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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).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).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
Sitei111 – 1122Cleavage; by PL1-PRO
Sitei897 – 8982Cleavage; by PL1-PRO
Active sitei1054 – 10541For PL1-PRO activityPROSITE-ProRule annotation
Active sitei1205 – 12051For PL1-PRO activityPROSITE-ProRule annotation
Active sitei1701 – 17011For PL2-PRO activityPROSITE-ProRule annotation
Active sitei1863 – 18631For PL2-PRO activityPROSITE-ProRule annotation
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 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1780 – 181536C4-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4007 – 402317By similarityAdd
BLAST
Zinc fingeri4049 – 406214By 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).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

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

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 11Sequence AnalysisPRO_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.3 Publications

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
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C6U2.

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1998 – 201821HelicalSequence AnalysisAdd
BLAST
Transmembranei2068 – 208821HelicalSequence AnalysisAdd
BLAST
Transmembranei2095 – 211521HelicalSequence AnalysisAdd
BLAST
Transmembranei2491 – 251121HelicalSequence AnalysisAdd
BLAST
Transmembranei2731 – 275121HelicalSequence AnalysisAdd
BLAST
Transmembranei2755 – 277521HelicalSequence AnalysisAdd
BLAST
Transmembranei2782 – 280221HelicalSequence AnalysisAdd
BLAST
Transmembranei2809 – 282921HelicalSequence AnalysisAdd
BLAST
Transmembranei2834 – 285421HelicalSequence AnalysisAdd
BLAST
Transmembranei3281 – 330121HelicalSequence AnalysisAdd
BLAST
Transmembranei3304 – 332421HelicalSequence AnalysisAdd
BLAST
Transmembranei3328 – 334821HelicalSequence AnalysisAdd
BLAST
Transmembranei3367 – 338721HelicalSequence AnalysisAdd
BLAST
Transmembranei3401 – 342121HelicalSequence AnalysisAdd
BLAST
Transmembranei3422 – 344221HelicalSequence AnalysisAdd
BLAST
Transmembranei3467 – 348721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1016 – 1268253Peptidase C16 1PROSITE-ProRule annotationAdd
BLAST
Domaini1269 – 1436168MacroPROSITE-ProRule annotationAdd
BLAST
Domaini1663 – 1914252Peptidase C16 2PROSITE-ProRule annotationAdd
BLAST
Domaini2966 – 3267302Peptidase C30PROSITE-ProRule annotationAdd
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.

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 fingeri1126 – 115732C4-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1780 – 181536C4-type 2; atypicalPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri4007 – 402317By similarityAdd
BLAST
Zinc fingeri4049 – 406214By 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.

