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P0C6U6

- R1A_CVHNL

UniProt

P0C6U6 - R1A_CVHNL

Protein

Replicase polyprotein 1a

Gene

1a

Organism
Human coronavirus NL63 (HCoV-NL63)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 45 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3.1 Publication
    The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function By similarity.PROSITE-ProRule annotation
    Nsp7-nsp8 hexadecamer may possibly confer processivity to the polymerase, maybe by binding to dsRNA or by producing primers utilized by the latter.By similarity
    Nsp9 is a ssRNA-binding protein.By similarity

    Catalytic activityi

    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei110 – 1112Cleavage; by PL1-PROBy similarity
    Sitei898 – 8992Cleavage; by PL1-PROBy similarity
    Active sitei1062 – 10621For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1212 – 12121For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1678 – 16781For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1836 – 18361For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2462 – 24632Cleavage; by PL2-PROBy similarity
    Sitei2939 – 29402Cleavage; by 3CL-PROBy similarity
    Active sitei2980 – 29801For 3CL-PRO activityPROSITE-ProRule annotation
    Active sitei3083 – 30831For 3CL-PRO activityPROSITE-ProRule annotation
    Sitei3242 – 32432Cleavage; by 3CL-PROBy similarity
    Sitei3521 – 35222Cleavage; by 3CL-PROBy similarity
    Sitei3604 – 36052Cleavage; by 3CL-PROBy similarity
    Sitei3799 – 38002Cleavage; by 3CL-PROBy similarity
    Sitei3908 – 39092Cleavage; by 3CL-PROBy similarity
    Sitei4043 – 40442Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1134 – 116532C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1757 – 178832C4-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri3982 – 399817By similarityAdd
    BLAST
    Zinc fingeri4024 – 403714By similarityAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: InterPro
    2. omega peptidase activity Source: InterPro
    3. RNA binding Source: UniProtKB-KW
    4. RNA-directed RNA polymerase activity Source: InterPro
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. induction by virus of host autophagy Source: UniProtKB-KW
    2. modulation by virus of host protein ubiquitination Source: UniProtKB-KW
    3. suppression by virus of host IRF3 activity Source: UniProtKB-KW
    4. viral genome replication Source: InterPro
    5. viral protein processing Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Activation of host autophagy by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host IRF3 by virus, Inhibition of host RLR pathway by virus, Modulation of host ubiquitin pathway by viral deubiquitinase, Modulation of host ubiquitin pathway by virus, Ubl conjugation pathway, Viral immunoevasion

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Replicase polyprotein 1a
    Short name:
    pp1a
    Alternative name(s):
    ORF1a polyprotein
    Cleaved into the following 11 chains:
    Non-structural protein 1
    Short name:
    nsp1
    Alternative name(s):
    p9
    Non-structural protein 2
    Short name:
    nsp2
    Alternative name(s):
    p87
    Alternative name(s):
    PL1-PRO/PL2-PRO
    PLP1/PLP2
    Papain-like proteinases 1/2
    p195
    Non-structural protein 4
    Short name:
    nsp4
    Alternative name(s):
    Peptide HD2
    3C-like proteinase (EC:3.4.22.-)
    Short name:
    3CL-PRO
    Short name:
    3CLp
    Alternative name(s):
    M-PRO
    nsp5
    p34
    Non-structural protein 6
    Short name:
    nsp6
    Non-structural protein 7
    Short name:
    nsp7
    Alternative name(s):
    p5
    Non-structural protein 8
    Short name:
    nsp8
    Alternative name(s):
    p23
    Non-structural protein 9
    Short name:
    nsp9
    Alternative name(s):
    p12
    Non-structural protein 10
    Short name:
    nsp10
    Alternative name(s):
    Growth factor-like peptide
    Short name:
    GFL
    p14
    Non-structural protein 11
    Short name:
    nsp11
    Gene namesi
    ORF Names:1a
    OrganismiHuman coronavirus NL63 (HCoV-NL63)
    Taxonomic identifieri277944 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000008573: Genome

    Subcellular locationi

    Chain Non-structural protein 7 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 8 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 9 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity
    Chain Non-structural protein 10 : Host cytoplasmhost perinuclear region By similarity
    Note: nsp7, nsp8, nsp9 and nsp10 are localized in cytoplasmic foci, largely perinuclear. Late in infection, they merge into confluent complexes By similarity.By similarity

