Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q98VG9

- R1AB_FIPV

UniProt

Q98VG9 - R1AB_FIPV

Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Feline coronavirus (strain FIPV WSU-79/1146) (FCoV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (17 Apr 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.
    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 By similarity.By similarity
    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
    The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G) By similarity.By similarity
    The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction.By similarity
    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
    NendoU is a Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.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).
    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei110 – 1112Cleavage; by PL1-PROBy similarity
    Sitei879 – 8802Cleavage; by PL1-PROBy similarity
    Active sitei1117 – 11171For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1268 – 12681For PL1-PRO activityPROSITE-ProRule annotation
    Active sitei1599 – 15991For PL2-PRO activityPROSITE-ProRule annotation
    Active sitei1752 – 17521For PL2-PRO activityPROSITE-ProRule annotation
    Sitei2413 – 24142Cleavage; by PL2-PROBy similarity
    Sitei2903 – 29042Cleavage; by 3CL-PROBy similarity
    Active sitei2944 – 29441For 3CL-PRO activity
    Active sitei3047 – 30471For 3CL-PRO activity
    Sitei3053 – 30531Important for substrate recognition
    Sitei3205 – 32062Cleavage; by 3CL-PROBy similarity
    Sitei3499 – 35002Cleavage; by 3CL-PROBy similarity
    Sitei3582 – 35832Cleavage; by 3CL-PROBy similarity
    Sitei3777 – 37782Cleavage; by 3CL-PROBy similarity
    Sitei3888 – 38892Cleavage; by 3CL-PROBy similarity
    Sitei4023 – 40242Cleavage; by 3CL-PROBy similarity
    Sitei4952 – 49532Cleavage; by 3CL-PROBy similarity
    Sitei5551 – 55522Cleavage; by 3CL-PROBy similarity
    Sitei6070 – 60712Cleavage; by 3CL-PROBy similarity
    Sitei6409 – 64102Cleavage; by 3CL-PROBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1188 – 121932C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1678 – 170730C4-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri3962 – 397817By similarityAdd
    BLAST
    Zinc fingeri4004 – 401714By similarityAdd
    BLAST
    Nucleotide bindingi5235 – 52428ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cysteine-type endopeptidase activity Source: InterPro
    3. endonuclease activity Source: UniProtKB-KW
    4. exoribonuclease activity, producing 5'-phosphomonoesters Source: InterPro
    5. helicase activity Source: UniProtKB-KW
    6. methyltransferase activity Source: InterPro
    7. omega peptidase activity Source: InterPro
    8. RNA binding Source: UniProtKB-KW
    9. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    10. 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. transcription, DNA-templated Source: InterPro
    5. viral genome replication Source: InterPro
    6. viral protein processing Source: InterPro

    Keywords - Molecular functioni

    Endonuclease, Exonuclease, Helicase, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase

    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, Viral RNA replication

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

    Protein family/group databases

    MEROPSiC30.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Replicase polyprotein 1ab
    Short name:
    pp1ab
    Alternative name(s):
    ORF1ab polyprotein
    Cleaved into the following 16 chains:
    Non-structural protein 1
    Short name:
    nsp1
    Non-structural protein 2
    Short name:
    nsp2
    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
    Non-structural protein 6
    Short name:
    nsp6
    Non-structural protein 7
    Short name:
    nsp7
    Non-structural protein 8
    Short name:
    nsp8
    Non-structural protein 9
    Short name:
    nsp9
    Non-structural protein 10
    Short name:
    nsp10
    Non-structural protein 11
    Short name:
    nsp11
    RNA-directed RNA polymerase (EC:2.7.7.48)
    Short name:
    Pol
    Short name:
    RdRp
    Alternative name(s):
    nsp12
    Helicase (EC:3.6.4.12, EC:3.6.4.13)
    Short name:
    Hel
    Alternative name(s):
    nsp13
    Exoribonuclease (EC:3.1.13.-)
    Short name:
    ExoN
    Alternative name(s):
    nsp14
    Alternative name(s):
    NendoU
    nsp15
    Alternative name(s):
    nsp16
    Gene namesi
    Name:rep
    ORF Names:1a-1b
    OrganismiFeline coronavirus (strain FIPV WSU-79/1146) (FCoV)
    Taxonomic identifieri33734 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
    Virus hostiFelidae (cat family) [TaxID: 9681]
    ProteomesiUP000000835: 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
    Chain Helicase : Host endoplasmic reticulum-Golgi intermediate compartment Curated
    Note: The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA.By similarity

