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Protein

Replicase polyprotein 1a

Gene

1a

Organism
Human coronavirus 229E (HCoV-229E)
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 (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)DescriptionActionsGraphical viewLength
Active sitei1054For PL1-PRO activityPROSITE-ProRule annotation1
Active sitei1205For PL1-PRO activityPROSITE-ProRule annotation1
Active sitei1701For PL2-PRO activityPROSITE-ProRule annotation1
Active sitei1863For PL2-PRO activityPROSITE-ProRule annotation1
Active sitei3006For 3CL-PRO activity1
Active sitei3109For 3CL-PRO activity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1126 – 1157C4-type 1PROSITE-ProRule annotationAdd BLAST32
Zinc fingeri1780 – 1815C4-type 2; atypicalPROSITE-ProRule annotationAdd BLAST36
Zinc fingeri4007 – 4023By similarityAdd BLAST17
Zinc fingeri4049 – 4062By 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
p16
Non-structural protein 11
Short name:
nsp11
Gene namesi
ORF Names:1a
OrganismiHuman coronavirus 229E (HCoV-229E)
Taxonomic identifieri11137 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeAlphacoronavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000006716 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
Transmembranei1998 – 2018HelicalSequence analysisAdd BLAST21
Transmembranei2068 – 2088HelicalSequence analysisAdd BLAST21
Transmembranei2095 – 2115HelicalSequence analysisAdd BLAST21
Transmembranei2491 – 2511HelicalSequence analysisAdd BLAST21
Transmembranei2731 – 2751HelicalSequence analysisAdd BLAST21
Transmembranei2755 – 2775HelicalSequence analysisAdd BLAST21
Transmembranei2782 – 2802HelicalSequence analysisAdd BLAST21
Transmembranei2809 – 2829HelicalSequence analysisAdd BLAST21
Transmembranei2834 – 2854HelicalSequence analysisAdd BLAST21
Transmembranei3281 – 3301HelicalSequence analysisAdd BLAST21
Transmembranei3304 – 3324HelicalSequence analysisAdd BLAST21
Transmembranei3328 – 3348HelicalSequence analysisAdd BLAST21
Transmembranei3367 – 3387HelicalSequence analysisAdd BLAST21
Transmembranei3401 – 3421HelicalSequence analysisAdd BLAST21
Transmembranei3422 – 3442HelicalSequence analysisAdd BLAST21
Transmembranei3467 – 3487HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1048K → E: Complete loss of PL1-PRO activity. 1 Publication1
Mutagenesisi1054C → A, G or S: Complete loss of PL1-PRO activity. 1 Publication1
Mutagenesisi1099G → A: Complete loss of PL1-PRO activity. 1 Publication1
Mutagenesisi1099G → P: No effect. 1 Publication1
Mutagenesisi1102G → A or S: No effect. 1 Publication1
Mutagenesisi1126C → D or H: Complete loss of PL1-PRO activity. 1 Publication1
Mutagenesisi1128C → A, D or P: Complete loss of PL1-PRO activity. 1 Publication1
Mutagenesisi1154C → A, H or D: Complete loss of PL1-PRO activity. 1 Publication1
Mutagenesisi1155Missing : Complete loss of PL1-PRO activity. 1 Publication1
Mutagenesisi1157C → A, D, H or P: Complete loss of PL1-PRO activity. 1 Publication1
Mutagenesisi1163C → A or D: No effect. 1 Publication1
Mutagenesisi1175V → H or P: Complete loss of PL1-PRO activity. 1 Publication1
Mutagenesisi1175V → N or T: No effect. 1 Publication1
Mutagenesisi1203C → A: Complete loss of PL1-PRO activity. 1 Publication1
Mutagenesisi1203C → D: No effect. 1 Publication1
Mutagenesisi1218D → A, E, H, K, N or Q: No effect. 1 Publication1
Mutagenesisi1702W → L: Complete loss of PL2-PRO activity. 1 Publication1
Mutagenesisi3006H → G, S, T or Y: Complete loss of 3CL-PRO activity. 1 Publication1
Mutagenesisi3028H → G or T: No loss of 3CL-PRO activity. 1 Publication1
Mutagenesisi3029N → A, D, E or Q: Increase of 3CL-PRO activity. 2 Publications1
Mutagenesisi3029N → G: No loss of 3CL-PRO activity. 2 Publications1
Mutagenesisi3029N → P: 95% loss of 3CL-PRO activity. 2 Publications1
Mutagenesisi3074E → H: No loss of 3CL-PRO activity. 1 Publication1
Mutagenesisi3099T → D: Complete loss of 3CL-PRO activity. 1 Publication1
Mutagenesisi3109C → P, S or V: Complete loss of 3CL-PRO activity. 1 Publication1
Mutagenesisi3127H → S: Complete loss of 3CL-PRO activity. 1 Publication1
Mutagenesisi3136H → A: 67% loss of 3CL-PRO activity. 1 Publication1
Mutagenesisi3136H → S: 77% loss of 3CL-PRO activity. 1 Publication1
Mutagenesisi3136H → T: 93% loss of 3CL-PRO activity. 1 Publication1
Mutagenesisi3267Q → A: No loss of 3CL-PRO activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003381821 – 4085Replicase polyprotein 1aAdd BLAST4085
ChainiPRO_00003381831 – 111Non-structural protein 1Add BLAST111
ChainiPRO_0000338184112 – 897Non-structural protein 2Add BLAST786
ChainiPRO_0000338185898 – 2484Non-structural protein 3Add BLAST1587
ChainiPRO_00003381862485 – 2965Non-structural protein 4Add BLAST481
ChainiPRO_00003381872966 – 32673C-like proteinaseAdd BLAST302
ChainiPRO_00003381883268 – 3546Non-structural protein 6Add BLAST279
ChainiPRO_00003381893547 – 3629Non-structural protein 7Add BLAST83
ChainiPRO_00003381903630 – 3824Non-structural protein 8Add BLAST195
ChainiPRO_00003381913825 – 3933Non-structural protein 9Add BLAST109
ChainiPRO_00003381923934 – 4068Non-structural protein 10Add BLAST135
ChainiPRO_00003381934069 – 4085Non-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.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei111 – 112Cleavage; by PL1-PRO2
Sitei897 – 898Cleavage; by PL1-PRO2
Sitei2484 – 2485Cleavage; by PL2-PRO2
Sitei2965 – 2966Cleavage; by 3CL-PRO2
Sitei3267 – 3268Cleavage; by 3CL-PRO2
Sitei3546 – 3547Cleavage; by 3CL-PRO2
Sitei3629 – 3630Cleavage; by 3CL-PRO2
Sitei3824 – 3825Cleavage; by 3CL-PRO2
Sitei3933 – 3934Cleavage; by 3CL-PRO2
Sitei4068 – 4069Cleavage; by 3CL-PRO2

