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Protein

Replicase polyprotein 1a

Gene

1a

Organism
Human coronavirus EMC (isolate United Kingdom/H123990006/2012) (HCoV-EMC)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.By similarity
Host translation inhibitor nsp1: Promotes the degradation of host mRNAs by inducing an endonucleolytic RNA cleavage in template mRNAs, and inhibits of host mRNA translation, a function that is separable from its RNA cleavage activity. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.1 Publication
Non-structural protein 2: May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.By similarity
Papain-like proteinase: Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.By similarity1 Publication
Non-structural protein 4: Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.By similarity
Proteinase 3CL-PRO: Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).PROSITE-ProRule annotationBy similarity
Non-structural protein 6: Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.By similarity
Non-structural protein 7: Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.By similarity
Non-structural protein 8: Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.By similarity
Non-structural protein 9: May participate in viral replication by acting as a ssRNA-binding protein.By similarity
Non-structural protein 10: Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.
TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
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 sitei1592For PL-PRO activityPROSITE-ProRule annotation1
Active sitei1759For PL-PRO activityPROSITE-ProRule annotation1
Active sitei3288For 3CL-PRO activityPROSITE-ProRule annotation1
Active sitei3395For 3CL-PRO activityPROSITE-ProRule annotation1
Metal bindingi4311Zinc1
Metal bindingi4314Zinc1
Metal bindingi4320Zinc1
Metal bindingi4327Zinc1
Metal bindingi4354Zinc1
Metal bindingi4357Zinc1
Metal bindingi4365Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1672 – 1709C4-typePROSITE-ProRule annotationAdd BLAST38
Zinc fingeri4311 – 4327Add BLAST17
Zinc fingeri4354 – 4367Add 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, Decay of host mRNAs by virus, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host IRF3 by virus, Inhibition of host ISG15 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:
Alternative name(s):
Leader protein
Non-structural protein 2
Short name:
nsp2
Alternative name(s):
p65 homolog
Papain-like proteinase (EC:3.4.19.12, EC:3.4.22.69)
Short name:
PL-PRO
Alternative name(s):
Non-structural protein 3
Short name:
nsp3
Non-structural protein 4
Short name:
nsp4
3C-like proteinase (EC:3.4.22.-)
Short name:
3CL-PRO
Short name:
3CLp
Alternative name(s):
nsp5
Non-structural protein 6
Short name:
nsp6
Non-structural protein 7
Short name:
nsp7
Non-structural protein 8
Short name:
nsp8
Non-structural protein 9
Short name:
nsp9
Non-structural protein 10
Short name:
nsp10
Alternative name(s):
Growth factor-like peptide
Short name:
GFL
Non-structural protein 11
Short name:
nsp11
Gene namesi
ORF Names:1a
OrganismiHuman coronavirus EMC (isolate United Kingdom/H123990006/2012) (HCoV-EMC)
Taxonomic identifieri1263720 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirusunclassified Betacoronavirus

Subcellular locationi

Papain-like proteinase :
Non-structural protein 4 :
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
Transmembranei2105 – 2125HelicalSequence analysisAdd BLAST21
Transmembranei2177 – 2197HelicalSequence analysisAdd BLAST21
Transmembranei2281 – 2301HelicalSequence analysisAdd BLAST21
Transmembranei2305 – 2325HelicalSequence analysisAdd BLAST21
Transmembranei2330 – 2350HelicalSequence analysisAdd BLAST21
Transmembranei2757 – 2777HelicalSequence analysisAdd BLAST21
Transmembranei3028 – 3048HelicalSequence analysisAdd BLAST21
Transmembranei3062 – 3082HelicalSequence analysisAdd BLAST21
Transmembranei3104 – 3124HelicalSequence analysisAdd BLAST21
Transmembranei3125 – 3145HelicalSequence analysisAdd BLAST21
Transmembranei3559 – 3579HelicalSequence analysisAdd BLAST21
Transmembranei3593 – 3613HelicalSequence analysisAdd BLAST21
Transmembranei3618 – 3638HelicalSequence analysisAdd BLAST21
Transmembranei3664 – 3684HelicalSequence analysisAdd BLAST21
Transmembranei3691 – 3711HelicalSequence analysisAdd BLAST21
Transmembranei3740 – 3760HelicalSequence analysisAdd BLAST21
Transmembranei3765 – 3785HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004224541 – 193Host translation inhibitor nsp1By similarityAdd BLAST193
ChainiPRO_0000422455194 – 853Non-structural protein 2By similarityAdd BLAST660
ChainiPRO_0000422456854 – 2740Papain-like proteinaseBy similarityAdd BLAST1887
ChainiPRO_00004224572741 – 3247Non-structural protein 4Sequence analysisAdd BLAST507
ChainiPRO_00004224583248 – 35533C-like proteinaseBy similarityAdd BLAST306
ChainiPRO_00004224593554 – 3845Non-structural protein 6By similarityAdd BLAST292
ChainiPRO_00004224603846 – 3928Non-structural protein 7By similarityAdd BLAST83
ChainiPRO_00004224613929 – 4127Non-structural protein 8By similarityAdd BLAST199
ChainiPRO_00004224624128 – 4237Non-structural protein 9By similarityAdd BLAST110
ChainiPRO_00004224634238 – 4377Non-structural protein 10By similarityAdd BLAST140
ChainiPRO_00004224644378 – 4391Non-structural protein 11By similarityAdd BLAST14

