Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0C6U2 (R1A_CVH22) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Replicase polyprotein 1a

Short name=pp1a
Alternative name(s):
ORF1a polyprotein

Cleaved into the following 11 chains:

  1. Non-structural protein 1
    Short name=nsp1
    Alternative name(s):
    p9
  2. Non-structural protein 2
    Short name=nsp2
    Alternative name(s):
    p87
  3. Non-structural protein 3
    Short name=nsp3
    EC=3.4.19.12
    EC=3.4.22.-
    Alternative name(s):
    PL1-PRO/PL2-PRO
    PLP1/PLP2
    Papain-like proteinases 1/2
    p195
  4. Non-structural protein 4
    Short name=nsp4
    Alternative name(s):
    Peptide HD2
  5. 3C-like proteinase
    Short name=3CL-PRO
    Short name=3CLp
    EC=3.4.22.-
    Alternative name(s):
    M-PRO
    nsp5
    p34
  6. Non-structural protein 6
    Short name=nsp6
  7. Non-structural protein 7
    Short name=nsp7
    Alternative name(s):
    p5
  8. Non-structural protein 8
    Short name=nsp8
    Alternative name(s):
    p23
  9. Non-structural protein 9
    Short name=nsp9
    Alternative name(s):
    p12
  10. Non-structural protein 10
    Short name=nsp10
    Alternative name(s):
    Growth factor-like peptide
    Short name=GFL
    p16
  11. Non-structural protein 11
    Short name=nsp11
Gene names
ORF Names:1a
OrganismHuman coronavirus 229E (HCoV-229E) [Reference proteome]
Taxonomic identifier11137 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length4085 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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.

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 activity

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).

Subunit structure

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.

Subcellular location

Non-structural protein 3: Host membrane; Multi-pass membrane protein Potential.

Non-structural protein 4: Host membrane; Multi-pass membrane protein Potential.

Non-structural protein 6: Host membrane; Multi-pass membrane protein Potential.

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.

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.

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.

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.

Domain

The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane. Ref.4

Post-translational modification

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

Sequence similarities

Belongs to the coronaviruses polyprotein 1ab family.

Contains 1 Macro domain.

Contains 2 peptidase C16 domains.

Contains 1 peptidase C30 domain.

Ontologies

Keywords
   Biological processActivation 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
   Cellular componentHost cytoplasm
Host membrane
Membrane
   Coding sequence diversityRibosomal frameshifting
   DomainRepeat
Transmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   Molecular functionHydrolase
Protease
Thiol protease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processinduction by virus of host autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

modulation by virus of host protein ubiquitination

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host IRF3 activity

Inferred from electronic annotation. Source: UniProtKB-KW

viral genome replication

Inferred from electronic annotation. Source: InterPro

viral protein processing

Inferred from electronic annotation. Source: InterPro

   Cellular_componenthost cell membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: InterPro

cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

omega peptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]
Isoform Replicase polyprotein 1a (identifier: P0C6U2-1)

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.
Note: Produced by conventional translation.
Isoform Replicase polyprotein 1ab (identifier: P0C6X1-1)

Also known as: pp1ab;

The sequence of this isoform can be found in the external entry P0C6X1.
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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 40854085Replicase polyprotein 1a
PRO_0000338182
Chain1 – 111111Non-structural protein 1
PRO_0000338183
Chain112 – 897786Non-structural protein 2
PRO_0000338184
Chain898 – 24841587Non-structural protein 3
PRO_0000338185
Chain2485 – 2965481Non-structural protein 4
PRO_0000338186
Chain2966 – 32673023C-like proteinase
PRO_0000338187
Chain3268 – 3546279Non-structural protein 6
PRO_0000338188
Chain3547 – 362983Non-structural protein 7
PRO_0000338189
Chain3630 – 3824195Non-structural protein 8
PRO_0000338190
Chain3825 – 3933109Non-structural protein 9
PRO_0000338191
Chain3934 – 4068135Non-structural protein 10
PRO_0000338192
Chain4069 – 408517Non-structural protein 11 Potential
PRO_0000338193