    GO - Cellular componenti

    1. host cell endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
    2. host cell membrane Source: UniProtKB-SubCell
    3. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host cytoplasm, Host membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2944 – 29441H → Y or R: Complete loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi2967 – 29671N → A or D: Increase of 3CL-PRO activity. 1 Publication
    Mutagenesisi2986 – 29861G → A: 5% loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi2986 – 29861G → D: Increase of 3CL-PRO activity. 1 Publication
    Mutagenesisi2986 – 29861G → E: 50% loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi2986 – 29861G → P or V: 95% loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi2986 – 29861G → R, T or W: 70% loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3041 – 30411S → A: 80% loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3041 – 30411S → T: 40% loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3047 – 30471C → A or S: Complete loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3063 – 30631Y → A, F, G or T: Almost complete loss of 3CL-PRO activity. 1 Publication
    Mutagenesisi3064 – 30641M → A: Increase of 3CL-PRO activity. 1 Publication
    Mutagenesisi3065 – 30651H → A: Complete loss of 3CL-PRO activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 67096709Replicase polyprotein 1abPRO_0000283825Add
    BLAST
    Chaini1 – 110110Non-structural protein 1By similarityPRO_5000140208Add
    BLAST
    Chaini111 – 879769Non-structural protein 2By similarityPRO_5000140209Add
    BLAST
    Chaini880 – 24131534Non-structural protein 3By similarityPRO_5000140210Add
    BLAST
    Chaini2414 – 2903490Non-structural protein 4By similarityPRO_5000140211Add
    BLAST
    Chaini2904 – 32053023C-like proteinaseBy similarityPRO_5000140212Add
    BLAST
    Chaini3206 – 3499294Non-structural protein 6By similarityPRO_5000140213Add
    BLAST
    Chaini3500 – 358283Non-structural protein 7By similarityPRO_5000140214Add
    BLAST
    Chaini3583 – 3777195Non-structural protein 8By similarityPRO_5000140215Add
    BLAST
    Chaini3778 – 3888111Non-structural protein 9By similarityPRO_5000140216Add
    BLAST
    Chaini3889 – 4023135Non-structural protein 10By similarityPRO_5000140217Add
    BLAST
    Chaini4024 – 4952929RNA-directed RNA polymeraseBy similarityPRO_5000140219Add
    BLAST
    Chaini4024 – 404219Non-structural protein 11By similarityPRO_5000140218Add
    BLAST
    Chaini4953 – 5551599HelicaseBy similarityPRO_5000140220Add
    BLAST
    Chaini5552 – 6070519ExoribonucleaseSequence AnalysisPRO_5000140221Add
    BLAST
    Chaini6071 – 6409339Uridylate-specific endoribonucleaseSequence AnalysisPRO_5000140222Add
    BLAST
    Chaini6410 – 6709300Putative 2'-O-methyl transferaseSequence AnalysisPRO_5000140223Add
    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 By similarity.By similarity

    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
    6709
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1336 – 13394
    Beta strandi1342 – 13476
    Helixi1349 – 13568
    Beta strandi1359 – 13657
    Helixi1376 – 13827
    Turni1383 – 13853
    Helixi1386 – 139510
    Beta strandi1405 – 14139
    Beta strandi1416 – 14227
    Helixi1431 – 144313
    Beta strandi1449 – 14513
    Helixi1463 – 147311
    Beta strandi1479 – 14835
    Helixi1486 – 149712
    Helixi2818 – 28236
    Beta strandi2826 – 28283
    Helixi2830 – 28378
    Turni2838 – 28403
    Helixi2842 – 28509
    Helixi2852 – 28565
    Helixi2864 – 288421
    Beta strandi2889 – 28913
    Beta strandi2895 – 28995
    Helixi3510 – 35189
    Helixi3521 – 35233
    Helixi3525 – 354016
    Helixi3544 – 356118
    Helixi3568 – 357710
    Helixi3579 – 35813
    Beta strandi3583 – 35853
    Helixi3587 – 360923
    Helixi3614 – 365239
    Helixi3663 – 368018
    Helixi3683 – 369311
    Beta strandi3697 – 37026
    Beta strandi3709 – 37146
    Helixi3717 – 37237
    Beta strandi3728 – 37314
    Beta strandi3734 – 37429
    Helixi3751 – 37533
    Helixi3756 – 37616
    Beta strandi3766 – 37727