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei193 – 194CleavageBy similarity2
Sitei853 – 854Cleavage; by PL-PROBy similarity2
Sitei2740 – 2741Cleavage; by PL-PROBy similarity2
Sitei3247 – 3248Cleavage; by 3CL-PROBy similarity2
Sitei3553 – 3554Cleavage; by 3CL-PROBy similarity2
Sitei3845 – 3846Cleavage; by 3CL-PROBy similarity2
Sitei3928 – 3929Cleavage; by 3CL-PROBy similarity2
Sitei4127 – 4128Cleavage; by 3CL-PROBy similarity2
Sitei4237 – 4238Cleavage; by 3CL-PROBy similarity2
Sitei4377 – 4378Cleavage; by 3CL-PROBy similarity2

Interactioni

Subunit structurei

Nsp2 interacts with host PHB and PHB2. 3CL-PRO exists as monomer and homodimer. Nsp4 interacts with PL-PRO and nsp6. Only the homodimer shows catalytic activity. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer dsRNA-encircling ring structure. Nsp9 is a dimer.By similarity

Structurei

Secondary structure

14391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1110 – 1113Combined sources4
Beta strandi1116 – 1118Combined sources3
Beta strandi1120 – 1128Combined sources9
Helixi1130 – 1134Combined sources5
Beta strandi1141 – 1146Combined sources6
Helixi1156 – 1163Combined sources8
Turni1164 – 1166Combined sources3
Helixi1167 – 1179Combined sources13
Beta strandi1187 – 1191Combined sources5
Beta strandi1195 – 1203Combined sources9
Helixi1207 – 1209Combined sources3
Helixi1213 – 1215Combined sources3
Helixi1216 – 1221Combined sources6
Helixi1222 – 1225Combined sources4
Beta strandi1226 – 1231Combined sources6
Helixi1243 – 1253Combined sources11
Beta strandi1256 – 1263Combined sources8
Helixi1265 – 1272Combined sources8
Beta strandi1484 – 1494Combined sources11
Beta strandi1496 – 1505Combined sources10
Helixi1507 – 1510Combined sources4
Beta strandi1513 – 1516Combined sources4
Helixi1528 – 1530Combined sources3
Beta strandi1534 – 1537Combined sources4
Helixi1543 – 1553Combined sources11
Helixi1560 – 1570Combined sources11
Turni1571 – 1573Combined sources3
Beta strandi1576 – 1579Combined sources4
Beta strandi1582 – 1585Combined sources4
Turni1589 – 1591Combined sources3
Helixi1592 – 1603Combined sources12
Beta strandi1607 – 1611Combined sources5
Helixi1612 – 1622Combined sources11
Helixi1627 – 1636Combined sources10
Helixi1647 – 1655Combined sources9
Beta strandi1658 – 1662Combined sources5
Beta strandi1665 – 1672Combined sources8
Turni1673 – 1675Combined sources3
Beta strandi1676 – 1683Combined sources8
Helixi1684 – 1687Combined sources4
Beta strandi1689 – 1692Combined sources4
Helixi1696 – 1699Combined sources4
Beta strandi1703 – 1706Combined sources4
Beta strandi1710 – 1740Combined sources31
Beta strandi1745 – 1751Combined sources7
Beta strandi1759 – 1766Combined sources8
Beta strandi1769 – 1773Combined sources5
Beta strandi1780 – 1799Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3DX-ray2.82A/B1481-1811[»]
5DUSX-ray1.43A1110-1273[»]
5HIHX-ray1.66A1109-1275[»]
SMRiK9N638.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1110 – 1276MacroPROSITE-ProRule annotationAdd BLAST167
Domaini1552 – 1823Peptidase C16PROSITE-ProRule annotationAdd BLAST272
Domaini3248 – 3553Peptidase C30PROSITE-ProRule annotationAdd BLAST306