Regions

Transmembrane1998 – 201821Helical; Potential
Transmembrane2068 – 208821Helical; Potential
Transmembrane2095 – 211521Helical; Potential
Transmembrane2491 – 251121Helical; Potential
Transmembrane2731 – 275121Helical; Potential
Transmembrane2755 – 277521Helical; Potential
Transmembrane2782 – 280221Helical; Potential
Transmembrane2809 – 282921Helical; Potential
Transmembrane2834 – 285421Helical; Potential
Transmembrane3281 – 330121Helical; Potential
Transmembrane3304 – 332421Helical; Potential
Transmembrane3328 – 334821Helical; Potential
Transmembrane3367 – 338721Helical; Potential
Transmembrane3401 – 342121Helical; Potential
Transmembrane3422 – 344221Helical; Potential
Transmembrane3467 – 348721Helical; Potential
Domain1016 – 1268253Peptidase C16 1
Domain1269 – 1436168Macro
Domain1663 – 1914252Peptidase C16 2
Domain2966 – 3267302Peptidase C30
Zinc finger1126 – 115732C4-type 1
Zinc finger1780 – 181536C4-type 2; atypical
Zinc finger4007 – 402317 By similarity
Zinc finger4049 – 406214 By similarity
Region1925 – 2115191HD1
Region2491 – 2854364HD2
Region3281 – 3487207HD3

Sites

Active site10541For PL1-PRO activity By similarity
Active site12051For PL1-PRO activity By similarity
Active site17011For PL2-PRO activity By similarity
Active site18631For PL2-PRO activity By similarity
Active site30061For 3CL-PRO activity
Active site31091For 3CL-PRO activity
Site111 – 1122Cleavage; by PL1-PRO
Site897 – 8982Cleavage; by PL1-PRO
Site2484 – 24852Cleavage; by PL2-PRO
Site2965 – 29662Cleavage; by 3CL-PRO
Site3267 – 32682Cleavage; by 3CL-PRO
Site3546 – 35472Cleavage; by 3CL-PRO
Site3629 – 36302Cleavage; by 3CL-PRO
Site3824 – 38252Cleavage; by 3CL-PRO
Site3933 – 39342Cleavage; by 3CL-PRO
Site4068 – 40692Cleavage; by 3CL-PRO

Experimental info

Mutagenesis10481K → E: Complete loss of PL1-PRO activity. Ref.4
Mutagenesis10541C → A, G or S: Complete loss of PL1-PRO activity. Ref.7
Mutagenesis10991G → A: Complete loss of PL1-PRO activity. Ref.4
Mutagenesis10991G → P: No effect. Ref.4
Mutagenesis11021G → A or S: No effect. Ref.4
Mutagenesis11261C → D or H: Complete loss of PL1-PRO activity. Ref.4
Mutagenesis11281C → A, D or P: Complete loss of PL1-PRO activity. Ref.4
Mutagenesis11541C → A, H or D: Complete loss of PL1-PRO activity. Ref.4
Mutagenesis11551Missing: Complete loss of PL1-PRO activity. Ref.4
Mutagenesis11571C → A, D, H or P: Complete loss of PL1-PRO activity. Ref.4
Mutagenesis11631C → A or D: No effect. Ref.4
Mutagenesis11751V → H or P: Complete loss of PL1-PRO activity. Ref.4
Mutagenesis11751V → N or T: No effect. Ref.4
Mutagenesis12031C → A: Complete loss of PL1-PRO activity. Ref.4
Mutagenesis12031C → D: No effect. Ref.4
Mutagenesis12181D → A, E, H, K, N or Q: No effect. Ref.4
Mutagenesis17021W → L: Complete loss of PL2-PRO activity. Ref.7
Mutagenesis30061H → G, S, T or Y: Complete loss of 3CL-PRO activity. Ref.3
Mutagenesis30281H → G or T: No loss of 3CL-PRO activity. Ref.3
Mutagenesis30291N → A, D, E or Q: Increase of 3CL-PRO activity. Ref.3 Ref.9
Mutagenesis30291N → G: No loss of 3CL-PRO activity. Ref.3 Ref.9
Mutagenesis30291N → P: 95% loss of 3CL-PRO activity. Ref.3 Ref.9
Mutagenesis30741E → H: No loss of 3CL-PRO activity. Ref.3
Mutagenesis30991T → D: Complete loss of 3CL-PRO activity. Ref.3
Mutagenesis31091C → P, S or V: Complete loss of 3CL-PRO activity. Ref.3
Mutagenesis31271H → S: Complete loss of 3CL-PRO activity. Ref.3
Mutagenesis31361H → A: 67% loss of 3CL-PRO activity. Ref.3
Mutagenesis31361H → S: 77% loss of 3CL-PRO activity. Ref.3
Mutagenesis31361H → T: 93% loss of 3CL-PRO activity. Ref.3
Mutagenesis32671Q → A: No loss of 3CL-PRO activity. Ref.3
Sequence conflict19821A → Q Ref.1
Sequence conflict40421F → S Ref.1

