGD IMGYGVLDTV 1800
    QYQSATDVQK RLKLKGRWNG SLAATDLLIA GAVFAGGCWM LWEYTKSGNE 1850
    IVQYQGKRRQ MQKLKFRNAR DNKVGREVYG DDGTIEHFFG AAYTERGKRK 1900
    GNNSTKGMGT KTRRFVHMYG FDPTEYSFVR FVDPLTGYSK DESVQTDISL 1950
    VQSEIGEYRQ KCMEDDDELI DFIKQKPGIQ AYFMKNGSDK ALQVDLTPHI 2000
    PLLSCAKTAT IAGFPERESE LRQTGTPIVV NKNVVPGEHK EVVREEGKSI 2050
    VKGLRNYNPI SSVVCRLTND SNGNAQTLYG VGFGPLIITN SHLFKMNNGT 2100
    LFVRSHQGEF TVQNTTQLQI YHVKDKDMIL IRMPKDFPPF PMKLKFRAPH 2150
    SEERACLVGS RFQQKSLSSE VSDSTLIRPT DSGSGYWKHW VSTKEGDCGL 2200
    PMVALKDGSL IGIHGLTSVR SELNYFVPFT DDFQSKYLSN IESLEWVKHW 2250
    RHTPDKVAWN GMTLRENGPA SEFSVSKLIA DLTHGYVDEV VEQGYSSKWV 2300
    ANRLDGNLKA VASSSSQLVT KHVVKGPCVL FQEFLATHEE AARYFVPRMG 2350
    EYGPSRLNKE AFLKDFLKYA GPITVGVVNT NSFEDAVASV INMLEDLDYG 2400
    ECAYVTDPDS IFDSLNMKAA VGALYKGKKK EYFEQLNTTE REDLLRLSCE 2450
    RLYEGKMGVW NGSLKAELRP KEKLEQNKTR TFTAAPIDTL LGGKVCVDDF 2500
    NNRFYSLNLK GPWSVGMTKF YGGWNELLQK LPDGWIYCDA DGSQFDSSLT 2550
    PYLINAVVQI REHFMEDWEI GRTMLRNFYT EIVYTPILTP DGTIVKKFKG 2600
    NNSGQPSTVV DNTLMVILAM HYAMHQQCWK EEEMKEKIRF FANGDDLLIA 2650
    IYPSKEKFLN VLSEYFHELG LKYDFSSRST VRETLWFMSH RGLYLDDMYI 2700
    PKLEEERIVS ILEWDRSNEA THRAEAICAA MIEAWGYPEL LKYIREFYLW 2750
    MMQHECYRDL VRDGKLPYIA ETALRKLYTD KSVDENELVK YWKALAPEED 2800
    DGPDIVTYQG DEKPSKSSQP QSSSPQVPQQ VDAGASSQGR DKQSVIKHDS 2850
    TKSKDVGQSS TAVPRLKQIS KMRMPVSKGR QVLALDHLLD YKPEQVDLSN 2900
    TRATKEQFDN WYEAVMREYD VSDSQMGVIM NGLMVWCIEN GTSPNLSGDW 2950
    VMMDGEEQVS FPLKPIVENA KPSFRQIMHH FSDAAEAYIE MRNRERPYMP 3000
    RYGAQRNLRD KTLARYAFDF YEVTSRTTDR AREAHFQMKA AALASVSNKL 3050
    FGLDGSVATT SEDTERHTAT DVNAHMHHMM GVRQG 3085

    Note: Produced by conventional translation.

    Length:3,085
    Mass (Da):349,731
    Last modified:July 5, 2004 - v1
    Checksum:i918576B242794C0D
    GO
    Isoform P3N-PIPO polyprotein (identifier: P0CJ96-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P0CJ96.
    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:1,038
    Mass (Da):117,627
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY206394 Genomic RNA. Translation: AAP41071.1.
    RefSeqiNP_954611.1. NC_005304.1. [Q6XW15-1]

    Genome annotation databases

    GeneIDi2943205.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY206394 Genomic RNA. Translation: AAP41071.1 .
    RefSeqi NP_954611.1. NC_005304.1. [Q6XW15-1 ]

    3D structure databases

    ProteinModelPortali Q6XW15.
    SMRi Q6XW15. Positions 2055-2269.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S30.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2943205.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR002540. Pept_S30_P1_potyvir.
    IPR001456. Peptidase_C6.
    IPR001592. Poty_coat.
    IPR001730. Potyv_NIa-pro_dom.
    IPR013648. PP_Potyviridae.
    IPR001205. RNA-dir_pol_C.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00270. 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 ]
    PRINTSi PR00966. NIAPOTYPTASE.
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete nucleotide sequence, genome organization, and specific detection of beet mosaic virus."
      Nemchinov L.G., Hammond J., Jordan R., Hammond R.W.
      Arch. Virol. 149:1201-1214(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Cited for: REVIEW.

    Entry informationi

    Entry nameiPOLG_BTMV
    AccessioniPrimary (citable) accession number: Q6XW15
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 82 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

    External Data

    Dasty 3