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2040 – 2363HD1Add BLAST324
Regioni2761 – 3171HD2Add BLAST411
Regioni3571 – 3785HD3Add BLAST215

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 1 peptidase C16 domain.PROSITE-ProRule annotation
Contains 1 peptidase C30 domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1672 – 1709C4-typePROSITE-ProRule annotationAdd BLAST38
Zinc fingeri4311 – 4327Add BLAST17
Zinc fingeri4354 – 4367Add BLAST14

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

InterProiIPR032505. Corona_NSP4_C.
IPR002589. Macro_dom.
IPR032592. NAR_dom.
IPR024375. Nsp3_coronavir.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
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.
PF16251. NAR. 1 hit.
PF09401. NSP10. 1 hit.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF11633. SUD-M. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
SUPFAMiSSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
PROSITEiPS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 1 hit.
[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: K9N638-1) [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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        10         20         30         40         50
MSFVAGVTAQ GARGTYRAAL NSEKHQDHVS LTVPLCGSGN LVEKLSPWFM
60 70 80 90 100
DGENAYEVVK AMLLKKEPLL YVPIRLAGHT RHLPGPRVYL VERLIACENP
110 120 130 140 150
FMVNQLAYSS SANGSLVGTT LQGKPIGMFF PYDIELVTGK QNILLRKYGR
160 170 180 190 200
GGYHYTPFHY ERDNTSCPEW MDDFEADPKG KYAQNLLKKL IGGDVTPVDQ
210 220 230 240 250
YMCGVDGKPI SAYAFLMAKD GITKLADVEA DVAARADDEG FITLKNNLYR
260 270 280 290 300
LVWHVERKDV PYPKQSIFTI NSVVQKDGVE NTPPHYFTLG CKILTLTPRN
310 320 330 340 350
KWSGVSDLSL KQKLLYTFYG KESLENPTYI YHSAFIECGS CGNDSWLTGN
360 370 380 390 400
AIQGFACGCG ASYTANDVEV QSSGMIKPNA LLCATCPFAK GDSCSSNCKH
410 420 430 440 450
SVAQLVSYLS ERCNVIADSK SFTLIFGGVA YAYFGCEEGT MYFVPRAKSV
460 470 480 490 500
VSRIGDSIFT GCTGSWNKVT QIANMFLEQT QHSLNFVGEF VVNDVVLAIL
510 520 530 540 550
SGTTTNVDKI RQLLKGVTLD KLRDYLADYD VAVTAGPFMD NAINVGGTGL
560 570 580 590 600
QYAAITAPYV VLTGLGESFK KVATIPYKVC NSVKDTLTYY AHSVLYRVFP
610 620 630 640 650
YDMDSGVSSF SELLFDCVDL SVASTYFLVR LLQDKTGDFM STIITSCQTA
660 670 680 690 700
VSKLLDTCFE ATEATFNFLL DLAGLFRIFL RNAYVYTSQG FVVVNGKVST
710 720 730 740 750
LVKQVLDLLN KGMQLLHTKV SWAGSNISAV IYSGRESLIF PSGTYYCVTT
760 770 780 790 800
KAKSVQQDLD VILPGEFSKK QLGLLQPTDN STTVSVTVSS NMVETVVGQL
810 820 830 840 850