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ETIX-ray2.20A/B/C/D/E/F/G/H1331-1498[»]
    3EW5X-ray3.10A/B/C1331-1498[»]
    3GZFX-ray2.76A/B/C/D/E2808-2902[»]
    3JZTX-ray3.91A/B/C/D/E/F/G/H1331-1498[»]
    3UB0X-ray2.60A/D3583-3777[»]
    B/C/E/F3500-3582[»]
    ProteinModelPortaliQ98VG9.
    SMRiQ98VG9. Positions 2904-3204, 3894-4019.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ98VG9.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1860 – 187819HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1921 – 194121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2006 – 202621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2043 – 206523HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2426 – 244621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2691 – 271121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2720 – 274021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2771 – 279121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3212 – 323221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3242 – 326221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3267 – 328721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3306 – 332621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3339 – 335921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3396 – 341621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei3419 – 343921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1079 – 1330252Peptidase C16 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1329 – 1500172MacroPROSITE-ProRule annotationAdd
    BLAST
    Domaini1561 – 1814254Peptidase C16 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2904 – 3205302Peptidase C30PROSITE-ProRule annotationAdd
    BLAST
    Domaini4632 – 4794163RdRp catalyticAdd
    BLAST
    Domaini4953 – 503684CV MBDAdd
    BLAST
    Domaini5200 – 5391192(+)RNA virus helicase ATP-bindingAdd
    BLAST
    Domaini5392 – 5561170(+)RNA virus helicase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1860 – 2065206HD1By similarityAdd
    BLAST
    Regioni2426 – 2791366HD2By similarityAdd
    BLAST
    Regioni3212 – 3439228HD3By similarityAdd
    BLAST

    Domaini

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

    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
    Contains 1 RdRp catalytic domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1188 – 121932C4-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1678 – 170730C4-type 2; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri3962 – 397817By similarityAdd
    BLAST
    Zinc fingeri4004 – 401714By similarityAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
    IPR009461. Coronavirus_NSP16.
    IPR027352. CV_MBD_dom.
    IPR002589. Macro_dom.
    IPR009466. NSP11.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR027417. P-loop_NTPase.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR009469. RNA_pol_N_coronovir.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view]
    PfamiPF06478. Corona_RPol_N. 1 hit.
    PF01661. Macro. 1 hit.
    PF09401. NSP10. 2 hits.
    PF06471. NSP11. 1 hit.
    PF06460. NSP13. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF01443. Viral_helicase1. 1 hit.
    PF08715. Viral_protease. 2 hits.
    [Graphical view]
    SMARTiSM00506. A1pp. 1 hit.
    [Graphical view]
    SUPFAMiSSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 2 hits.
    SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF53335. SSF53335. 1 hit.
    PROSITEiPS51653. CV_MBD. 1 hit.
    PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 2 hits.
    PS51657. PSRV_HELICASE. 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 Replicase polyprotein 1ab (identifier: Q98VG9-1) [UniParc]FASTAAdd to Basket