Secondary structure

............................................................................ 4085
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: EAB38E3D375F36B5

FASTA4,085454,215
        10         20         30         40         50         60 
MACNRVTLAV ASDSEISANG CSTIAQAVRR YSEAASNGFR ACRFVSLDLQ DCIVGIADDT 

        70         80         90        100        110        120 
YVMGLHGNQT LFCNIMKFSD RPFMLHGWLV FSNSNYLLEE FDVVFGKRGG GNVTYTDQYL 

       130        140        150        160        170        180 
CGADGKPVMS EDLWQFVDHF GENEEIIING HTYVCAWLTK RKPLDYKRQN NLAIEEIEYV 

       190        200        210        220        230        240 
HGDALHTLRN GSVLEMAKEV KTSSKVVLSD ALDKLYKVFG SPVMTNGSNI LEAFTKPVFI 

       250        260        270        280        290        300 
SALVQCTCGT KSWSVGDWTG FKSSCCNVIS NKLCVVPGNV KPGDAVITTQ QAGAGIKYFC 

       310        320        330        340        350        360 
GMTLKFVANI EGVSVWRVIA LQSVDCFVAS STFVEEEHVN RMDTFCFNVR NSVTDECRLA 

       370        380        390        400        410        420 
MLGAEMTSNV RRQVASGVID ISTGWFDVYD DIFAESKPWF VRKAEDIFGP CWSALASALK 

       430        440        450        460        470        480 
QLKVTTGELV RFVKSICNSA VAVVGGTIQI LASVPEKFLN AFDVFVTAIQ TVFDCAVETC 

       490        500        510        520        530        540 
TIAGKAFDKV FDYVLLDNAL VKLVTTKLKG VRERGLNKVK YATVVVGSTE EVKSSRVERS 

       550        560        570        580        590        600 
TAVLTIANNY SKLFDEGYTV VIGDVAYFVS DGYFRLMASP NSVLTTAVYK PLFAFNVNVM 

       610        620        630        640        650        660 
GTRPEKFPTT VTCENLESAV LFVNDKITEF QLDYSIDVID NEIIVKPNIS LCVPLYVRDY 

       670        680        690        700        710        720 
VDKWDDFCRQ YSNESWFEDD YRAFISVLDI TDAAVKAAES KAFVDTIVPP CPSILKVIDG 

       730        740        750        760        770        780 
GKIWNGVIKN VNSVRDWLKS LKLNLTQQGL LGTCAKRFKR WLGILLEAYN AFLDTVVSTV 

       790        800        810        820        830        840 
KIGGLTFKTY AFDKPYIVIR DIVCKVENKT EAEWIELFPH NDRIKSFSTF ESAYMPIADP 

       850        860        870        880        890        900 
THFDIEEVEL LDAEFVEPGC GGILAVIDEH VFYKKDGVYY PSNGTNILPV AFTKAAGGKV 

       910        920        930        940        950        960 
SFSDDVEVKD IEPVYRVKLC FEFEDEKLVD VCEKAIGKKI KHEGDWDSFC KTIQSALSVV 

       970        980        990       1000       1010       1020 
SCYVNLPTYY IYDEEGGNDL SLPVMISEWP LSVQQAQQEA TLPDIAEDVV DQVEEVNSIF 

      1030       1040       1050       1060       1070       1080 
DIETVDVKHD VSPFEMPFEE LNGLKILKQL DNNCWVNSVM LQIQLTGILD GDYAMQFFKM 

      1090       1100       1110       1120       1130       1140 
GRVAKMIERC YTAEQCIRGA MGDVGLCMYR LLKDLHTGFM VMDYKCSCTS GRLEESGAVL 

      1150       1160       1170       1180       1190       1200 
FCTPTKKAFP YGTCLNCNAP RMCTIRQLQG TIIFVQQKPE PVNPVSFVVK PVCSSIFRGA 

      1210       1220       1230       1240       1250       1260 
VSCGHYQTNI YSQNLCVDGF GVNKIQPWTN DALNTICIKD ADYNAKVEIS VTPIKNTVDT 