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

14085
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1275 – 1278Combined sources4
Beta strandi1281 – 1285Combined sources5
Helixi1288 – 1294Combined sources7
Beta strandi1298 – 1304Combined sources7
Helixi1313 – 1321Combined sources9
Turni1322 – 1324Combined sources3
Helixi1325 – 1333Combined sources9
Beta strandi1345 – 1350Combined sources6
Beta strandi1353 – 1359Combined sources7
Helixi1367 – 1380Combined sources14
Beta strandi1381 – 1383Combined sources3
Beta strandi1385 – 1387Combined sources3
Helixi1399 – 1409Combined sources11
Beta strandi1415 – 1419Combined sources5
Helixi1422 – 1433Combined sources12
Helixi2976 – 2979Combined sources4
Beta strandi2982 – 2987Combined sources6
Beta strandi2990 – 2997Combined sources8
Beta strandi3000 – 3004Combined sources5
Helixi3005 – 3008Combined sources4
Helixi3018 – 3024Combined sources7
Helixi3027 – 3029Combined sources3
Beta strandi3030 – 3034Combined sources5
Beta strandi3037 – 3039Combined sources3
Beta strandi3041 – 3047Combined sources7
Beta strandi3050 – 3057Combined sources8
Beta strandi3064 – 3067Combined sources4
Beta strandi3075 – 3093Combined sources19
Beta strandi3112 – 3117Combined sources6
Beta strandi3120 – 3130Combined sources11
Beta strandi3136 – 3139Combined sources4
Helixi3146 – 3148Combined sources3
Beta strandi3151 – 3154Combined sources4
Helixi3165 – 3177Combined sources13
Helixi3191 – 3199Combined sources9
Turni3200 – 3202Combined sources3
Helixi3209 – 3212Combined sources4
Helixi3213 – 3219Combined sources7
Helixi3223 – 3233Combined sources11
Beta strandi3245 – 3247Combined sources3
Helixi3254 – 3262Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P9SX-ray2.54A/B2966-3265[»]
2ZU2X-ray1.80A/B2966-3267[»]
3EWQX-ray2.10A1269-1436[»]
3EWRX-ray2.01A1269-1436[»]
ProteinModelPortaliP0C6U2.
SMRiP0C6U2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C6U2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1016 – 1268Peptidase C16 1PROSITE-ProRule annotationAdd BLAST253
Domaini1269 – 1436MacroPROSITE-ProRule annotationAdd BLAST168
Domaini1663 – 1914Peptidase C16 2PROSITE-ProRule annotationAdd BLAST252
Domaini2966 – 3267Peptidase C30PROSITE-ProRule annotationAdd BLAST302

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1925 – 2115HD1Add BLAST191
Regioni2491 – 2854HD2Add BLAST364
Regioni3281 – 3487HD3Add BLAST207

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 fingeri1126 – 1157C4-type 1PROSITE-ProRule annotationAdd BLAST32
Zinc fingeri1780 – 1815C4-type 2; atypicalPROSITE-ProRule annotationAdd BLAST36
Zinc fingeri4007 – 4023By similarityAdd BLAST17
Zinc fingeri4049 – 4062By 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: 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)DescriptionActionsGraphical viewLength
Sequence conflicti1982A → Q (PubMed:11369870).Curated1
Sequence conflicti4042F → S (PubMed:11369870).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF304460 Genomic RNA. Translation: AAG48590.1.
X69721 Genomic RNA. Translation: CAA49377.1.
PIRiS28600.
RefSeqiNP_073550.1. NC_002645.1. [P0C6U2-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P9SX-ray2.54A/B2966-3265[»]
2ZU2X-ray1.80A/B2966-3267[»]
3EWQX-ray2.10A1269-1436[»]
3EWRX-ray2.01A1269-1436[»]
ProteinModelPortaliP0C6U2.
SMRiP0C6U2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi918764.

Miscellaneous databases

EvolutionaryTraceiP0C6U2.

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_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: November 2, 2016
This is version 56 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

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.