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P0C6U2

- R1A_CVH22

UniProt

P0C6U2 - R1A_CVH22

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Protein

Replicase polyprotein 1a

Gene
1a
Organism
Human coronavirus 229E (HCoV-229E)
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 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 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
Sitei111 – 1122Cleavage; by PL1-PRO
Sitei897 – 8982Cleavage; by PL1-PRO
Active sitei1054 – 10541For PL1-PRO activity By similarity
Active sitei1205 – 12051For PL1-PRO activity By similarity
Active sitei1701 – 17011For PL2-PRO activity By similarity
Active sitei1863 – 18631For PL2-PRO activity By similarity
Sitei2484 – 24852Cleavage; by PL2-PRO
Sitei2965 – 29662Cleavage; by 3CL-PRO
Active sitei3006 – 30061For 3CL-PRO activity
Active sitei3109 – 31091For 3CL-PRO activity
Sitei3267 – 32682Cleavage; by 3CL-PRO
Sitei3546 – 35472Cleavage; by 3CL-PRO
Sitei3629 – 36302Cleavage; by 3CL-PRO
Sitei3824 – 38252Cleavage; by 3CL-PRO
Sitei3933 – 39342Cleavage; by 3CL-PRO
Sitei4068 – 40692Cleavage; by 3CL-PRO

