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Protein

Replicase polyprotein 1a

Gene

1a

Organism
Human coronavirus NL63 (HCoV-NL63)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei1062For PL1-PRO activityPROSITE-ProRule annotation1
Active sitei1212For PL1-PRO activityPROSITE-ProRule annotation1
Active sitei1678For PL2-PRO activityPROSITE-ProRule annotation1
Active sitei1836For PL2-PRO activityPROSITE-ProRule annotation1
Active sitei2980For 3CL-PRO activityPROSITE-ProRule annotation1
Active sitei3083For 3CL-PRO activityPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1134 – 1165C4-type 1PROSITE-ProRule annotationAdd BLAST32
Zinc fingeri1757 – 1788C4-type 2; atypicalPROSITE-ProRule annotationAdd BLAST32
Zinc fingeri3982 – 3998By similarityAdd BLAST17
Zinc fingeri4024 – 4037By similarityAdd BLAST14

GO - Molecular functioni

GO - Biological processi

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 virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008573 Componenti: Genome

Subcellular locationi

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
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
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
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)DescriptionActionsGraphical viewLength
Transmembranei1903 – 1923HelicalSequence analysisAdd BLAST21
Transmembranei1968 – 1988HelicalSequence analysisAdd BLAST21
Transmembranei2050 – 2070HelicalSequence analysisAdd BLAST21
Transmembranei2073 – 2093HelicalSequence analysisAdd BLAST21
Transmembranei2111 – 2131HelicalSequence analysisAdd BLAST21
Transmembranei2468 – 2488HelicalSequence analysisAdd BLAST21
Transmembranei2727 – 2747HelicalSequence analysisAdd BLAST21
Transmembranei2752 – 2769HelicalSequence analysisAdd BLAST18
Transmembranei2772 – 2792HelicalSequence analysisAdd BLAST21
Transmembranei2800 – 2820HelicalSequence analysisAdd BLAST21
Transmembranei3254 – 3274HelicalSequence analysisAdd BLAST21
Transmembranei3279 – 3299HelicalSequence analysisAdd BLAST21
Transmembranei3303 – 3323HelicalSequence analysisAdd BLAST21
Transmembranei3342 – 3362HelicalSequence analysisAdd BLAST21
Transmembranei3376 – 3396HelicalSequence analysisAdd BLAST21
Transmembranei3397 – 3417HelicalSequence analysisAdd BLAST21
Transmembranei3442 – 3462HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3232683.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003382301 – 4060Replicase polyprotein 1aAdd BLAST4060
ChainiPRO_00003382311 – 110Non-structural protein 1By similarityAdd BLAST110
ChainiPRO_0000338232111 – 898Non-structural protein 2By similarityAdd BLAST788
ChainiPRO_0000338233899 – 2462Non-structural protein 3By similarityAdd BLAST1564
ChainiPRO_00003382342463 – 2939Non-structural protein 4By similarityAdd BLAST477
ChainiPRO_00003382352940 – 32423C-like proteinaseBy similarityAdd BLAST303
ChainiPRO_00003382363243 – 3521Non-structural protein 6By similarityAdd BLAST279
ChainiPRO_00003382373522 – 3604Non-structural protein 7By similarityAdd BLAST83
ChainiPRO_00003382383605 – 3799Non-structural protein 8By similarityAdd BLAST195
ChainiPRO_00003382393800 – 3908Non-structural protein 9By similarityAdd BLAST109
ChainiPRO_00003382403909 – 4043Non-structural protein 10By similarityAdd BLAST135
ChainiPRO_00003382414044 – 4060Non-structural protein 11Sequence analysisAdd BLAST17

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei110 – 111Cleavage; by PL1-PROBy similarity2
Sitei898 – 899Cleavage; by PL1-PROBy similarity2
Sitei2462 – 2463Cleavage; by PL2-PROBy similarity2
Sitei2939 – 2940Cleavage; by 3CL-PROBy similarity2
Sitei3242 – 3243Cleavage; by 3CL-PROBy similarity2
Sitei3521 – 3522Cleavage; by 3CL-PROBy similarity2
Sitei3604 – 3605Cleavage; by 3CL-PROBy similarity2
Sitei3799 – 3800Cleavage; by 3CL-PROBy similarity2
Sitei3908 – 3909Cleavage; by 3CL-PROBy similarity2
Sitei4043 – 4044Cleavage; by 3CL-PROBy similarity2

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

Chemistry databases

BindingDBiP0C6U6.