    GO - Cellular componenti

    1. host cell membrane Source: UniProtKB-SubCell
    2. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host cytoplasm, Host membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 40604060Replicase polyprotein 1aPRO_0000338230Add
    BLAST
    Chaini1 – 110110Non-structural protein 1By similarityPRO_0000338231Add
    BLAST
    Chaini111 – 898788Non-structural protein 2By similarityPRO_0000338232Add
    BLAST
    Chaini899 – 24621564Non-structural protein 3By similarityPRO_0000338233Add
    BLAST
    Chaini2463 – 2939477Non-structural protein 4By similarityPRO_0000338234Add
    BLAST
    Chaini2940 – 32423033C-like proteinaseBy similarityPRO_0000338235Add
    BLAST
    Chaini3243 – 3521279Non-structural protein 6By similarityPRO_0000338236Add
    BLAST
    Chaini3522 – 360483Non-structural protein 7By similarityPRO_0000338237Add
    BLAST
    Chaini3605 – 3799195Non-structural protein 8By similarityPRO_0000338238Add
    BLAST
    Chaini3800 – 3908109Non-structural protein 9By similarityPRO_0000338239Add
    BLAST
    Chaini3909 – 4043135Non-structural protein 10By similarityPRO_0000338240Add
    BLAST
    Chaini4044 – 406017Non-structural protein 11Sequence AnalysisPRO_0000338241Add
    BLAST

    Post-translational modificationi

    Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. 3CL-PRO and PL-PRO proteinases are autocatalytically processed.

    Interactioni

    Subunit structurei

    3CL-PRO exists as monomer and homodimer. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer By similarity.By similarity

    Structurei

    Secondary structure

    1
    4060
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1260 – 12634
    Beta strandi1266 – 12716
    Helixi1273 – 12764
    Turni1277 – 12793
    Beta strandi1283 – 12897
    Helixi1298 – 13069
    Turni1307 – 13093
    Helixi1310 – 132213
    Beta strandi1330 – 13345
    Beta strandi1339 – 13446
    Helixi1352 – 136514
    Beta strandi1366 – 13683
    Beta strandi1370 – 13734
    Helixi1378 – 13803
    Helixi1384 – 13929
    Beta strandi1400 – 14045
    Helixi1407 – 141812
    Helixi2950 – 29534
    Beta strandi2956 – 29616
    Beta strandi2964 – 29718
    Beta strandi2974 – 29785
    Helixi2979 – 29824
    Helixi2992 – 29987
    Helixi3001 – 30033
    Beta strandi3004 – 30085
    Beta strandi3011 – 30133
    Beta strandi3015 – 30217
    Beta strandi3024 – 30318
    Beta strandi3038 – 30414
    Beta strandi3049 – 30568
    Beta strandi3059 – 30679
    Beta strandi3086 – 30905
    Beta strandi3096 – 310510
    Beta strandi3111 – 31144
    Helixi3121 – 31233
    Beta strandi3126 – 31283
    Helixi3140 – 315213
    Helixi3166 – 317510
    Helixi3185 – 31873
    Helixi3188 – 31947
    Helixi3198 – 320811
    Beta strandi3220 – 32223
    Helixi3229 – 32379

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VRIX-ray1.80A1258-1421[»]
    3TLOX-ray1.60A/B2940-3242[»]
    ProteinModelPortaliP0C6U6.
    SMRiP0C6U6. Positions 2940-3240, 3802-3907, 3915-4039.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0C6U6.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1903 – 192321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1968 – 198821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2050 – 207021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2073 – 209321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2111 – 213121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2468 – 248821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2727 – 274721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2752 – 276918HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2772 – 279221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2800 – 282021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3254 – 327421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3279 – 329921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3303 – 332321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3342 – 336221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3376 – 339621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3397 – 341721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3442 – 346221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1021 – 1262242Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1263 – 1421159MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1640 – 1886247Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2940 – 3242303Peptidase C30PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1903 – 2131229HD1By similarityAdd
    BLAST
    Regioni2468 – 2820353HD2By similarityAdd
    BLAST
    Regioni3254 – 3462209HD3By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi625 – 6284Poly-Leu
    Compositional biasi1975 – 19784Poly-Leu

    Domaini

    The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane.

