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P0C6U6

- R1A_CVHNL

UniProt

P0C6U6 - R1A_CVHNL

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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

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
Complete GO annotation...

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

Topology

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

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. host cell membrane Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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

        10         20         30         40         50
MFYNQVTLAV ASDSEISGFG FAIPSVAVRT YSEAAAQGFQ ACRFVAFGLQ
60 70 80 90 100
DCVTGINDDD YVIALTGTNQ LCAKILPFSD RPLNLRGWLI FSNSNYVLQD
110 120 130 140 150
FDVVFGHGAG SVVFVDKYMC GFDGKPVLPK NMWEFRDYFN NNTDSIVIGG
160 170 180 190 200
VTYQLAWDVI RKDLSYEQQN VLAIESIHYL GTTGHTLKSG CKLTNAKPPK
210 220 230 240 250
YSSKVVLSGE WNAVYRAFGS PFITNGMSLL DIIVKPVFFN AFVKCNCGSE
260 270 280 290 300
SWSVGAWDGY LSSCCGTPAK KLCVVPGNVV PGDVIITSTS AGCGVKYYAG
310 320 330 340 350
LVVKHITNIT GVSLWRVTAV HSDGMFVASS SYDALLHRNS LDPFCFDVNT
360 370 380 390 400
LLSNQLRLAF LGASVTEDVK FAASTGVIDI SAGMFGLYDD ILTNNKPWFV
410 420 430 440 450
RKASGLFDAI WDAFVAAIKL VPTTTGVLVR FVKSIASTVL TVSNGVIIMC
460 470 480 490 500
ADVPDAFQSV YRTFTQAICA AFDFSLDVFK IGDVKFKRLG DYVLTENALV
510 520 530 540 550
RLTTEVVRGV RDARIKKAMF TKVVVGPTTE VKFSVIELAT VNLRLVDCAP
560 570 580 590 600
VVCPKGKIVV IAGQAFFYSG GFYRFMVDPT TVLNDPVFTG DLFYTIKFSG
610 620 630 640 650
FKLDGFNHQF VTASSATDAI IAVELLLLDF KTAVFVYTCV VDGCSVIVRR
660 670 680 690 700
DATFATHVCF KDCYNVWEQF CIDNCGEPWF LTDYNAILQS NNPQCAIVQA
710 720 730 740 750
SESKVLLERF LPKCPEILLS IDDGHLWNLF VEKFNFVTDW LKTLKLTLTS
760 770 780 790 800
NGLLGNCAKR FRRVLVKLLD VYNGFLETVC SVAYTAGVCI KYYAVNVPYV
810 820 830 840 850
VISGFVSRVI RRERCDMTFP CVSCVTFFYE FLDTCFGVSK PNAIDVEHLE
860 870 880 890 900
LKETVFVEPK DGGQFFVSGD YLWYVVDDIY YPASCNGVLP VAFTKLAGGK
910 920 930 940 950
ISFSDDVIVH DVEPTHKVKL IFEFEDDVVT SLCKKSFGKS IIYTGDWEGL
960 970 980 990 1000
HEVLTSAMNV IGQHIKLPQF YIYDEEGGYD VSKPVMISQW PISNDSNGCV
1010 1020 1030 1040 1050
VEASTDFHQL ECIVDDSVRE EVDIIEQPFE EVEHVLSIKQ PFSFSFRDEL
1060 1070 1080 1090 1100
GVRVLDQSDN NCWISTTLVQ LQLTKLLDDS IEMQLFKVGK VDSIVQKCYE
1110 1120 1130 1140 1150
LSHLISGSLG DSGKLLSELL KEKYTCSITF EMSCDCGKKF DDQVGCLFWI
1160 1170 1180 1190 1200
MPYTKLFQKG ECCICHKMQT YKLVSMKGTG VFVQDPAPID IDAFPVKPIC