      1270       1280       1290       1300       1310       1320 
TPKEEFVVKE KLNAFLVHDN VAFYQGDVDT VVNGVDFDFI VNAANENLAH GGGLAKALDV 

      1330       1340       1350       1360       1370       1380 
YTKGKLQRLS KEHIGLAGKV KVGTGVMVEC DSLRIFNVVG PRKGKHERDL LIKAYNTINN 

      1390       1400       1410       1420       1430       1440 
EQGTPLTPIL SCGIFGIKLE TSLEVLLDVC NTKEVKVFVY TDTEVCKVKD FVSGLVNVQK 

      1450       1460       1470       1480       1490       1500 
VEQPKIEPKP VSVIKVAPKP YRVDGKFSYF TEDLLCVADD KPIVLFTDSM LTLDDRGLAL 

      1510       1520       1530       1540       1550       1560 
DNALSGVLSA AIKDCVDINK AIPSGNLIKF DIGSVVVYMC VVPSEKDKHL DNNVQRCTRK 

      1570       1580       1590       1600       1610       1620 
LNRLMCDIVC TIPADYILPL VLSSLTCNVS FVGELKAAEA KVITIKVTED GVNVHDVTVT 

      1630       1640       1650       1660       1670       1680 
TDKSFEQQVG VIADKDKDLS GAVPSDLNTS ELLTKAIDVD WVEFYGFKDA VTFATVDHSA 

      1690       1700       1710       1720       1730       1740 
FAYESAVVNG IRVLKTSDNN CWVNAVCIAL QYSKPHFISQ GLDAAWNKFV LGDVEIFVAF 

      1750       1760       1770       1780       1790       1800 
VYYVARLMKG DKGDAEDTLT KLSKYLANEA QVQLEHYSSC VECDAKFKNS VASINSAIVC 

      1810       1820       1830       1840       1850       1860 
ASVKRDGVQV GYCVHGIKYY SRVRSVRGRA IIVSVEQLEP CAQSRLLSGV AYTAFSGPVD 

      1870       1880       1890       1900       1910       1920 
KGHYTVYDTA KKSMYDGDRF VKHDLSLLSV TSVVMVGGYV APVNTVKPKP VINQLDEKAQ 

      1930       1940       1950       1960       1970       1980 
KFFDFGDFLI HNFVIFFTWL LSMFTLCKTA VTTGDVKIMA KAPQRTGVVL KRSLKYNLKA 

      1990       2000       2010       2020       2030       2040 
SAAVLKSKWW LLAKFTKLLL LIYTLYSVVL LCVRFGPFNF CSETVNGYAK SNFVKDDYCD 

      2050       2060       2070       2080       2090       2100 
GSLGCKMCLF GYQELSQFSH LDVVWKHITD PLFSNMQPFI VMVLLLIFGD NYLRCFLLYF 

      2110       2120       2130       2140       2150       2160 
VAQMISTVGV FLGYKETNWF LHFIPFDVIC DELLVTVIVI KVISFVRHVL FGCENPDCIA 

      2170       2180       2190       2200       2210       2220 
CSKSARLKRF PVNTIVNGVQ RSFYVNANGG SKFCKKHRFF CVDCDSYGYG STFITPEVSR 

      2230       2240       2250       2260       2270       2280 
ELGNITKTNV QPTGPAYVMI DKVEFENGFY RLYSCETFWR YNFDITESKY SCKEVFKNCN 

      2290       2300       2310       2320       2330       2340 
VLDDFIVFNN NGTNVTQVKN ASVYFSQLLC RPIKLVDSEL LSTLSVDFNG VLHKAYIDVL 

      2350       2360       2370       2380       2390       2400 
RNSFGKDLNA NMSLAECKRA LGLSISDHEF TSAISNAHRC DVLLSDLSFN NFVSSYAKPE 

      2410       2420       2430       2440       2450       2460 
EKLSAYDLAC CMRAGAKVVN ANVLTKDQTP IVWHAKDFNS LSAEGRKYIV KTSKAKGLTF 

      2470       2480       2490       2500       2510       2520 
LLTINENQAV TQIPATSIVA KQGAGDAGHS LTWLWLLCGL VCLIQFYLCF FMPYFMYDIV 