    Sequence similaritiesi

    Contains 1 Macro domain.PROSITE-ProRule annotation
    Contains 2 peptidase C16 domains.PROSITE-ProRule annotation
    Contains 1 peptidase C30 domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1134 – 116532C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1757 – 178832C4-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri3982 – 399817By similarityAdd
    BLAST
    Zinc fingeri4024 – 403714By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    InterProiIPR002589. Macro_dom.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR011050. Pectin_lyase_fold/virulence.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view]
    PfamiPF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF08715. Viral_protease. 2 hits.
    [Graphical view]
    SMARTiSM00506. A1pp. 1 hit.
    [Graphical view]
    SUPFAMiSSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    SSF51126. SSF51126. 1 hit.
    PROSITEiPS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 2 hits.
    [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 Replicase polyprotein 1a (identifier: P0C6U6-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    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

    MFYNQVTLAV ASDSEISGFG FAIPSVAVRT YSEAAAQGFQ ACRFVAFGLQ     50
    DCVTGINDDD YVIALTGTNQ LCAKILPFSD RPLNLRGWLI FSNSNYVLQD 100
    FDVVFGHGAG SVVFVDKYMC GFDGKPVLPK NMWEFRDYFN NNTDSIVIGG 150
    VTYQLAWDVI RKDLSYEQQN VLAIESIHYL GTTGHTLKSG CKLTNAKPPK 200
    YSSKVVLSGE WNAVYRAFGS PFITNGMSLL DIIVKPVFFN AFVKCNCGSE 250
    SWSVGAWDGY LSSCCGTPAK KLCVVPGNVV PGDVIITSTS AGCGVKYYAG 300
    LVVKHITNIT GVSLWRVTAV HSDGMFVASS SYDALLHRNS LDPFCFDVNT 350
    LLSNQLRLAF LGASVTEDVK FAASTGVIDI SAGMFGLYDD ILTNNKPWFV 400
    RKASGLFDAI WDAFVAAIKL VPTTTGVLVR FVKSIASTVL TVSNGVIIMC 450
    ADVPDAFQSV YRTFTQAICA AFDFSLDVFK IGDVKFKRLG DYVLTENALV 500
    RLTTEVVRGV RDARIKKAMF TKVVVGPTTE VKFSVIELAT VNLRLVDCAP 550
    VVCPKGKIVV IAGQAFFYSG GFYRFMVDPT TVLNDPVFTG DLFYTIKFSG 600
    FKLDGFNHQF VTASSATDAI IAVELLLLDF KTAVFVYTCV VDGCSVIVRR 650
    DATFATHVCF KDCYNVWEQF CIDNCGEPWF LTDYNAILQS NNPQCAIVQA 700
    SESKVLLERF LPKCPEILLS IDDGHLWNLF VEKFNFVTDW LKTLKLTLTS 750
    NGLLGNCAKR FRRVLVKLLD VYNGFLETVC SVAYTAGVCI KYYAVNVPYV 800
    VISGFVSRVI RRERCDMTFP CVSCVTFFYE FLDTCFGVSK PNAIDVEHLE 850
    LKETVFVEPK DGGQFFVSGD YLWYVVDDIY YPASCNGVLP VAFTKLAGGK 900
    ISFSDDVIVH DVEPTHKVKL IFEFEDDVVT SLCKKSFGKS IIYTGDWEGL 950
    HEVLTSAMNV IGQHIKLPQF YIYDEEGGYD VSKPVMISQW PISNDSNGCV 1000
    VEASTDFHQL ECIVDDSVRE EVDIIEQPFE EVEHVLSIKQ PFSFSFRDEL 1050
    GVRVLDQSDN NCWISTTLVQ LQLTKLLDDS IEMQLFKVGK VDSIVQKCYE 1100
    LSHLISGSLG DSGKLLSELL KEKYTCSITF EMSCDCGKKF DDQVGCLFWI 1150
    MPYTKLFQKG ECCICHKMQT YKLVSMKGTG VFVQDPAPID IDAFPVKPIC 1200
    SSVYLGVKGS GHYQTNLYSF NKAIDGFGVF DIKNSSVNTV CFVDVDFHSV 1250
    EIEAGEVKPF AVYKNVKFYL GDISHLVNCV SFDFVVNAAN ENLLHGGGVA 1300
    RAIDILTEGQ LQSLSKDYIS SNGPLKVGAG VMLECEKFNV FNVVGPRTGK 1350
    HEHSLLVEAY NSILFENGIP LMPLLSCGIF GVRIENSLKA LFSCDINKPL 1400
    QVFVYSSNEE QAVLKFLDGL DLTPVIDDVD VVKPFRVEGN FSFFDCGVNA 1450
    LDGDIYLLFT NSILMLDKQG QLLDTKLNGI LQQAALDYLA TVKTVPAGNL 1500
    VKLFVESCTI YMCVVPSIND LSFDKNLGRC VRKLNRLKTC VIANVPAIDV 1550