    Also known as: pp1ab

    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

    MSSKQFKILV NEDYQVNVPS LPFRDALQEI KYCYRNGFDG YVFVPEYRRD     50
    LVDCNRKDHY VIGVLGNGIS DLKPVLLTEP SVMLQGFIVR ANCNGVLEDF 100
    DLKFARTGNG AIYVDQYMCG ADGKPVIEGE FKDYFGDEDV IIYEGEEYHC 150
    AWLTVRDEKP LWQQTLLTIR EIQYNLDIPH KLPNCAIREV APPVKKNSKV 200
    VLSEEYRKLY DIFGSPFMGN GDSLNTCFDS LHFIAATLKC PCGAESSGVG 250
    DWTGFKTACC GLHGKVKGVT LGAVKPGDAI VTSMSAGKGV KFFANSVLQY 300
    AGDVENVSVW KVIKTFTVNE TVCTTDFEGE LNDFIRPEST SPVSCSIKRA 350
    FITGEVDDAV HDCIIAGKLD LSTNLFGSAN LLFKKMPWFV QKCGAIFADA 400
    WKVVEELLCS LKLTYKQIYD VVASLCTSAF TIMDYKPVFV VSSNSVKDLV 450
    DKCVKILVKA FDVFTQTITI AGVEAKCFVL GSKYLLFNNA LVKLVSVKIL 500
    GKRQKGLDSA FFATNLIGAT VNVTPQRTES AYISLNKVDD VVTPGGGHIV 550
    IIGDMAFYKS EEYYFMMASP DSVLVNNVFK AARVPSYNIV YDVNDDTKSK 600
    MVVKIGTSFD FDGDLDAAIA KVNDLLIEFR QEKLCFRALK DGENILVEAY 650
    LKKYKMPVCL KNHVGLWDII RQDSGKKGFL DTFNHLNELE DVKDIKIQTI 700
    KNIICPDLLL ELDFGAIWYR CMPACSDKSI LGNVKIMLGN GVKVVCDGCH 750
    SFANRLTINY NKLCDTARKD IEIGGIPFST FKTPSSSFID MKDAIYSVVE 800
    YGEALSFKTA SVPVTNSGII TTDDWSDPIL LEPADYVEPK DNGDVIVIAG 850
    YTFYKDEDDH FYPYGSGMVV QKMYNKMGGG DKSVSFSDNV NVREIEPVTR 900
    VRLEFEFDNE VVTQVLEKVI GTKYKFIGTT WEEFEDSISE KLDKIFDTLA 950
    EQGVELEGYF IYDTCGGFDI NNPDGVMISQ YDLNTAADDK SDSDASVEDI 1000
    SLISDNEDVE QIEEDNTSTD DAEDVSSVEG ETVSVVDVED FVEQVSLVEE 1050
    NNVLTPAVNP DEQLSSVEKK DEVSAKNDPW AAAVDEQEAE QPKPSLTPFK 1100
    TTNLNGKIIL KQQDNNCWIN ACCYQLQAFD FFNHDLWDGF KKDDVMPFVD 1150
    FCYAALTLKQ GDSGDAEYLL ETMLNDYSTA KVTLSAKCGC GVKEIVLERT 1200
    VFKLTPLRNE FKYGVCGDCK QINMCKFASV EGSGVFVHDR IEKQTPVSQF 1250
    IVTPTMHAVY TGTTQSGHYM IEDCIHDYCV DGMGIKPRKH KFYTSTLFLN 1300
    ANVMTAKSKT MVEPPVPVED KCVEDCQSPK DLILPFYKAG KVSFYQGDLD 1350
    VLINFLEPDV LVNAANGDLR HVGGVARAID VFTGGKLTKR SKEYLKSSKA 1400
    IAPGNAVLFE NVLEHLSVLN AVGPRNGDSR VEGKLCNVYK AIAKCDGKIL 1450
    TPLISVGIFK VKLEVSLQCL LKTVTDRDLN VFVYTDQERV TIENFFNGTI 1500
    PIKVTEDTVN QKRVSVALDK TYGEQLKGTV VIKDKDVTNQ LPSVSDVGEK 1550
    VVKALDVDWN AYYGFPNAAA FSASSHDAYE FDVVTHNNFI VHKQTDNNCW 1600
    VNAICLALQR LKPTWKFPGV KSLWDAFLTR KTAGFVHMLY HISGLTKGQP 1650