      2530       2540       2550       2560       2570       2580 
SSFEGYDFKY IENGQLKNFE APLKCVRNVF ENFEDWHYAK FGFTPLNKQS CPIVVGVSEI 

      2590       2600       2610       2620       2630       2640 
VNTVAGIPSN VYLVGKTLIF TLQAAFGNAG VCYDIFGVTT PEKCIFTSAC TRLEGLGGNN 

      2650       2660       2670       2680       2690       2700 
VYCYNTALME GSLPYSSIQA NAYYKYDNGN FIKLPEVIAQ GFGFRTVRTI ATKYCRVGEC 

      2710       2720       2730       2740       2750       2760 
VESNAGVCFG FDKWFVNDGR VANGYVCGTG LWNLVFNILS MFSSSFSVAA MSGQILLNCA 

      2770       2780       2790       2800       2810       2820 
LGAFAIFCCF LVTKFRRMFG DLSVGVCTVV VAVLLNNVSY IVTQNLVTMI AYAILYFFAT 

      2830       2840       2850       2860       2870       2880 
RSLRYAWIWC AAYLIAYISF APWWLCAWYF LAMLTGLLPS LLKLKVSTNL FEGDKFVGTF 

      2890       2900       2910       2920       2930       2940 
ESAAAGTFVI DMRSYEKLAN SISPEKLKSY AASYNRYKYY SGNANEADYR CACYAYLAKA 

      2950       2960       2970       2980       2990       3000 
MLDFSRDHND ILYTPPTVSY GSTLQAGLRK MAQPSGFVEK CVVRVCYGNT VLNGLWLGDI 

      3010       3020       3030       3040       3050       3060 
VYCPRHVIAS NTTSAIDYDH EYSIMRLHNF SIISGTAFLG VVGATMHGVT LKIKVSQTNM 

      3070       3080       3090       3100       3110       3120 
HTPRHSFRTL KSGEGFNILA CYDGCAQGVF GVNMRTNWTI RGSFINGACG SPGYNLKNGE 

      3130       3140       3150       3160       3170       3180 
VEFVYMHQIE LGSGSHVGSS FDGVMYGGFE DQPNLQVESA NQMLTVNVVA FLYAAILNGC 

      3190       3200       3210       3220       3230       3240 
TWWLKGEKLF VEHYNEWAQA NGFTAMNGED AFSILAAKTG VCVERLLHAI QVLNNGFGGK 

      3250       3260       3270       3280       3290       3300 
QILGYSSLND EFSINEVVKQ MFGVNLQSGK TTSMFKSISL FAGFFVMFWA ELFVYTTTIW 

      3310       3320       3330       3340       3350       3360 
VNPGFLTPFM ILLVALSLCL TFVVKHKVLF LQVFLLPSII VAAIQNCAWD YHVTKVLAEK 

      3370       3380       3390       3400       3410       3420 
FDYNVSVMQM DIQGFVNIFI CLFVALLHTW RFAKERCTHW CTYLFSLIAV LYTALYSYDY 

      3430       3440       3450       3460       3470       3480 
VSLLVMLLCA ISNEWYIGAI IFRICRFGVA FLPVEYVSYF DGVKTVLLFY MLLGFVSCMY 

      3490       3500       3510       3520       3530       3540 
YGLLYWINRF CKCTLGVYDF CVSPAEFKYM VANGLNAPNG PFDALFLSFK LMGIGGPRTI 

      3550       3560       3570       3580       3590       3600 
KVSTVQSKLT DLKCTNVVLM GILSNMNIAS NSKEWAYCVE MHNKINLCDD PETAQELLLA 

      3610       3620       3630       3640       3650       3660 
LLAFFLSKHS DFGLGDLVDS YFENDSILQS VASSFVGMPS FVAYETARQE YENAVANGSS 

      3670       3680       3690       3700       3710       3720 
PQIIKQLKKA MNVAKAEFDR ESSVQKKINR MAEQAAAAMY KEARAVNRKS KVVSAMHSLL 

      3730       3740       3750       3760       3770       3780 
FGMLRRLDMS SVDTILNMAR NGVVPLSVIP ATSAARLVVV VPDHDSFVKM MVDGFVHYAG 

      3790       3800       3810       3820       3830       3840 
VVWTLQEVKD NDGKNVHLKD VTKENQEILV WPLILTCERV VKLQNNEIMP GKMKVKATKG 