Structurei

Secondary structure

14060
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1260 – 1263Combined sources4
Beta strandi1266 – 1271Combined sources6
Helixi1273 – 1276Combined sources4
Turni1277 – 1279Combined sources3
Beta strandi1283 – 1289Combined sources7
Helixi1298 – 1306Combined sources9
Turni1307 – 1309Combined sources3
Helixi1310 – 1322Combined sources13
Beta strandi1330 – 1334Combined sources5
Beta strandi1339 – 1344Combined sources6
Helixi1352 – 1365Combined sources14
Beta strandi1366 – 1368Combined sources3
Beta strandi1370 – 1373Combined sources4
Helixi1378 – 1380Combined sources3
Helixi1384 – 1392Combined sources9
Beta strandi1400 – 1404Combined sources5
Helixi1407 – 1418Combined sources12
Helixi2950 – 2953Combined sources4
Beta strandi2956 – 2961Combined sources6
Beta strandi2964 – 2971Combined sources8
Beta strandi2974 – 2978Combined sources5
Helixi2979 – 2982Combined sources4
Helixi2992 – 2998Combined sources7
Helixi3001 – 3003Combined sources3
Beta strandi3004 – 3008Combined sources5
Beta strandi3011 – 3013Combined sources3
Beta strandi3015 – 3021Combined sources7
Beta strandi3024 – 3031Combined sources8
Beta strandi3038 – 3041Combined sources4
Beta strandi3049 – 3056Combined sources8
Beta strandi3059 – 3067Combined sources9
Beta strandi3086 – 3090Combined sources5
Beta strandi3096 – 3105Combined sources10
Beta strandi3111 – 3114Combined sources4
Helixi3121 – 3123Combined sources3
Beta strandi3126 – 3128Combined sources3
Helixi3140 – 3152Combined sources13
Helixi3166 – 3175Combined sources10
Helixi3185 – 3187Combined sources3
Helixi3188 – 3194Combined sources7
Helixi3198 – 3208Combined sources11
Beta strandi3220 – 3222Combined sources3
Helixi3229 – 3237Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VRIX-ray1.80A1258-1421[»]
3TLOX-ray1.60A/B2940-3242[»]
ProteinModelPortaliP0C6U6.
SMRiP0C6U6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C6U6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1021 – 1262Peptidase C16 1PROSITE-ProRule annotationAdd BLAST242
Domaini1263 – 1421MacroPROSITE-ProRule annotationAdd BLAST159
Domaini1640 – 1886Peptidase C16 2PROSITE-ProRule annotationAdd BLAST247
Domaini2940 – 3242Peptidase C30PROSITE-ProRule annotationAdd BLAST303

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1903 – 2131HD1By similarityAdd BLAST229
Regioni2468 – 2820HD2By similarityAdd BLAST353
Regioni3254 – 3462HD3By similarityAdd BLAST209

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi625 – 628Poly-Leu4
Compositional biasi1975 – 1978Poly-Leu4

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)DescriptionActionsGraphical viewLength
Zinc fingeri1134 – 1165C4-type 1PROSITE-ProRule annotationAdd BLAST32
Zinc fingeri1757 – 1788C4-type 2; atypicalPROSITE-ProRule annotationAdd BLAST32
Zinc fingeri3982 – 3998By similarityAdd BLAST17
Zinc fingeri4024 – 4037By similarityAdd BLAST14

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

InterProiIPR032505. Corona_NSP4_C.
IPR002589. Macro_dom.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR011050. Pectin_lyase_fold/virulence.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR009003. Peptidase_S1_PA.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR014827. Viral_protease.
[Graphical view]
PfamiPF16348. Corona_NSP4_C. 1 hit.
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]
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. AlignAdd to basket

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VRIX-ray1.80A1258-1421[»]
3TLOX-ray1.60A/B2940-3242[»]
ProteinModelPortaliP0C6U6.
SMRiP0C6U6.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP0C6U6.
ChEMBLiCHEMBL3232683.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP0C6U6.

Family and domain databases

InterProiIPR032505. Corona_NSP4_C.
IPR002589. Macro_dom.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR011050. Pectin_lyase_fold/virulence.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR009003. Peptidase_S1_PA.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR014827. Viral_protease.
[Graphical view]
PfamiPF16348. Corona_NSP4_C. 1 hit.
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]
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]
ProtoNetiSearch...

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 30, 2016
This is version 57 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, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.