    GDAELTLHKL VDLMSSDSAV TVTHTTACDK CAKVETFTGP VVAAPLLVCG 1700
    TDEICVHGVH VNVKVTSIRG TVAITSLIGP VVGDVIDATG YICYTGLNSR 1750
    GHYTYYDNRN GLMVDADKAY HFEKNLLQVT TAIASNFVAN TPKKEIMPKT 1800
    QAKESKAKES NTARVFSEVE ENPKNIVRKE KLLAIESGVD YTITTLGKYA 1850
    DVFFMAGDKI LRFLLEVFKY LLVVFMCLRK SKMPKVKVKP PHVFRNLGAK 1900
    VRTLNYVRQL NKPALWRYIK LVLLLIALYH FFYLFVSIPV VHKLACSGSV 1950
    QAYSNSSFVK SEVCGNSILC KACLASYDEL ADFDHLQVSW DYKSDPLWNR 2000
    VIQLSYFIFL AVFGNNYVRC LLMYFVSQYL NLWLSYFGYV KYSWFLHVVN 2050
    FESISVEFVI IVVVFKAVLA LKHIFLPCNN PSCKTCSKIA RQTRIPIQVV 2100
    VNGSMKTVYV HANGTGKLCK KHNFYCKNCD SYGFDHTFIC DEIVRDLSNS 2150
    IKQTVYATDR SYQEVTKVEC TDGFYRFYVG EEFTAYDYDV KHKKYSSQEV 2200
    LKTMFLLDDF IVYNPSGSSL ASVRNVCVYF SQLIGRPIKI VNSELLEDLS 2250
    VDFKGALFNA KKNVIKNSFN VDVSECKNLE ECYKLCNLDV TFSTFEMAIN 2300
    NAHRFGILIT DRSFNNFWPS KIKPGSSGVS AMDIGKCMTF DAKIVNAKVL 2350
    TQRGKSVVWL SQDFSTLSST AQKVLVKTFV EEGVNFSLTF NAVGSDEDLP 2400
    YERFTESVSA KSGSGFFDVL KQLKQLFWCL VLFITLYGLC SVYSVATQSY 2450
    IDSAEGYDYM VIKNGVVQSF DDSINCVHNT YKGFAVWFKA KHGFVPTFDK 2500
    SCPIVLGTVF DLGNMRPIPD VPAYVALVGR SLVFAINAAF GVTNVCYDHT 2550
    GAAVSKNSYF DTCVFNSACT TLTGIGGTVV YCAKQGLVEG AKLYSELLPD 2600
    YYYEHASGNM VKIPAIIRSF GLRFVKTQAT TYCRVGECTE SQAGFCFGGD 2650
    NWFVYDKEFG DGYICGSSTL GFFKNVFALF NSNMSVVATS GAMLANIVIA 2700
    CLAIAVCYGV LKFKKIFGDC TLLVVMIIVT LVVNNVSYFV TQNTFFMIVY 2750
    AIIYYFTTRK LAYPGVLDAG FIIAYLNMAP WYVLVLYIMV FLYDSLPSLF 2800
    KLKVTTNLFE GDKFVGSFES AAMGTFVIDM RSYETLVNST SLDRIKSYAN 2850
    SFNKYKYYTG SMGEADYRMA CYAHLGKALM DYSVSRNDML YTPPTVSVNS 2900
    TLQSGLRKMA QPSGVVEPCI VRVAYGNNVL NGLWLGDEVI CPRHVIASDT 2950
    SRVINYENEL SSVRLHNFSI AKNNAFLGVV SAKYKGVNLV LKVNQVNPNT 3000
    PEHKFKSVRP GESFNILACY EGCPGSVYGV NMRSQGTIKG SFIAGTCGSV 3050
    GYVLENGTLY FVYMHHLELG NGSHVGSNLE GEMYGGYEDQ PSMQLEGTNV 3100
    MSSDNVVAFL YAALINGERW FVTNTSMTLE SYNAWAKTNS FTEIVSTDAF 3150
    NMLAAKTGYS VEKLLECIVR LNKGFGGRTI LSYGSLCDEF TPTEVIRQMY 3200
    GVNLQSGKVK SIFYPMMTAI AILFAFWLEF FMYTPFTWIN PTFVSVVLAI 3250
    TTLVSVLLVA GIKHKMLFFM SFVMPSVILA TAHNVVWDMT YYESLQVLVE 3300
    NVNTTFLPVD MQGVMLALFC VVVFVICTIR FFTCKQSWFS LFATTIFVMF 3350