      3850       3860       3870       3880       3890       3900 
EGDGGITSEG NALYNNEGGR AFMYAYVTTK PGMKYVKWEH DSGVVTVELE PPCRFVIDTP 

      3910       3920       3930       3940       3950       3960 
TGPQIKYLYF VKNLNNLRRG AVLGYIGATV RLQAGKQTEF VSNSHLLTHC SFAVDPAAAY 

      3970       3980       3990       4000       4010       4020 
LDAVKQGAKP VGNCVKMLTN GSGSGQAITC TIDSNTTQDT YGGASVCIYC RAHVAHPTMD 

      4030       4040       4050       4060       4070       4080 
GFCQYKGKWV QVPIGTNDPI RFCLENTVCK VCGCWLNHGC TCDRTAIQSF DNSYLNESGA 


LVPLD 

« Hide

Isoform Replicase polyprotein 1ab (pp1ab) [UniParc].

See P0C6X1.

References

[1]"Infectious RNA transcribed in vitro from a cDNA copy of the human coronavirus genome cloned in vaccinia virus."
Thiel V., Herold J., Schelle B., Siddell S.G.
J. Gen. Virol. 82:1273-1281(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Nucleotide sequence of the human coronavirus 229E RNA polymerase locus."
Herold J., Raabe T., Schelle-Prinz B., Siddell S.G.
Virology 195:680-691(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase."
Ziebuhr J., Heusipp G., Siddell S.G.
J. Virol. 71:3992-3997(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF 3CL-PRO, MUTAGENESIS OF HIS-3006; HIS-3028; ASN-3029; GLU-3074; THR-3099; CYS-3109; HIS-3127; HIS-3136 AND GLN-3267.
[4]"A human RNA viral cysteine proteinase that depends upon a unique Zn2+-binding finger connecting the two domains of a papain-like fold."
Herold J., Siddell S.G., Gorbalenya A.E.
J. Biol. Chem. 274:14918-14925(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ZINC-FINGER DOMAIN OF PL1-PRO, MUTAGENESIS OF LYS-1048; GLY-1099; GLY-1102; CYS-1126; CYS-1128; CYS-1154; LEU-1155; CYS-1157; CYS-1163; VAL-1175; CYS-1203 AND ASP-1218.
[5]Erratum
Herold J., Siddell S.G., Gorbalenya A.E.
J. Biol. Chem. 274:21490-21490(1999)
[6]"Processing of the human coronavirus 229E replicase polyproteins by the virus-encoded 3C-like proteinase: identification of proteolytic products and cleavage sites common to pp1a and pp1ab."
Ziebuhr J., Siddell S.G.
J. Virol. 73:177-185(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[7]"The autocatalytic release of a putative RNA virus transcription factor from its polyprotein precursor involves two paralogous papain-like proteases that cleave the same peptide bond."
Ziebuhr J., Thiel V., Gorbalenya A.E.
J. Biol. Chem. 276:33220-33232(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, MUTAGENESIS OF CYS-1054 AND TRP-1702.
[8]"Conservation of substrate specificities among coronavirus main proteases."
Hegyi A., Ziebuhr J.
J. Gen. Virol. 83:595-599(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[9]"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: MUTAGENESIS OF ASN-3029.
[10]"Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs."
Anand K., Ziebuhr J., Wadhwani P., Mesters J.R., Hilgenfeld R.
Science 300:1763-1767(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 2966-3265.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Proteic grace - Issue 77 of December 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF304460 Genomic RNA. Translation: AAG48590.1.
X69721 Genomic RNA. Translation: CAA49377.1.
PIRS28600.
RefSeqNP_073550.1. NC_002645.1. [P0C6U2-1]

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P9SX-ray2.54A/B2966-3265[»]
2ZU2X-ray1.80A/B2966-3267[»]
3EWQX-ray2.10A1269-1436[»]
3EWRX-ray2.01A1269-1436[»]
ProteinModelPortalP0C6U2.
SMRP0C6U2. Positions 2966-3265, 3827-3932, 3940-4064.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID918764.

Family and domain databases

InterProIPR002589. 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]
PfamPF01661. 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]
SMARTSM00506. A1pp. 1 hit.
[Graphical view]
SUPFAMSSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF51126. SSF51126. 1 hit.
PROSITEPS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0C6U2.

Entry information

Entry nameR1A_CVH22
AccessionPrimary (citable) accession number: P0C6U2
Secondary accession number(s): Q05002
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references