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1126 – 115732C4-type 1Add
BLAST
Zinc fingeri1780 – 181536C4-type 2; atypicalAdd
BLAST
Zinc fingeri4007 – 402317 By similarityAdd
BLAST
Zinc fingeri4049 – 406214 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
p16
Non-structural protein 11
Short name:
nsp11
Gene namesi
ORF Names:1a
OrganismiHuman coronavirus 229E (HCoV-229E)
Taxonomic identifieri11137 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000006716: 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
Transmembranei1998 – 201821Helical; Reviewed predictionAdd
BLAST
Transmembranei2068 – 208821Helical; Reviewed predictionAdd
BLAST
Transmembranei2095 – 211521Helical; Reviewed predictionAdd
BLAST
Transmembranei2491 – 251121Helical; Reviewed predictionAdd
BLAST
Transmembranei2731 – 275121Helical; Reviewed predictionAdd
BLAST
Transmembranei2755 – 277521Helical; Reviewed predictionAdd
BLAST
Transmembranei2782 – 280221Helical; Reviewed predictionAdd
BLAST
Transmembranei2809 – 282921Helical; Reviewed predictionAdd
BLAST
Transmembranei2834 – 285421Helical; Reviewed predictionAdd
BLAST
Transmembranei3281 – 330121Helical; Reviewed predictionAdd
BLAST
Transmembranei3304 – 332421Helical; Reviewed predictionAdd
BLAST
Transmembranei3328 – 334821Helical; Reviewed predictionAdd
BLAST
Transmembranei3367 – 338721Helical; Reviewed predictionAdd
BLAST
Transmembranei3401 – 342121Helical; Reviewed predictionAdd
BLAST
Transmembranei3422 – 344221Helical; Reviewed predictionAdd
BLAST
Transmembranei3467 – 348721Helical; 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1048 – 10481K → E: Complete loss of PL1-PRO activity. 1 Publication
Mutagenesisi1054 – 10541C → A, G or S: Complete loss of PL1-PRO activity. 1 Publication
Mutagenesisi1099 – 10991G → A: Complete loss of PL1-PRO activity. 1 Publication
Mutagenesisi1099 – 10991G → P: No effect. 1 Publication
Mutagenesisi1102 – 11021G → A or S: No effect. 1 Publication
Mutagenesisi1126 – 11261C → D or H: Complete loss of PL1-PRO activity. 1 Publication
Mutagenesisi1128 – 11281C → A, D or P: Complete loss of PL1-PRO activity. 1 Publication
Mutagenesisi1154 – 11541C → A, H or D: Complete loss of PL1-PRO activity. 1 Publication
Mutagenesisi1155 – 11551Missing: Complete loss of PL1-PRO activity. 1 Publication
Mutagenesisi1157 – 11571C → A, D, H or P: Complete loss of PL1-PRO activity. 1 Publication
Mutagenesisi1163 – 11631C → A or D: No effect. 1 Publication
Mutagenesisi1175 – 11751V → H or P: Complete loss of PL1-PRO activity. 1 Publication
Mutagenesisi1175 – 11751V → N or T: No effect. 1 Publication
Mutagenesisi1203 – 12031C → A: Complete loss of PL1-PRO activity. 1 Publication
Mutagenesisi1203 – 12031C → D: No effect. 1 Publication
Mutagenesisi1218 – 12181D → A, E, H, K, N or Q: No effect. 1 Publication
Mutagenesisi1702 – 17021W → L: Complete loss of PL2-PRO activity. 1 Publication
Mutagenesisi3006 – 30061H → G, S, T or Y: Complete loss of 3CL-PRO activity. 1 Publication
Mutagenesisi3028 – 30281H → G or T: No loss of 3CL-PRO activity. 1 Publication
Mutagenesisi3029 – 30291N → A, D, E or Q: Increase of 3CL-PRO activity. 2 Publications
Mutagenesisi3029 – 30291N → G: No loss of 3CL-PRO activity. 2 Publications
Mutagenesisi3029 – 30291N → P: 95% loss of 3CL-PRO activity. 2 Publications
Mutagenesisi3074 – 30741E → H: No loss of 3CL-PRO activity. 1 Publication
Mutagenesisi3099 – 30991T → D: Complete loss of 3CL-PRO activity. 1 Publication
Mutagenesisi3109 – 31091C → P, S or V: Complete loss of 3CL-PRO activity. 1 Publication
Mutagenesisi3127 – 31271H → S: Complete loss of 3CL-PRO activity. 1 Publication
Mutagenesisi3136 – 31361H → A: 67% loss of 3CL-PRO activity. 1 Publication
Mutagenesisi3136 – 31361H → S: 77% loss of 3CL-PRO activity. 1 Publication
Mutagenesisi3136 – 31361H → T: 93% loss of 3CL-PRO activity. 1 Publication
Mutagenesisi3267 – 32671Q → A: No loss of 3CL-PRO activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 40854085Replicase polyprotein 1aPRO_0000338182Add
BLAST
Chaini1 – 111111Non-structural protein 1PRO_0000338183Add
BLAST
Chaini112 – 897786Non-structural protein 2PRO_0000338184Add
BLAST
Chaini898 – 24841587Non-structural protein 3PRO_0000338185Add
BLAST
Chaini2485 – 2965481Non-structural protein 4PRO_0000338186Add
BLAST
Chaini2966 – 32673023C-like proteinasePRO_0000338187Add
BLAST
Chaini3268 – 3546279Non-structural protein 6PRO_0000338188Add
BLAST
Chaini3547 – 362983Non-structural protein 7PRO_0000338189Add
BLAST
Chaini3630 – 3824195Non-structural protein 8PRO_0000338190Add
BLAST
Chaini3825 – 3933109Non-structural protein 9PRO_0000338191Add
BLAST
Chaini3934 – 4068135Non-structural protein 10PRO_0000338192Add
BLAST
Chaini4069 – 408517Non-structural protein 11 Reviewed predictionPRO_0000338193Add
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
4085
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1275 – 12784
Beta strandi1281 – 12855
Helixi1288 – 12947
Beta strandi1298 – 13047
Helixi1313 – 13219
Turni1322 – 13243
Helixi1325 – 13339
Beta strandi1345 – 13506
Beta strandi1353 – 13597
Helixi1367 – 138014
Beta strandi1381 – 13833
Beta strandi1385 – 13873
Helixi1399 – 140911
Beta strandi1415 – 14195
Helixi1422 – 143312
Helixi2976 – 29794
Beta strandi2982 – 29876
Beta strandi2990 – 29978
Beta strandi3000 – 30045
Helixi3005 – 30084
Helixi3018 – 30247
Helixi3027 – 30293
Beta strandi3030 – 30345
Beta strandi3037 – 30393
Beta strandi3041 – 30477
Beta strandi3050 – 30578
Beta strandi3064 – 30674
Beta strandi3075 – 309319
Beta strandi3112 – 31176
Beta strandi3120 – 313011
Beta strandi3136 – 31394
Helixi3146 – 31483
Beta strandi3151 – 31544
Helixi3165 – 317713
Helixi3191 – 31999
Turni3200 – 32023
Helixi3209 – 32124
Helixi3213 – 32197
Helixi3223 – 323311
Beta strandi3245 – 32473
Helixi3254 – 32629

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P9SX-ray2.54A/B2966-3265[»]
2ZU2X-ray1.80A/B2966-3267[»]
3EWQX-ray2.10A1269-1436[»]
3EWRX-ray2.01A1269-1436[»]
ProteinModelPortaliP0C6U2.
SMRiP0C6U2. Positions 2966-3265, 3827-3932, 3940-4064.