    NIVKLLGMIG EPWTDDHFLL CLVNMLTMLI SLTTKDWFVV FASYKVAYYI 3400
    VVYVMQPAFV QDFGFVKCVS IIYMACGYLF CCYYGILYWV NRFTCMTCGV 3450
    YQFTVSPAEL KYMTANNLSA PKTAYDAMIL SFKLMGIGGG RNIKISTVQS 3500
    KLTEMKCTNV VLLGLLSKMH VESNSKEWNY CVGLHNEINL CDDPDAVLEK 3550
    LLALIAFFLS KHNTCDLSDL IESYFENTTI LQSVASAYAA LPSWIAYEKA 3600
    RADLEEAKKN DVSPQLLKQL TKACNIAKSE FEREASVQKK LDKMAEQAAA 3650
    SMYKEARAVD RKSKIVSAMH SLLFGMLKKL DMSSVNTIIE QARNGVLPLS 3700
    IIPAASATRL IVVTPNLEVL SKVRQENNVH YAGAIWSIVE VKDANGAQVH 3750
    LKEVTAANEL NITWPLSITC ERTTKLQNNE ILPGKLKEKA VKASATIDGD 3800
    AYGSGKALMA SEGGKSFIYA FIASDSNLKY VKWESNNDVI PIELEAPLRF 3850
    YVDGVNGPEV KYLYFVKSLN TLRRGAVLGY IGATVRLQAG KPTEHPSNSG 3900
    LLTLCAFAPD PAKAYVDAVK RGMQPVTNCV KMLSNGAGNG MAITNGVESN 3950
    TQQDSYGGAS VCIYCRCHVE HPAIDGLCRF KGKFVQVPTG TQDPIRFCIE 4000
    NEVCVVCGCW LTNGCMCDRT SIQGTTIDQS YLNECGVLVQ LDLEPCNGTD 4050
    PDHVSRAFDI YNKDVACIGK FLKTNCSRFR NLDKHDAYYV VKRCTKSVMD 4100
    HEQVCYNDLK DSGVVAEHDF FLYKEGRCEF GNVARKDLTK YTMMDLCYAI 4150
    RNFDEKNCEV LKEILVTLGA CNESFFENKD WFDPVENEAI HEVYARLGPI 4200
    VANAMLKCVA FCDAIVEKGY IGIITLDNQD LNGNFYDFGD FVKTTPGFGC 4250
    ACVTSYYSYM MPLMGMTSCL ESENFVKSDI YGADYKQYDL LAYDFTDHKE 4300
    KLFHKYFKHW DRTYHPNCSD CTSDECIIHC ANFNTLFSMT IPSTAFGPLV 4350
    RKVHIDGVPV VVTAGYHFKQ LGIVWNLDVK LDTMKLSMTD LLRFVTDPTL 4400
    LVASSPALLD QRTVCFSIAA LSTGVTYQTV KPGHFNKDFY DFITERGFFE 4450
    EGSELTLKHF FFAQGGEAAM TDFNYYRYNR VTVLDICQAQ FVYKIVGKYF 4500
    ECYDGGCINA REVVVTNYDK SAGYPLNKFG KARLYYETLS YEEQDALFAL 4550
    TKRNVLPTMT QMNLKYAISG KARARTVGGV SLLSTMTTRQ YHQKHLKSIA 4600
    ATRNATVVIG STKFYGGWDN MLKNLMRDVD NGCLMGWDYP KCDRALPNMI 4650
    RMASAMILGS KHVGCCTHSD RFYRLSNELA QVLTEVVHCT GGFYFKPGGT 4700
    TSGDGTTAYA NSAFNIFQAV SANVNKLLGV DSNACNNVTV KSIQRKIYDN 4750
    CYRSSSIDEE FVVEYFSYLR KHFSMMILSD DGVVCYNKDY ADLGYVADIN 4800
    AFKATLYYQN NVFMSTSKCW VEPDLSVGPH EFCSQHTLQI VGPDGDYYLP 4850
    YPDPSRILSA GVFVDDIVKT DNVIMLERYV SLAIDAYPLT KHPKPAYQKV 4900
    FYTLLDWVKH LQKNLNAGVL DSFSVTMLEE GQDKFWSEEF YASLYEKSTV 4950
    LQAAGMCVVC GSQTVLRCGD CLRRPLLCTK CAYDHVMGTK HKFIMSITPY 5000