1210 1220 1230 1240 1250
SSVYLGVKGS GHYQTNLYSF NKAIDGFGVF DIKNSSVNTV CFVDVDFHSV
1260 1270 1280 1290 1300
EIEAGEVKPF AVYKNVKFYL GDISHLVNCV SFDFVVNAAN ENLLHGGGVA
1310 1320 1330 1340 1350
RAIDILTEGQ LQSLSKDYIS SNGPLKVGAG VMLECEKFNV FNVVGPRTGK
1360 1370 1380 1390 1400
HEHSLLVEAY NSILFENGIP LMPLLSCGIF GVRIENSLKA LFSCDINKPL
1410 1420 1430 1440 1450
QVFVYSSNEE QAVLKFLDGL DLTPVIDDVD VVKPFRVEGN FSFFDCGVNA
1460 1470 1480 1490 1500
LDGDIYLLFT NSILMLDKQG QLLDTKLNGI LQQAALDYLA TVKTVPAGNL
1510 1520 1530 1540 1550
VKLFVESCTI YMCVVPSIND LSFDKNLGRC VRKLNRLKTC VIANVPAIDV
1560 1570 1580 1590 1600
LKKLLSSLTL TVKFVVESNV MDVNDCFKND NVVLKITEDG INVKDVVVES
1610 1620 1630 1640 1650
SKSLGKQLGV VSDGVDSFEG VLPINTDTVL SVAPEVDWVA FYGFEKAALF
1660 1670 1680 1690 1700
ASLDVKPYGY PNDFVGGFRV LGTTDNNCWV NATCIILQYL KPTFKSKGLN
1710 1720 1730 1740 1750
VLWNKFVTGD VGPFVSFIYF ITMSSKGQKG DAEEALSKLS EYLISDSIVT
1760 1770 1780 1790 1800
LEQYSTCDIC KSTVVEVKSA IVCASVLKDG CDVGFCPHRH KLRSRVKFVN
1810 1820 1830 1840 1850
GRVVITNVGE PIISQPSKLL NGIAYTTFSG SFDNGHYVVY DAANNAVYDG
1860 1870 1880 1890 1900
ARLFSSDLST LAVTAIVVVG GCVTSNVPTI VSEKISVMDK LDTGAQKFFQ
1910 1920 1930 1940 1950
FGDFVMNNIV LFLTWLLSMF SLLRTSIMKH DIKVIAKAPK RTGVILTRSF
1960 1970 1980 1990 2000
KYNIRSALFV IKQKWCVIVT LFKFLLLLYA IYALVFMIVQ FSPFNSLLCG
2010 2020 2030 2040 2050
DIVSGYEKST FNKDIYCGNS MVCKMCLFSY QEFNDLDHTS LVWKHIRDPI
2060 2070 2080 2090 2100
LISLQPFVIL VILLIFGNMY LRFGLLYFVA QFISTFGSFL GFHQKQWFLH
2110 2120 2130 2140 2150
FVPFDVLCNE FLATFIVCKI VLFVRHIIVG CNNADCVACS KSARLKRVPL
2160 2170 2180 2190 2200
QTIINGMHKS FYVNANGGTC FCNKHNFFCV NCDSFGPGNT FINGDIAREL
2210 2220 2230 2240 2250
GNVVKTAVQP TAPAYVIIDK VDFVNGFYRL YSGDTFWRYD FDITESKYSC
2260 2270 2280 2290 2300
KEVLKNCNVL ENFIVYNNSG SNITQIKNAC VYFSQLLCEP IKLVNSELLS
2310 2320 2330 2340 2350
TLSVDFNGVL HKAYVDVLCN SFFKELTANM SMAECKATLG LTVSDDDFVS
2360 2370 2380 2390 2400
AVANAHRYDV LLSDLSFNNF FISYAKPEDK LSVYDIACCM RAGSKVVNHN
2410 2420 2430 2440 2450
VLIKESIPIV WGVKDFNTLS QEGKKYLVKT TKAKGLTFLL TFNDNQAITQ
2460 2470 2480 2490 2500
VPATSIVAKQ GAGFKRTYNF LWYVCLFVVA LFIGVSFIDY TTTVTSFHGY
2510 2520 2530 2540 2550
DFKYIENGQL KVFEAPLHCV RNVFDNFNQW HEAKFGVVTT NSDKCPIVVG
2560 2570 2580 2590 2600
VSERINVVPG VPTNVYLVGK TLVFTLQAAF GNTGVCYDFD GVTTSDKCIF
2610 2620 2630 2640 2650
NSACTRLEGL GGDNVYCYNT DLIEGSKPYS TLQPNAYYKY DAKNYVRFPE
2660 2670 2680 2690 2700
ILARGFGLRT IRTLATRYCR VGECRDSHKG VCFGFDKWYV NDGRVDDGYI
2710 2720 2730 2740 2750
CGDGLIDLLV NVLSIFSSSF SVVAMSGHML FNFLFAAFIT FLCFLVTKFK