Miscellaneous databases

EvolutionaryTraceiP0C6U2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1016 – 1268253Peptidase C16 1Add
BLAST
Domaini1269 – 1436168MacroAdd
BLAST
Domaini1663 – 1914252Peptidase C16 2Add
BLAST
Domaini2966 – 3267302Peptidase C30Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1925 – 2115191HD1Add
BLAST
Regioni2491 – 2854364HD2Add
BLAST
Regioni3281 – 3487207HD3Add
BLAST

Domaini

The hydrophobic domains (HD) could mediate the membrane association of the replication complex and thereby alter the architecture of the host cell membrane.1 Publication

Sequence similaritiesi

Contains 1 Macro domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1126 – 115732C4-type 1Add
BLAST
Zinc fingeri1780 – 181536C4-type 2; atypicalAdd
BLAST
Zinc fingeri4007 – 402317 By similarityAdd
BLAST
Zinc fingeri4049 – 406214 By 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: P0C6U2-1) [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.

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MACNRVTLAV ASDSEISANG CSTIAQAVRR YSEAASNGFR ACRFVSLDLQ     50
DCIVGIADDT YVMGLHGNQT LFCNIMKFSD RPFMLHGWLV FSNSNYLLEE 100
FDVVFGKRGG GNVTYTDQYL CGADGKPVMS EDLWQFVDHF GENEEIIING 150
HTYVCAWLTK RKPLDYKRQN NLAIEEIEYV HGDALHTLRN GSVLEMAKEV 200
KTSSKVVLSD ALDKLYKVFG SPVMTNGSNI LEAFTKPVFI SALVQCTCGT 250
KSWSVGDWTG FKSSCCNVIS NKLCVVPGNV KPGDAVITTQ QAGAGIKYFC 300
GMTLKFVANI EGVSVWRVIA LQSVDCFVAS STFVEEEHVN RMDTFCFNVR 350
NSVTDECRLA MLGAEMTSNV RRQVASGVID ISTGWFDVYD DIFAESKPWF 400
VRKAEDIFGP CWSALASALK QLKVTTGELV RFVKSICNSA VAVVGGTIQI 450
LASVPEKFLN AFDVFVTAIQ TVFDCAVETC TIAGKAFDKV FDYVLLDNAL 500
VKLVTTKLKG VRERGLNKVK YATVVVGSTE EVKSSRVERS TAVLTIANNY 550
SKLFDEGYTV VIGDVAYFVS DGYFRLMASP NSVLTTAVYK PLFAFNVNVM 600
GTRPEKFPTT VTCENLESAV LFVNDKITEF QLDYSIDVID NEIIVKPNIS 650
LCVPLYVRDY VDKWDDFCRQ YSNESWFEDD YRAFISVLDI TDAAVKAAES 700
KAFVDTIVPP CPSILKVIDG GKIWNGVIKN VNSVRDWLKS LKLNLTQQGL 750
LGTCAKRFKR WLGILLEAYN AFLDTVVSTV KIGGLTFKTY AFDKPYIVIR 800
DIVCKVENKT EAEWIELFPH NDRIKSFSTF ESAYMPIADP THFDIEEVEL 850
LDAEFVEPGC GGILAVIDEH VFYKKDGVYY PSNGTNILPV AFTKAAGGKV 900
SFSDDVEVKD IEPVYRVKLC FEFEDEKLVD VCEKAIGKKI KHEGDWDSFC 950
KTIQSALSVV SCYVNLPTYY IYDEEGGNDL SLPVMISEWP LSVQQAQQEA 1000
TLPDIAEDVV DQVEEVNSIF DIETVDVKHD VSPFEMPFEE LNGLKILKQL 1050
DNNCWVNSVM LQIQLTGILD GDYAMQFFKM GRVAKMIERC YTAEQCIRGA 1100
MGDVGLCMYR LLKDLHTGFM VMDYKCSCTS GRLEESGAVL FCTPTKKAFP 1150
YGTCLNCNAP RMCTIRQLQG TIIFVQQKPE PVNPVSFVVK PVCSSIFRGA 1200
VSCGHYQTNI YSQNLCVDGF GVNKIQPWTN DALNTICIKD ADYNAKVEIS 1250
VTPIKNTVDT TPKEEFVVKE KLNAFLVHDN VAFYQGDVDT VVNGVDFDFI 1300
VNAANENLAH GGGLAKALDV YTKGKLQRLS KEHIGLAGKV KVGTGVMVEC 1350
DSLRIFNVVG PRKGKHERDL LIKAYNTINN EQGTPLTPIL SCGIFGIKLE 1400
TSLEVLLDVC NTKEVKVFVY TDTEVCKVKD FVSGLVNVQK VEQPKIEPKP 1450
VSVIKVAPKP YRVDGKFSYF TEDLLCVADD KPIVLFTDSM LTLDDRGLAL 1500
DNALSGVLSA AIKDCVDINK AIPSGNLIKF DIGSVVVYMC VVPSEKDKHL 1550
DNNVQRCTRK LNRLMCDIVC TIPADYILPL VLSSLTCNVS FVGELKAAEA 1600