« Hide

        10         20         30         40         50
MACNRVTLAV ASDSEISANG CSTIAQAVRR YSEAASNGFR ACRFVSLDLQ
60 70 80 90 100
DCIVGIADDT YVMGLHGNQT LFCNIMKFSD RPFMLHGWLV FSNSNYLLEE
110 120 130 140 150
FDVVFGKRGG GNVTYTDQYL CGADGKPVMS EDLWQFVDHF GENEEIIING
160 170 180 190 200
HTYVCAWLTK RKPLDYKRQN NLAIEEIEYV HGDALHTLRN GSVLEMAKEV
210 220 230 240 250
KTSSKVVLSD ALDKLYKVFG SPVMTNGSNI LEAFTKPVFI SALVQCTCGT
260 270 280 290 300
KSWSVGDWTG FKSSCCNVIS NKLCVVPGNV KPGDAVITTQ QAGAGIKYFC
310 320 330 340 350
GMTLKFVANI EGVSVWRVIA LQSVDCFVAS STFVEEEHVN RMDTFCFNVR
360 370 380 390 400
NSVTDECRLA MLGAEMTSNV RRQVASGVID ISTGWFDVYD DIFAESKPWF
410 420 430 440 450
VRKAEDIFGP CWSALASALK QLKVTTGELV RFVKSICNSA VAVVGGTIQI
460 470 480 490 500
LASVPEKFLN AFDVFVTAIQ TVFDCAVETC TIAGKAFDKV FDYVLLDNAL
510 520 530 540 550
VKLVTTKLKG VRERGLNKVK YATVVVGSTE EVKSSRVERS TAVLTIANNY
560 570 580 590 600
SKLFDEGYTV VIGDVAYFVS DGYFRLMASP NSVLTTAVYK PLFAFNVNVM
610 620 630 640 650
GTRPEKFPTT VTCENLESAV LFVNDKITEF QLDYSIDVID NEIIVKPNIS
660 670 680 690 700
LCVPLYVRDY VDKWDDFCRQ YSNESWFEDD YRAFISVLDI TDAAVKAAES
710 720 730 740 750
KAFVDTIVPP CPSILKVIDG GKIWNGVIKN VNSVRDWLKS LKLNLTQQGL
760 770 780 790 800
LGTCAKRFKR WLGILLEAYN AFLDTVVSTV KIGGLTFKTY AFDKPYIVIR
810 820 830 840 850
DIVCKVENKT EAEWIELFPH NDRIKSFSTF ESAYMPIADP THFDIEEVEL
860 870 880 890 900
LDAEFVEPGC GGILAVIDEH VFYKKDGVYY PSNGTNILPV AFTKAAGGKV
910 920 930 940 950
SFSDDVEVKD IEPVYRVKLC FEFEDEKLVD VCEKAIGKKI KHEGDWDSFC
960 970 980 990 1000
KTIQSALSVV SCYVNLPTYY IYDEEGGNDL SLPVMISEWP LSVQQAQQEA
1010 1020 1030 1040 1050
TLPDIAEDVV DQVEEVNSIF DIETVDVKHD VSPFEMPFEE LNGLKILKQL
1060 1070 1080 1090 1100
DNNCWVNSVM LQIQLTGILD GDYAMQFFKM GRVAKMIERC YTAEQCIRGA
1110 1120 1130 1140 1150
MGDVGLCMYR LLKDLHTGFM VMDYKCSCTS GRLEESGAVL FCTPTKKAFP
1160 1170 1180 1190 1200
YGTCLNCNAP RMCTIRQLQG TIIFVQQKPE PVNPVSFVVK PVCSSIFRGA
1210 1220 1230 1240 1250
VSCGHYQTNI YSQNLCVDGF GVNKIQPWTN DALNTICIKD ADYNAKVEIS
1260 1270 1280 1290 1300
VTPIKNTVDT TPKEEFVVKE KLNAFLVHDN VAFYQGDVDT VVNGVDFDFI
1310 1320 1330 1340 1350
VNAANENLAH GGGLAKALDV YTKGKLQRLS KEHIGLAGKV KVGTGVMVEC
1360 1370 1380 1390 1400
DSLRIFNVVG PRKGKHERDL LIKAYNTINN EQGTPLTPIL SCGIFGIKLE
1410 1420 1430 1440 1450
TSLEVLLDVC NTKEVKVFVY TDTEVCKVKD FVSGLVNVQK VEQPKIEPKP