    LKKLLSSLTL TVKFVVESNV MDVNDCFKND NVVLKITEDG INVKDVVVES 1600
    SKSLGKQLGV VSDGVDSFEG VLPINTDTVL SVAPEVDWVA FYGFEKAALF 1650
    ASLDVKPYGY PNDFVGGFRV LGTTDNNCWV NATCIILQYL KPTFKSKGLN 1700
    VLWNKFVTGD VGPFVSFIYF ITMSSKGQKG DAEEALSKLS EYLISDSIVT 1750
    LEQYSTCDIC KSTVVEVKSA IVCASVLKDG CDVGFCPHRH KLRSRVKFVN 1800
    GRVVITNVGE PIISQPSKLL NGIAYTTFSG SFDNGHYVVY DAANNAVYDG 1850
    ARLFSSDLST LAVTAIVVVG GCVTSNVPTI VSEKISVMDK LDTGAQKFFQ 1900
    FGDFVMNNIV LFLTWLLSMF SLLRTSIMKH DIKVIAKAPK RTGVILTRSF 1950
    KYNIRSALFV IKQKWCVIVT LFKFLLLLYA IYALVFMIVQ FSPFNSLLCG 2000
    DIVSGYEKST FNKDIYCGNS MVCKMCLFSY QEFNDLDHTS LVWKHIRDPI 2050
    LISLQPFVIL VILLIFGNMY LRFGLLYFVA QFISTFGSFL GFHQKQWFLH 2100
    FVPFDVLCNE FLATFIVCKI VLFVRHIIVG CNNADCVACS KSARLKRVPL 2150
    QTIINGMHKS FYVNANGGTC FCNKHNFFCV NCDSFGPGNT FINGDIAREL 2200
    GNVVKTAVQP TAPAYVIIDK VDFVNGFYRL YSGDTFWRYD FDITESKYSC 2250
    KEVLKNCNVL ENFIVYNNSG SNITQIKNAC VYFSQLLCEP IKLVNSELLS 2300
    TLSVDFNGVL HKAYVDVLCN SFFKELTANM SMAECKATLG LTVSDDDFVS 2350
    AVANAHRYDV LLSDLSFNNF FISYAKPEDK LSVYDIACCM RAGSKVVNHN 2400
    VLIKESIPIV WGVKDFNTLS QEGKKYLVKT TKAKGLTFLL TFNDNQAITQ 2450
    VPATSIVAKQ GAGFKRTYNF LWYVCLFVVA LFIGVSFIDY TTTVTSFHGY 2500
    DFKYIENGQL KVFEAPLHCV RNVFDNFNQW HEAKFGVVTT NSDKCPIVVG 2550
    VSERINVVPG VPTNVYLVGK TLVFTLQAAF GNTGVCYDFD GVTTSDKCIF 2600
    NSACTRLEGL GGDNVYCYNT DLIEGSKPYS TLQPNAYYKY DAKNYVRFPE 2650
    ILARGFGLRT IRTLATRYCR VGECRDSHKG VCFGFDKWYV NDGRVDDGYI 2700
    CGDGLIDLLV NVLSIFSSSF SVVAMSGHML FNFLFAAFIT FLCFLVTKFK 2750
    RVFGDLSYGV FTVVCATLIN NISYVVTQNL FFMLLYAILY FVFTRTVRYA 2800
    WIWHIAYIVA YFLLIPWWLL TWFSFAAFLE LLPNVFKLKI STQLFEGDKF 2850
    IGTFESAAAG TFVLDMRSYE RLINTISPEK LKNYAASYNK YKYYSGSASE 2900
    ADYRCACYAH LAKAMLDYAK DHNDMLYSPP TISYNSTLQS GLKKMAQPSG 2950
    CVERCVVRVC YGSTVLNGVW LGDTVTCPRH VIAPSTTVLI DYDHAYSTMR 3000
    LHNFSVSHNG VFLGVVGVTM HGSVLRIKVS QSNVHTPKHV FKTLKPGDSF 3050
    NILACYEGIA SGVFGVNLRT NFTIKGSFIN GACGSPGYNV RNDGTVEFCY 3100
    LHQIELGSGA HVGSDFTGSV YGNFDDQPSL QVESANLMLS DNVVAFLYAA 3150
    LLNGCRWWLC STRVNVDGFN EWAMANGYTS VSSVECYSIL AAKTGVSVEQ 3200
    LLASIQHLHE GFGGKNILGY SSLCDEFTLA EVVKQMYGVN LQSGKVIFGL 3250
    KTMFLFSVFF TMFWAELFIY TNTIWINPVI LTPIFCLLLF LSLVLTMFLK 3300
    HKFLFLQVFL LPTVIATALY NCVLDYYIVK FLADHFNYNV SVLQMDVQGL 3350
    VNVLVCLFVV FLHTWRFSKE RFTHWFTYVC SLIAVAYTYF YSGDFLSLLV 3400
    MFLCAISSDW YIGAIVFRLS RLIVFFSPES VFSVFGDVKL TLVVYLICGY 3450
    LVCTYWGILY WFNRFFKCTM GVYDFKVSAA EFKYMVANGL HAPHGPFDAL 3500
    WLSFKLLGIG GDRCIKISTV QSKLTDLKCT NVVLLGCLSS MNIAANSSEW 3550
    AYCVDLHNKI NLCDDPEKAQ SMLLALLAFF LSKHSDFGLD GLIDSYFDNS 3600
    STLQSVASSF VSMPSYIAYE NARQAYEDAI ANGSSSQLIK QLKRAMNIAK 3650
    SEFDHEISVQ KKINRMAEQA ATQMYKEARS VNRKSKVISA MHSLLFGMLR 3700
    RLDMSSVETV LNLARDGVVP LSVIPATSAS KLTIVSPDLE SYSKIVCDGS 3750
    VHYAGVVWTL NDVKDNDGRP VHVKEITKEN VETLTWPLIL NCERVVKLQN 3800
    NEIMPGKLKQ KPMKAEGDGG VLGDGNALYN TEGGKTFMYA YISNKADLKF 3850
    VKWEYEGGCN TIELDSPCRF MVETPNGPQV KYLYFVKNLN TLRRGAVLGF 3900
    IGATIRLQAG KQTELAVNSG LLTACAFSVD PATTYLEAVK HGAKPVSNCI 3950
    KMLSNGAGNG QAITTSVDAN TNQDSYGGAS ICLYCRAHVP HPSMDGYCKF 4000
    KGKCVQVPIG CLDPIRFCLE NNVCNVCGCW LGHGCACDRT TIQSVDISYL 4050
    NEQGVLVQLD 4060