KVITIKVTED GVNVHDVTVT TDKSFEQQVG VIADKDKDLS GAVPSDLNTS 1650
ELLTKAIDVD WVEFYGFKDA VTFATVDHSA FAYESAVVNG IRVLKTSDNN 1700
CWVNAVCIAL QYSKPHFISQ GLDAAWNKFV LGDVEIFVAF VYYVARLMKG 1750
DKGDAEDTLT KLSKYLANEA QVQLEHYSSC VECDAKFKNS VASINSAIVC 1800
ASVKRDGVQV GYCVHGIKYY SRVRSVRGRA IIVSVEQLEP CAQSRLLSGV 1850
AYTAFSGPVD KGHYTVYDTA KKSMYDGDRF VKHDLSLLSV TSVVMVGGYV 1900
APVNTVKPKP VINQLDEKAQ KFFDFGDFLI HNFVIFFTWL LSMFTLCKTA 1950
VTTGDVKIMA KAPQRTGVVL KRSLKYNLKA SAAVLKSKWW LLAKFTKLLL 2000
LIYTLYSVVL LCVRFGPFNF CSETVNGYAK SNFVKDDYCD GSLGCKMCLF 2050
GYQELSQFSH LDVVWKHITD PLFSNMQPFI VMVLLLIFGD NYLRCFLLYF 2100
VAQMISTVGV FLGYKETNWF LHFIPFDVIC DELLVTVIVI KVISFVRHVL 2150
FGCENPDCIA CSKSARLKRF PVNTIVNGVQ RSFYVNANGG SKFCKKHRFF 2200
CVDCDSYGYG STFITPEVSR ELGNITKTNV QPTGPAYVMI DKVEFENGFY 2250
RLYSCETFWR YNFDITESKY SCKEVFKNCN VLDDFIVFNN NGTNVTQVKN 2300
ASVYFSQLLC RPIKLVDSEL LSTLSVDFNG VLHKAYIDVL RNSFGKDLNA 2350
NMSLAECKRA LGLSISDHEF TSAISNAHRC DVLLSDLSFN NFVSSYAKPE 2400
EKLSAYDLAC CMRAGAKVVN ANVLTKDQTP IVWHAKDFNS LSAEGRKYIV 2450
KTSKAKGLTF LLTINENQAV TQIPATSIVA KQGAGDAGHS LTWLWLLCGL 2500
VCLIQFYLCF FMPYFMYDIV SSFEGYDFKY IENGQLKNFE APLKCVRNVF 2550
ENFEDWHYAK FGFTPLNKQS CPIVVGVSEI VNTVAGIPSN VYLVGKTLIF 2600
TLQAAFGNAG VCYDIFGVTT PEKCIFTSAC TRLEGLGGNN VYCYNTALME 2650
GSLPYSSIQA NAYYKYDNGN FIKLPEVIAQ GFGFRTVRTI ATKYCRVGEC 2700
VESNAGVCFG FDKWFVNDGR VANGYVCGTG LWNLVFNILS MFSSSFSVAA 2750
MSGQILLNCA LGAFAIFCCF LVTKFRRMFG DLSVGVCTVV VAVLLNNVSY 2800
IVTQNLVTMI AYAILYFFAT RSLRYAWIWC AAYLIAYISF APWWLCAWYF 2850
LAMLTGLLPS LLKLKVSTNL FEGDKFVGTF ESAAAGTFVI DMRSYEKLAN 2900
SISPEKLKSY AASYNRYKYY SGNANEADYR CACYAYLAKA MLDFSRDHND 2950
ILYTPPTVSY GSTLQAGLRK MAQPSGFVEK CVVRVCYGNT VLNGLWLGDI 3000
VYCPRHVIAS NTTSAIDYDH EYSIMRLHNF SIISGTAFLG VVGATMHGVT 3050
LKIKVSQTNM HTPRHSFRTL KSGEGFNILA CYDGCAQGVF GVNMRTNWTI 3100
RGSFINGACG SPGYNLKNGE VEFVYMHQIE LGSGSHVGSS FDGVMYGGFE 3150
DQPNLQVESA NQMLTVNVVA FLYAAILNGC TWWLKGEKLF VEHYNEWAQA 3200
NGFTAMNGED AFSILAAKTG VCVERLLHAI QVLNNGFGGK QILGYSSLND 3250
EFSINEVVKQ MFGVNLQSGK TTSMFKSISL FAGFFVMFWA ELFVYTTTIW 3300
VNPGFLTPFM ILLVALSLCL TFVVKHKVLF LQVFLLPSII VAAIQNCAWD 3350
YHVTKVLAEK FDYNVSVMQM DIQGFVNIFI CLFVALLHTW RFAKERCTHW 3400
CTYLFSLIAV LYTALYSYDY VSLLVMLLCA ISNEWYIGAI IFRICRFGVA 3450
FLPVEYVSYF DGVKTVLLFY MLLGFVSCMY YGLLYWINRF CKCTLGVYDF 3500
CVSPAEFKYM VANGLNAPNG PFDALFLSFK LMGIGGPRTI KVSTVQSKLT 3550
DLKCTNVVLM GILSNMNIAS NSKEWAYCVE MHNKINLCDD PETAQELLLA 3600
LLAFFLSKHS DFGLGDLVDS YFENDSILQS VASSFVGMPS FVAYETARQE 3650
YENAVANGSS PQIIKQLKKA MNVAKAEFDR ESSVQKKINR MAEQAAAAMY 3700
KEARAVNRKS KVVSAMHSLL FGMLRRLDMS SVDTILNMAR NGVVPLSVIP 3750
ATSAARLVVV VPDHDSFVKM MVDGFVHYAG VVWTLQEVKD NDGKNVHLKD 3800
VTKENQEILV WPLILTCERV VKLQNNEIMP GKMKVKATKG EGDGGITSEG 3850
NALYNNEGGR AFMYAYVTTK PGMKYVKWEH DSGVVTVELE PPCRFVIDTP 3900
TGPQIKYLYF VKNLNNLRRG AVLGYIGATV RLQAGKQTEF VSNSHLLTHC 3950
SFAVDPAAAY LDAVKQGAKP VGNCVKMLTN GSGSGQAITC TIDSNTTQDT 4000
YGGASVCIYC RAHVAHPTMD GFCQYKGKWV QVPIGTNDPI RFCLENTVCK 4050
VCGCWLNHGC TCDRTAIQSF DNSYLNESGA LVPLD 4085

