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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.1 Publication
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.1 Publication
Nsp9 is a ssRNA-binding protein By similarity.1 Publication

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-PRO By similarity
Sitei898 – 8992Cleavage; by PL1-PRO By similarity
Active sitei1062 – 10621For PL1-PRO activity By similarity
Active sitei1212 – 12121For PL1-PRO activity By similarity
Active sitei1678 – 16781For PL2-PRO activity By similarity
Active sitei1836 – 18361For PL2-PRO activity By similarity
Sitei2462 – 24632Cleavage; by PL2-PRO By similarity
Sitei2939 – 29402Cleavage; by 3CL-PRO By similarity
Active sitei2980 – 29801For 3CL-PRO activity By similarity
Active sitei3083 – 30831For 3CL-PRO activity By similarity
Sitei3242 – 32432Cleavage; by 3CL-PRO By similarity
Sitei3521 – 35222Cleavage; by 3CL-PRO By similarity
Sitei3604 – 36052Cleavage; by 3CL-PRO By similarity
Sitei3799 – 38002Cleavage; by 3CL-PRO By similarity
Sitei3908 – 39092Cleavage; by 3CL-PRO By similarity
Sitei4043 – 40442Cleavage; by 3CL-PRO By similarity

Regions

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

Topology

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

GO - Cellular componenti

  1. host cell membrane Source: UniProtKB-SubCell
  2. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
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 1 By similarityPRO_0000338231Add
BLAST
Chaini111 – 898788Non-structural protein 2 By similarityPRO_0000338232Add
BLAST
Chaini899 – 24621564Non-structural protein 3 By similarityPRO_0000338233Add
BLAST
Chaini2463 – 2939477Non-structural protein 4 By similarityPRO_0000338234Add
BLAST
Chaini2940 – 32423033C-like proteinase By similarityPRO_0000338235Add
BLAST
Chaini3243 – 3521279Non-structural protein 6 By similarityPRO_0000338236Add
BLAST
Chaini3522 – 360483Non-structural protein 7 By similarityPRO_0000338237Add
BLAST
Chaini3605 – 3799195Non-structural protein 8 By similarityPRO_0000338238Add
BLAST
Chaini3800 – 3908109Non-structural protein 9 By similarityPRO_0000338239Add
BLAST
Chaini3909 – 4043135Non-structural protein 10 By similarityPRO_0000338240Add
BLAST
Chaini4044 – 406017Non-structural protein 11 Reviewed predictionPRO_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.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0C6U6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1021 – 1262242Peptidase C16 1Add
BLAST
Domaini1263 – 1421159MacroAdd
BLAST
Domaini1640 – 1886247Peptidase C16 2Add
BLAST
Domaini2940 – 3242303Peptidase C30Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1903 – 2131229HD1 By similarityAdd
BLAST
Regioni2468 – 2820353HD2 By similarityAdd
BLAST
Regioni3254 – 3462209HD3 By 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.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

Isoform Replicase polyprotein 1a (identifier: P0C6U6-1) [UniParc]FASTAAdd to Basket

Also known as: pp1a, ORF1a polyprotein

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

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

Note: Produced by conventional translation.

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

Also known as: pp1ab

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

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

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

Sequence databases

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

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

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

3D structure databases

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

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P0C6U6.

Family and domain databases

InterProi IPR002589. Macro_dom.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR011050. Pectin_lyase_fold/virulence.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view ]
Pfami PF01661. Macro. 1 hit.
PF09401. NSP10. 1 hit.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF08715. Viral_protease. 2 hits.
[Graphical view ]
SMARTi SM00506. A1pp. 1 hit.
[Graphical view ]
SUPFAMi SSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
SSF51126. SSF51126. 1 hit.
PROSITEi PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
[Graphical view ]
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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: May 14, 2014
This is version 44 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

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