    VCSFNGCNVN DVTKLFLGGL SYYCMDHKPQ LSFPLCANGN VFGLYKSSAV 5050
    GSEDVEDFNK LAVSDWTNVE DYKLANNVKE SLKIFAAETV KAKEESVKSE 5100
    YAYAILKEVI GPKEIVLQWE ASKTKPPLNR NSVFTCFQIS KDTKIQLGEF 5150
    VFEQSEYGSD SVYYKSTSTY KLTPGMIFVL TSHNVSPLKA TILVNQEKYN 5200
    TISKLYPVFN IAEAYNTLVP YYQMIGKQKF TTIQGPPGSG KSHCVIGLGL 5250
    YYPQARIVYT ACSHAAVDAL CEKAAKNFNV DRCSRIIPQR IRVDCYTGFK 5300
    PNNTNAQYLF CTVNALPEAS CDIVVVDEVS MCTNYDLSVI NSRLSYKHIV 5350
    YVGDPQQLPA PRTLINKGVL QPQDYNVVTQ RVCTLGPDVF LHKCYRCPAE 5400
    IVKTVSALVY ENKFVPVNPE SKQCFKMFVK GQVQIESNSS INNKQLEVVK 5450
    AFLAHNPKWR KAVFISPYNS QNYVARRLLG LQTQTVDSAQ GSEYDYVIYT 5500
    QTSDTQHATN VNRFNVAITR AKVGILCIMC DRTMYENLDF YELKDSKIGL 5550
    QAKPETCGLF KDCSKSEQYI PPAYATTYMS LSDNFKTSDG LAVNIGTKDV 5600
    KYANVISYMG FRFEANIPGY HTLFCTRDFA MRNVRAWLGF DVEGAHVCGD 5650
    NVGTNVPLQL GFSNGVDFVV QTEGCVVTEK GNSIEVVKAR APPGEQFAHL 5700
    IPLMRKGQPW HIVRRRIVQM VCDYFDGLSD ILIFVLWAGG LELTTMRYFV 5750
    KIGRPQKCEC GKSATCYSSS QCVYACFKHA LGCDYLYNPY CIDIQQWGYT 5800
    GSLSMNHHEV CNIHRNEHVA SGDAIMTRCL AIHDCFVKRV DWSIVYPFID 5850
    NEEKINKAGR IVQSHVMKAA LKIFNPAAIH DVGNPKGIRC ATTPIPWFCY 5900
    DRDPINNNVR CLEYDYMVHG QMNGLMLFWN CNVDMYPEFS IVCRFDTRTR 5950
    SKLSLEGCNG GALYVNNHAF HTPAYDRRAF AKLKPMPFFY YDDSNCELVD 6000
    GQPNYVPLKS NVCITKCNIG GAVCKKHAAL YRAYVEDYNM FMQAGFTIWC 6050
    PQNFDTYMLW HGFVNSKALQ SLENVAFNVV KKGAFTGLKG DLPTAVIADK 6100
    IMVRDGPTDK CIFTNKTSLP TNVAFELYAK RKLGLTPPLT ILRNLGVVAT 6150
    YKFVLWDYEA ECPFSNFTKQ VCSYTDLDSE VVTCFDNSIA GSFERFTTTK 6200
    DAVLISNNAV KGLSAIKLQY GFLNDLPVST VGNKPVTWYI YVRKNGEYVE 6250
    QIDSYYTHGR TFETFKPRST MEEDFLSMDT TLFIQKYGLE DYGFEHVVFG 6300
    DVSKTTIGGM HLLISQVRLA KMGLFSVQEF MTNSDSTLKS CCITYADDPS 6350
    SKNVCTYMDI LLDDFVTIIK SLDLNVVSKV VDVIVDCKAW RWMLWCENSQ 6400
    IKTFYPQLQS AEWNPGYSMP TLYKIQRMCL ERCNLYNYGA QVRLPDGITT 6450
    NVVKYTQLCQ YLNTTTVCVP HKMRVLHLGA AGASGVAPGS TVLRRWLPDD 6500
    AILVDNDLRD YVSDADFSVT GDCTSLYIED KFDLLISDLY DGSTKSIDGE 6550
    NTSKDGFFTY INGFIKEKLS LGGSAAIKIT EFSWNKDLYE LIQRFEYWTV 6600
    FCTSVNTSSS EGFLIGINYL GPYCDKAIVD GNIMHANYIF WRNSTIMALS 6650
    HNSVLDTPKF KCRCNNALIV NLKEKELNEM VVGLLRKGKL LIRNNGKLLN 6700
    FGNHLVNVP 6709