Note: Produced by conventional translation.

Length:4,085
Mass (Da):454,215
Last modified:June 10, 2008 - v1
Checksum:iEAB38E3D375F36B5
GO
Isoform Replicase polyprotein 1ab (identifier: P0C6X1-1) [UniParc]FASTAAdd to Basket

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.

Length:6,758
Mass (Da):754,163
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1982 – 19821A → Q1 Publication
Sequence conflicti4042 – 40421F → S1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF304460 Genomic RNA. Translation: AAG48590.1.
X69721 Genomic RNA. Translation: CAA49377.1.
PIRiS28600.
RefSeqiNP_073550.1. NC_002645.1. [P0C6U2-1]

Genome annotation databases

GeneIDi918764.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Web resourcesi

Protein Spotlight

Proteic grace - Issue 77 of December 2006

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF304460 Genomic RNA. Translation: AAG48590.1 .
X69721 Genomic RNA. Translation: CAA49377.1 .
PIRi S28600.
RefSeqi NP_073550.1. NC_002645.1. [P0C6U2-1 ]

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P9S X-ray 2.54 A/B 2966-3265 [» ]
2ZU2 X-ray 1.80 A/B 2966-3267 [» ]
3EWQ X-ray 2.10 A 1269-1436 [» ]
3EWR X-ray 2.01 A 1269-1436 [» ]
ProteinModelPortali P0C6U2.
SMRi P0C6U2. Positions 2966-3265, 3827-3932, 3940-4064.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 918764.

Miscellaneous databases

EvolutionaryTracei P0C6U2.

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. "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.

Entry informationi

Entry nameiR1A_CVH22
AccessioniPrimary (citable) accession number: P0C6U2
Secondary accession number(s): Q05002
Entry historyi
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 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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