2760 2770 2780 2790 2800
RVFGDLSYGV FTVVCATLIN NISYVVTQNL FFMLLYAILY FVFTRTVRYA
2810 2820 2830 2840 2850
WIWHIAYIVA YFLLIPWWLL TWFSFAAFLE LLPNVFKLKI STQLFEGDKF
2860 2870 2880 2890 2900
IGTFESAAAG TFVLDMRSYE RLINTISPEK LKNYAASYNK YKYYSGSASE
2910 2920 2930 2940 2950
ADYRCACYAH LAKAMLDYAK DHNDMLYSPP TISYNSTLQS GLKKMAQPSG
2960 2970 2980 2990 3000
CVERCVVRVC YGSTVLNGVW LGDTVTCPRH VIAPSTTVLI DYDHAYSTMR
3010 3020 3030 3040 3050
LHNFSVSHNG VFLGVVGVTM HGSVLRIKVS QSNVHTPKHV FKTLKPGDSF
3060 3070 3080 3090 3100
NILACYEGIA SGVFGVNLRT NFTIKGSFIN GACGSPGYNV RNDGTVEFCY
3110 3120 3130 3140 3150
LHQIELGSGA HVGSDFTGSV YGNFDDQPSL QVESANLMLS DNVVAFLYAA
3160 3170 3180 3190 3200
LLNGCRWWLC STRVNVDGFN EWAMANGYTS VSSVECYSIL AAKTGVSVEQ
3210 3220 3230 3240 3250
LLASIQHLHE GFGGKNILGY SSLCDEFTLA EVVKQMYGVN LQSGKVIFGL
3260 3270 3280 3290 3300
KTMFLFSVFF TMFWAELFIY TNTIWINPVI LTPIFCLLLF LSLVLTMFLK
3310 3320 3330 3340 3350
HKFLFLQVFL LPTVIATALY NCVLDYYIVK FLADHFNYNV SVLQMDVQGL
3360 3370 3380 3390 3400
VNVLVCLFVV FLHTWRFSKE RFTHWFTYVC SLIAVAYTYF YSGDFLSLLV
3410 3420 3430 3440 3450
MFLCAISSDW YIGAIVFRLS RLIVFFSPES VFSVFGDVKL TLVVYLICGY
3460 3470 3480 3490 3500
LVCTYWGILY WFNRFFKCTM GVYDFKVSAA EFKYMVANGL HAPHGPFDAL
3510 3520 3530 3540 3550
WLSFKLLGIG GDRCIKISTV QSKLTDLKCT NVVLLGCLSS MNIAANSSEW
3560 3570 3580 3590 3600
AYCVDLHNKI NLCDDPEKAQ SMLLALLAFF LSKHSDFGLD GLIDSYFDNS
3610 3620 3630 3640 3650
STLQSVASSF VSMPSYIAYE NARQAYEDAI ANGSSSQLIK QLKRAMNIAK
3660 3670 3680 3690 3700
SEFDHEISVQ KKINRMAEQA ATQMYKEARS VNRKSKVISA MHSLLFGMLR
3710 3720 3730 3740 3750
RLDMSSVETV LNLARDGVVP LSVIPATSAS KLTIVSPDLE SYSKIVCDGS
3760 3770 3780 3790 3800
VHYAGVVWTL NDVKDNDGRP VHVKEITKEN VETLTWPLIL NCERVVKLQN
3810 3820 3830 3840 3850
NEIMPGKLKQ KPMKAEGDGG VLGDGNALYN TEGGKTFMYA YISNKADLKF
3860 3870 3880 3890 3900
VKWEYEGGCN TIELDSPCRF MVETPNGPQV KYLYFVKNLN TLRRGAVLGF
3910 3920 3930 3940 3950
IGATIRLQAG KQTELAVNSG LLTACAFSVD PATTYLEAVK HGAKPVSNCI
3960 3970 3980 3990 4000
KMLSNGAGNG QAITTSVDAN TNQDSYGGAS ICLYCRAHVP HPSMDGYCKF
4010 4020 4030 4040 4050
KGKCVQVPIG CLDPIRFCLE NNVCNVCGCW LGHGCACDRT TIQSVDISYL
4060
NEQGVLVQLD

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:
EMBLi
GenBanki
DDBJi
Links Updated
AY567487 Genomic RNA. No translation available.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY567487 Genomic RNA. No translation available.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 47 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