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

    Length:6,709
    Mass (Da):751,196
    Last modified:April 17, 2007 - v2
    Checksum:iF26AC0FFF5FE27F9
    GO
    Isoform Replicase polyprotein 1a (identifier: Q98VG9-2) [UniParc]FASTAAdd to Basket

    Also known as: pp1a, ORF1a polyprotein

    The sequence of this isoform differs from the canonical sequence as follows:
         4043-6709: Missing.

    Note: Produced by conventional translation.

    Show »
    Length:4,042
    Mass (Da):449,790
    Checksum:i34663B2576D09550
    GO

    Sequence cautioni

    The sequence AAY16374.1 differs from that shown. Reason: Frameshift at position 4033.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1016 – 109277Missing in AAY32594. (PubMed:16033972)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti162 – 1621W → C.
    Natural varianti177 – 1771D → G.
    Natural varianti388 – 3881W → C.
    Natural varianti808 – 8081K → T.
    Natural varianti1784 – 17841A → V.
    Natural varianti2889 – 28891M → K.
    Natural varianti3280 – 32801A → V.
    Natural varianti3992 – 39921Q → R.
    Natural varianti4304 – 43041H → Q.
    Natural varianti5846 – 58461Y → H.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei4043 – 67092667Missing in isoform Replicase polyprotein 1a. CuratedVSP_032885Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ010921 Genomic RNA. Translation: AAY32594.1.
    DQ010921 Genomic RNA. Translation: AAY32595.1.
    AY994055 Genomic RNA. Translation: AAY16374.1. Frameshift.
    AF326575 Genomic RNA. Translation: AAK09095.1.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ010921 Genomic RNA. Translation: AAY32594.1 .
    DQ010921 Genomic RNA. Translation: AAY32595.1 .
    AY994055 Genomic RNA. Translation: AAY16374.1 . Frameshift.
    AF326575 Genomic RNA. Translation: AAK09095.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ETI X-ray 2.20 A/B/C/D/E/F/G/H 1331-1498 [» ]
    3EW5 X-ray 3.10 A/B/C 1331-1498 [» ]
    3GZF X-ray 2.76 A/B/C/D/E 2808-2902 [» ]
    3JZT X-ray 3.91 A/B/C/D/E/F/G/H 1331-1498 [» ]
    3UB0 X-ray 2.60 A/D 3583-3777 [» ]
    B/C/E/F 3500-3582 [» ]
    ProteinModelPortali Q98VG9.
    SMRi Q98VG9. Positions 2904-3204, 3894-4019.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C30.004.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q98VG9.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR027351. (+)RNA_virus_helicase_core_dom.
    IPR009461. Coronavirus_NSP16.
    IPR027352. CV_MBD_dom.
    IPR002589. Macro_dom.
    IPR009466. NSP11.
    IPR014828. NSP7.
    IPR014829. NSP8.
    IPR014822. NSP9.
    IPR027417. P-loop_NTPase.
    IPR008740. Peptidase_C30.
    IPR013016. Peptidase_C30/C16.
    IPR009469. RNA_pol_N_coronovir.
    IPR018995. RNA_synth_NSP10_coronavirus.
    IPR029063. SAM-dependent_MTases-like.
    IPR009003. Trypsin-like_Pept_dom.
    IPR014827. Viral_protease.
    [Graphical view ]
    Pfami PF06478. Corona_RPol_N. 1 hit.
    PF01661. Macro. 1 hit.
    PF09401. NSP10. 2 hits.
    PF06471. NSP11. 1 hit.
    PF06460. NSP13. 1 hit.
    PF08716. nsp7. 1 hit.
    PF08717. nsp8. 1 hit.
    PF08710. nsp9. 1 hit.
    PF05409. Peptidase_C30. 1 hit.
    PF01443. Viral_helicase1. 1 hit.
    PF08715. Viral_protease. 2 hits.
    [Graphical view ]
    SMARTi SM00506. A1pp. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101816. SSF101816. 1 hit.
    SSF144246. SSF144246. 2 hits.
    SSF50494. SSF50494. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF53335. SSF53335. 1 hit.
    PROSITEi PS51653. CV_MBD. 1 hit.
    PS51442. M_PRO. 1 hit.
    PS51154. MACRO. 1 hit.
    PS51124. PEPTIDASE_C16. 2 hits.
    PS51657. PSRV_HELICASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic RNA sequence of Feline coronavirus strain FIPV WSU-79/1146."
      Dye C., Siddell S.G.
      J. Gen. Virol. 86:2249-2253(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. Haijema B.J., de Groot-Mijnes J.D.F., Vennema H., Raamsman M.J., Rottier P.J.M., de Groot R.J.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    3. "Mutational analysis of the active centre of coronavirus 3C-like proteases."
      Hegyi A., Friebe A., Gorbalenya A.E., Ziebuhr J.
      J. Gen. Virol. 83:581-593(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2894-3215, MUTAGENESIS OF HIS-2944; ASN-2967; GLY-2986; SER-3041; CYS-3047; TYR-3063; MET-3064 AND HIS-3065.

    Entry informationi

    Entry nameiR1AB_FIPV
    AccessioniPrimary (citable) accession number: Q98VG9
    Secondary accession number(s): Q4U5G1, Q4U5G2, Q52PA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: April 17, 2007
    Last modified: October 1, 2014
    This is version 94 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

    3D-structure, Complete proteome, Reference 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