1460 1470 1480 1490 1500
VSVIKVAPKP YRVDGKFSYF TEDLLCVADD KPIVLFTDSM LTLDDRGLAL
1510 1520 1530 1540 1550
DNALSGVLSA AIKDCVDINK AIPSGNLIKF DIGSVVVYMC VVPSEKDKHL
1560 1570 1580 1590 1600
DNNVQRCTRK LNRLMCDIVC TIPADYILPL VLSSLTCNVS FVGELKAAEA
1610 1620 1630 1640 1650
KVITIKVTED GVNVHDVTVT TDKSFEQQVG VIADKDKDLS GAVPSDLNTS
1660 1670 1680 1690 1700
ELLTKAIDVD WVEFYGFKDA VTFATVDHSA FAYESAVVNG IRVLKTSDNN
1710 1720 1730 1740 1750
CWVNAVCIAL QYSKPHFISQ GLDAAWNKFV LGDVEIFVAF VYYVARLMKG
1760 1770 1780 1790 1800
DKGDAEDTLT KLSKYLANEA QVQLEHYSSC VECDAKFKNS VASINSAIVC
1810 1820 1830 1840 1850
ASVKRDGVQV GYCVHGIKYY SRVRSVRGRA IIVSVEQLEP CAQSRLLSGV
1860 1870 1880 1890 1900
AYTAFSGPVD KGHYTVYDTA KKSMYDGDRF VKHDLSLLSV TSVVMVGGYV
1910 1920 1930 1940 1950
APVNTVKPKP VINQLDEKAQ KFFDFGDFLI HNFVIFFTWL LSMFTLCKTA
1960 1970 1980 1990 2000
VTTGDVKIMA KAPQRTGVVL KRSLKYNLKA SAAVLKSKWW LLAKFTKLLL
2010 2020 2030 2040 2050
LIYTLYSVVL LCVRFGPFNF CSETVNGYAK SNFVKDDYCD GSLGCKMCLF
2060 2070 2080 2090 2100
GYQELSQFSH LDVVWKHITD PLFSNMQPFI VMVLLLIFGD NYLRCFLLYF
2110 2120 2130 2140 2150
VAQMISTVGV FLGYKETNWF LHFIPFDVIC DELLVTVIVI KVISFVRHVL
2160 2170 2180 2190 2200
FGCENPDCIA CSKSARLKRF PVNTIVNGVQ RSFYVNANGG SKFCKKHRFF
2210 2220 2230 2240 2250
CVDCDSYGYG STFITPEVSR ELGNITKTNV QPTGPAYVMI DKVEFENGFY
2260 2270 2280 2290 2300
RLYSCETFWR YNFDITESKY SCKEVFKNCN VLDDFIVFNN NGTNVTQVKN
2310 2320 2330 2340 2350
ASVYFSQLLC RPIKLVDSEL LSTLSVDFNG VLHKAYIDVL RNSFGKDLNA
2360 2370 2380 2390 2400
NMSLAECKRA LGLSISDHEF TSAISNAHRC DVLLSDLSFN NFVSSYAKPE
2410 2420 2430 2440 2450
EKLSAYDLAC CMRAGAKVVN ANVLTKDQTP IVWHAKDFNS LSAEGRKYIV
2460 2470 2480 2490 2500
KTSKAKGLTF LLTINENQAV TQIPATSIVA KQGAGDAGHS LTWLWLLCGL
2510 2520 2530 2540 2550
VCLIQFYLCF FMPYFMYDIV SSFEGYDFKY IENGQLKNFE APLKCVRNVF
2560 2570 2580 2590 2600
ENFEDWHYAK FGFTPLNKQS CPIVVGVSEI VNTVAGIPSN VYLVGKTLIF
2610 2620 2630 2640 2650
TLQAAFGNAG VCYDIFGVTT PEKCIFTSAC TRLEGLGGNN VYCYNTALME
2660 2670 2680 2690 2700
GSLPYSSIQA NAYYKYDNGN FIKLPEVIAQ GFGFRTVRTI ATKYCRVGEC
2710 2720 2730 2740 2750
VESNAGVCFG FDKWFVNDGR VANGYVCGTG LWNLVFNILS MFSSSFSVAA
2760 2770 2780 2790 2800
MSGQILLNCA LGAFAIFCCF LVTKFRRMFG DLSVGVCTVV VAVLLNNVSY
2810 2820 2830 2840 2850
IVTQNLVTMI AYAILYFFAT RSLRYAWIWC AAYLIAYISF APWWLCAWYF
2860 2870 2880 2890 2900