EQTNMHSPDV IVGDYVIISE KLFVRSKEED GFAFYPACTN GHAVPTLFRL
860 870 880 890 900
KGGAPVKKVA FGGDQVHEVA AVRSVTVEYN IHAVLDTLLA SSSLRTFVVD
910 920 930 940 950
KSLSIEEFAD VVKEQVSDLL VKLLRGMPIP DFDLDDFIDA PCYCFNAEGD
960 970 980 990 1000
ASWSSTMIFS LHPVECDEEC SEVEASDLEE GESECISETS TEQVDVSHEI
1010 1020 1030 1040 1050
SDDEWAAAVD EAFPLDEAED VTESVQEEAQ PVEVPVEDIA QVVIADTLQE
1060 1070 1080 1090 1100
TPVVSDTVEV PPQVVKLPSE PQTIQPEVKE VAPVYEADTE QTQSVTVKPK
1110 1120 1130 1140 1150
RLRKKRNVDP LSNFEHKVIT ECVTIVLGDA IQVAKCYGES VLVNAANTHL
1160 1170 1180 1190 1200
KHGGGIAGAI NAASKGAVQK ESDEYILAKG PLQVGDSVLL QGHSLAKNIL
1210 1220 1230 1240 1250
HVVGPDARAK QDVSLLSKCY KAMNAYPLVV TPLVSAGIFG VKPAVSFDYL
1260 1270 1280 1290 1300
IREAKTRVLV VVNSQDVYKS LTIVDIPQSL TFSYDGLRGA IRKAKDYGFT
1310 1320 1330 1340 1350
VFVCTDNSAN TKVLRNKGVD YTKKFLTVDG VQYYCYTSKD TLDDILQQAN
1360 1370 1380 1390 1400
KSVGIISMPL GYVSHGLDLI QAGSVVRRVN VPYVCLLANK EQEAILMSED
1410 1420 1430 1440 1450
VKLNPSEDFI KHVRTNGGYN SWHLVEGELL VQDLRLNKLL HWSDQTICYK
1460 1470 1480 1490 1500
DSVFYVVKNS TAFPFETLSA CRAYLDSRTT QQLTIEVLVT VDGVNFRTVV
1510 1520 1530 1540 1550
LNNKNTYRSQ LGCVFFNGAD ISDTIPDEKQ NGHSLYLADN LTADETKALK
1560 1570 1580 1590 1600
ELYGPVDPTF LHRFYSLKAA VHKWKMVVCD KVRSLKLSDN NCYLNAVIMT
1610 1620 1630 1640 1650
LDLLKDIKFV IPALQHAFMK HKGGDSTDFI ALIMAYGNCT FGAPDDASRL
1660 1670 1680 1690 1700
LHTVLAKAEL CCSARMVWRE WCNVCGIKDV VLQGLKACCY VGVQTVEDLR
1710 1720 1730 1740 1750
ARMTYVCQCG GERHRQIVEH TTPWLLLSGT PNEKLVTTST APDFVAFNVF
1760 1770 1780 1790 1800
QGIETAVGHY VHARLKGGLI LKFDSGTVSK TSDWKCKVTD VLFPGQKYSS
1810 1820 1830 1840 1850
DCNVVRYSLD GNFRTEVDPD LSAFYVKDGK YFTSEPPVTY SPATILAGSV
1860 1870 1880 1890 1900
YTNSCLVSSD GQPGGDAISL SFNNLLGFDS SKPVTKKYTY SFLPKEDGDV
1910 1920 1930 1940 1950
LLAEFDTYDP IYKNGAMYKG KPILWVNKAS YDTNLNKFNR ASLRQIFDVA
1960 1970 1980 1990 2000
PIELENKFTP LSVESTPVEP PTVDVVALQQ EMTIVKCKGL NKPFVKDNVS
2010 2020 2030 2040 2050
FVADDSGTPV VEYLSKEDLH TLYVDPKYQV IVLKDNVLSS MLRLHTVESG
2060 2070 2080 2090 2100
DINVVAASGS LTRKVKLLFR ASFYFKEFAT RTFTATTAVG SCIKSVVRHL
2110 2120 2130 2140 2150
GVTKGILTGC FSFVKMLFML PLAYFSDSKL GTTEVKVSAL KTAGVVTGNV
2160 2170 2180 2190 2200
VKQCCTAAVD LSMDKLRRVD WKSTLRLLLM LCTTMVLLSS VYHLYVFNQV
2210 2220 2230 2240 2250
LSSDVMFEDA QGLKKFYKEV RAYLGISSAC DGLASAYRAN SFDVPTFCAN
2260 2270 2280 2290 2300
RSAMCNWCLI SQDSITHYPA LKMVQTHLSH YVLNIDWLWF AFETGLAYML
2310 2320 2330 2340 2350
YTSAFNWLLL AGTLHYFFAQ TSIFVDWRSY NYAVSSAFWL FTHIPMAGLV
2360 2370 2380 2390 2400