    Note: Produced by conventional translation.

    Length:4,060
    Mass (Da):451,388
    Last modified:June 10, 2008 - v1
    Checksum:i0F6313C474B7ED9C
    GO
    Isoform Replicase polyprotein 1ab (identifier: P0C6X5-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    The sequence of this isoform can be found in the external entry P0C6X5.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.

    Length:6,729
    Mass (Da):752,702
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY567487 Genomic RNA. No translation available.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY567487 Genomic RNA. No translation available.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VRI X-ray 1.80 A 1258-1421 [» ]
    3TLO X-ray 1.60 A/B 2940-3242 [» ]
    ProteinModelPortali P0C6U6.
    SMRi P0C6U6. Positions 2940-3240, 3802-3907, 3915-4039.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P0C6U6.

    Family and domain databases

    InterProi IPR002589. Macro_dom.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR011050. Pectin_lyase_fold/virulence.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view ]
    Pfami PF01661. Macro. 1 hit.
    PF09401. NSP10. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF08715. Viral_protease. 2 hits.
    [Graphical view ]
    SMARTi SM00506. A1pp. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 1 hit.
    SSF50494. SSF50494. 1 hit.
    SSF51126. SSF51126. 1 hit.
    PROSITEi PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
      Strain: Isolate Amsterdam I.
    2. "Deubiquitinating and interferon antagonism activities of coronavirus papain-like proteases."
      Clementz M.A., Chen Z., Banach B.S., Wang Y., Sun L., Ratia K., Baez-Santos Y.M., Wang J., Takayama J., Ghosh A.K., Li K., Mesecar A.D., Baker S.C.
      J. Virol. 84:4619-4629(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiR1A_CVHNL
    AccessioniPrimary (citable) accession number: P0C6U6
    Secondary accession number(s): Q6Q1S3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 45 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

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3