LAMLTGLLPS LLKLKVSTNL FEGDKFVGTF ESAAAGTFVI DMRSYEKLAN
2910 2920 2930 2940 2950
SISPEKLKSY AASYNRYKYY SGNANEADYR CACYAYLAKA MLDFSRDHND
2960 2970 2980 2990 3000
ILYTPPTVSY GSTLQAGLRK MAQPSGFVEK CVVRVCYGNT VLNGLWLGDI
3010 3020 3030 3040 3050
VYCPRHVIAS NTTSAIDYDH EYSIMRLHNF SIISGTAFLG VVGATMHGVT
3060 3070 3080 3090 3100
LKIKVSQTNM HTPRHSFRTL KSGEGFNILA CYDGCAQGVF GVNMRTNWTI
3110 3120 3130 3140 3150
RGSFINGACG SPGYNLKNGE VEFVYMHQIE LGSGSHVGSS FDGVMYGGFE
3160 3170 3180 3190 3200
DQPNLQVESA NQMLTVNVVA FLYAAILNGC TWWLKGEKLF VEHYNEWAQA
3210 3220 3230 3240 3250
NGFTAMNGED AFSILAAKTG VCVERLLHAI QVLNNGFGGK QILGYSSLND
3260 3270 3280 3290 3300
EFSINEVVKQ MFGVNLQSGK TTSMFKSISL FAGFFVMFWA ELFVYTTTIW
3310 3320 3330 3340 3350
VNPGFLTPFM ILLVALSLCL TFVVKHKVLF LQVFLLPSII VAAIQNCAWD
3360 3370 3380 3390 3400
YHVTKVLAEK FDYNVSVMQM DIQGFVNIFI CLFVALLHTW RFAKERCTHW
3410 3420 3430 3440 3450
CTYLFSLIAV LYTALYSYDY VSLLVMLLCA ISNEWYIGAI IFRICRFGVA
3460 3470 3480 3490 3500
FLPVEYVSYF DGVKTVLLFY MLLGFVSCMY YGLLYWINRF CKCTLGVYDF
3510 3520 3530 3540 3550
CVSPAEFKYM VANGLNAPNG PFDALFLSFK LMGIGGPRTI KVSTVQSKLT
3560 3570 3580 3590 3600
DLKCTNVVLM GILSNMNIAS NSKEWAYCVE MHNKINLCDD PETAQELLLA
3610 3620 3630 3640 3650
LLAFFLSKHS DFGLGDLVDS YFENDSILQS VASSFVGMPS FVAYETARQE
3660 3670 3680 3690 3700
YENAVANGSS PQIIKQLKKA MNVAKAEFDR ESSVQKKINR MAEQAAAAMY
3710 3720 3730 3740 3750
KEARAVNRKS KVVSAMHSLL FGMLRRLDMS SVDTILNMAR NGVVPLSVIP
3760 3770 3780 3790 3800
ATSAARLVVV VPDHDSFVKM MVDGFVHYAG VVWTLQEVKD NDGKNVHLKD
3810 3820 3830 3840 3850
VTKENQEILV WPLILTCERV VKLQNNEIMP GKMKVKATKG EGDGGITSEG
3860 3870 3880 3890 3900
NALYNNEGGR AFMYAYVTTK PGMKYVKWEH DSGVVTVELE PPCRFVIDTP
3910 3920 3930 3940 3950
TGPQIKYLYF VKNLNNLRRG AVLGYIGATV RLQAGKQTEF VSNSHLLTHC
3960 3970 3980 3990 4000
SFAVDPAAAY LDAVKQGAKP VGNCVKMLTN GSGSGQAITC TIDSNTTQDT
4010 4020 4030 4040 4050
YGGASVCIYC RAHVAHPTMD GFCQYKGKWV QVPIGTNDPI RFCLENTVCK
4060 4070 4080
VCGCWLNHGC TCDRTAIQSF DNSYLNESGA LVPLD

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1982 – 19821A → Q(PubMed:11369870)Curated
Sequence conflicti4042 – 40421F → S(PubMed:11369870)Curated

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: October 29, 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, 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