RMYNLLACLW LLRKFYQHVI NGCKDTACLL CYKRNRLTRV EASTVVCGGK
2410 2420 2430 2440 2450
RTFYITANGG ISFCRRHNWN CVDCDTAGVG NTFICEEVAN DLTTALRRPI
2460 2470 2480 2490 2500
NATDRSHYYV DSVTVKETVV QFNYRRDGQP FYERFPLCAF TNLDKLKFKE
2510 2520 2530 2540 2550
VCKTTTGIPE YNFIIYDSSD RGQESLARSA CVYYSQVLCK SILLVDSSLV
2560 2570 2580 2590 2600
TSVGDSSEIA TKMFDSFVNS FVSLYNVTRD KLEKLISTAR DGVRRGDNFH
2610 2620 2630 2640 2650
SVLTTFIDAA RGPAGVESDV ETNEIVDSVQ YAHKHDIQIT NESYNNYVPS
2660 2670 2680 2690 2700
YVKPDSVSTS DLGSLIDCNA ASVNQIVLRN SNGACIWNAA AYMKLSDALK
2710 2720 2730 2740 2750
RQIRIACRKC NLAFRLTTSK LRANDNILSV RFTANKIVGG APTWFNALRD
2760 2770 2780 2790 2800
FTLKGYVLAT IIVFLCAVLM YLCLPTFSMV PVEFYEDRIL DFKVLDNGII
2810 2820 2830 2840 2850
RDVNPDDKCF ANKHRSFTQW YHEHVGGVYD NSITCPLTVA VIAGVAGARI
2860 2870 2880 2890 2900
PDVPTTLAWV NNQIIFFVSR VFANTGSVCY TPIDEIPYKS FSDSGCILPS
2910 2920 2930 2940 2950
ECTMFRDAEG RMTPYCHDPT VLPGAFAYSQ MRPHVRYDLY DGNMFIKFPE
2960 2970 2980 2990 3000
VVFESTLRIT RTLSTQYCRF GSCEYAQEGV CITTNGSWAI FNDHHLNRPG
3010 3020 3030 3040 3050
VYCGSDFIDI VRRLAVSLFQ PITYFQLTTS LVLGIGLCAF LTLLFYYINK
3060 3070 3080 3090 3100
VKRAFADYTQ CAVIAVVAAV LNSLCICFVA SIPLCIVPYT ALYYYATFYF
3110 3120 3130 3140 3150
TNEPAFIMHV SWYIMFGPIV PIWMTCVYTV AMCFRHFFWV LAYFSKKHVE
3160 3170 3180 3190 3200
VFTDGKLNCS FQDAASNIFV INKDTYAALR NSLTNDAYSR FLGLFNKYKY
3210 3220 3230 3240 3250
FSGAMETAAY REAAACHLAK ALQTYSETGS DLLYQPPNCS ITSGVLQSGL
3260 3270 3280 3290 3300
VKMSHPSGDV EACMVQVTCG SMTLNGLWLD NTVWCPRHVM CPADQLSDPN
3310 3320 3330 3340 3350
YDALLISMTN HSFSVQKHIG APANLRVVGH AMQGTLLKLT VDVANPSTPA
3360 3370 3380 3390 3400
YTFTTVKPGA AFSVLACYNG RPTGTFTVVM RPNYTIKGSF LCGSCGSVGY
3410 3420 3430 3440 3450
TKEGSVINFC YMHQMELANG THTGSAFDGT MYGAFMDKQV HQVQLTDKYC
3460 3470 3480 3490 3500
SVNVVAWLYA AILNGCAWFV KPNRTSVVSF NEWALANQFT EFVGTQSVDM
3510 3520 3530 3540 3550
LAVKTGVAIE QLLYAIQQLY TGFQGKQILG STMLEDEFTP EDVNMQIMGV
3560 3570 3580 3590 3600
VMQSGVRKVT YGTAHWLFAT LVSTYVIILQ ATKFTLWNYL FETIPTQLFP
3610 3620 3630 3640 3650
LLFVTMAFVM LLVKHKHTFL TLFLLPVAIC LTYANIVYEP TTPISSALIA
3660 3670 3680 3690 3700
VANWLAPTNA YMRTTHTDIG VYISMSLVLV IVVKRLYNPS LSNFALALCS
3710 3720 3730 3740 3750
GVMWLYTYSI GEASSPIAYL VFVTTLTSDY TITVFVTVNL AKVCTYAIFA
3760 3770 3780 3790 3800
YSPQLTLVFP EVKMILLLYT CLGFMCTCYF GVFSLLNLKL RAPMGVYDFK
3810 3820 3830 3840 3850
VSTQEFRFMT ANNLTAPRNS WEAMALNFKL IGIGGTPCIK VAAMQSKLTD
3860 3870 3880 3890 3900
LKCTSVVLLS VLQQLHLEAN SRAWAFCVKC HNDILAATDP SEAFEKFVSL
3910 3920 3930 3940 3950
FATLMTFSGN VDLDALASDI FDTPSVLQAT LSEFSHLATF AELEAAQKAY
3960 3970 3980 3990 4000
QEAMDSGDTS PQVLKALQKA VNIAKNAYEK DKAVARKLER MADQAMTSMY
4010 4020 4030 4040 4050
KQARAEDKKA KIVSAMQTML FGMIKKLDND VLNGIISNAR NGCIPLSVIP
4060 4070 4080 4090 4100
LCASNKLRVV IPDFTVWNQV VTYPSLNYAG ALWDITVINN VDNEIVKSSD
4110 4120 4130 4140 4150
VVDSNENLTW PLVLECTRAS TSAVKLQNNE IKPSGLKTMV VSAGQEQTNC
4160 4170 4180 4190 4200
NTSSLAYYEP VQGRKMLMAL LSDNAYLKWA RVEGKDGFVS VELQPPCKFL
4210 4220 4230 4240 4250
IAGPKGPEIR YLYFVKNLNN LHRGQVLGHI AATVRLQAGS NTEFASNSSV
4260 4270 4280 4290 4300
LSLVNFTVDP QKAYLDFVNA GGAPLTNCVK MLTPKTGTGI AISVKPESTA
4310 4320 4330 4340 4350
DQETYGGASV CLYCRAHIEH PDVSGVCKYK GKFVQIPAQC VRDPVGFCLS
4360 4370 4380 4390
NTPCNVCQYW IGYGCNCDSL RQAALPQSKD SNFLNESGVL L
Note: Produced by conventional translation.
Length:4,391
Mass (Da):486,059
Last modified:March 6, 2013 - v1
Checksum:iD0A87AE59773BBB8
GO
Isoform Replicase polyprotein 1ab (identifier: K9N7C7-1) [UniParc]FASTAAdd to basket
Also known as: pp1ab
The sequence of this isoform can be found in the external entry K9N7C7.
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:7,078
Mass (Da):789,563
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KC164505 Genomic RNA. Translation: AFY13305.1.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
KC164505 Genomic RNA. Translation: AFY13305.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3DX-ray2.82A/B1481-1811[»]
5DUSX-ray1.43A1110-1273[»]
5HIHX-ray1.66A1109-1275[»]
SMRiK9N638.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR032505. Corona_NSP4_C.
IPR002589. Macro_dom.
IPR032592. NAR_dom.
IPR024375. Nsp3_coronavir.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
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.
PF16251. NAR. 1 hit.
PF09401. NSP10. 1 hit.
PF08716. nsp7. 1 hit.
PF08717. nsp8. 1 hit.
PF08710. nsp9. 1 hit.
PF05409. Peptidase_C30. 1 hit.
PF11633. SUD-M. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view]
SMARTiSM00506. A1pp. 1 hit.
[Graphical view]
SUPFAMiSSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
PROSITEiPS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiR1A_CVEMC
AccessioniPrimary (citable) accession number: K9N638
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2013
Last sequence update: March 6, 2013
Last modified: November 2, 2016
This is version 27 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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