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P0C6T5

- R1A_BCHK5

UniProt

P0C6T5 - R1A_BCHK5

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Protein
Replicase polyprotein 1a
Gene
1a
Organism
Bat coronavirus HKU5 (BtCoV) (BtCoV/HKU5/2004)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

Functioni

The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of 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. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent 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

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei195 – 1962Cleavage Reviewed prediction
Sitei851 – 8522Cleavage; by PL-PRO Reviewed prediction
Active sitei1668 – 16681For PL-PRO activity By similarity
Active sitei1838 – 18381For PL-PRO activity By similarity
Sitei2830 – 28312Cleavage; by PL-PRO Reviewed prediction
Sitei3338 – 33392Cleavage; by 3CL-PRO Reviewed prediction
Active sitei3379 – 33791For 3CL-PRO activity By similarity
Active sitei3486 – 34861For 3CL-PRO activity By similarity
Sitei3644 – 36452Cleavage; by 3CL-PRO Reviewed prediction
Sitei3936 – 39372Cleavage; by 3CL-PRO Reviewed prediction
Sitei4019 – 40202Cleavage; by 3CL-PRO Reviewed prediction
Sitei4218 – 42192Cleavage; by 3CL-PRO Reviewed prediction
Sitei4328 – 43292Cleavage; by 3CL-PRO Reviewed prediction
Sitei4467 – 44682Cleavage; by 3CL-PRO Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1748 – 178538C4-type By similarity
Add
BLAST
Zinc fingeri4402 – 441817 By similarity
Add
BLAST
Zinc fingeri4444 – 445714 By similarity
Add
BLAST

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. RNA-directed RNA polymerase activity Source: InterPro
  3. cysteine-type endopeptidase activity Source: InterPro
  4. omega peptidase activity Source: InterPro
  5. zinc ion binding Source: InterPro
Complete GO annotation...

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. suppression by virus of host ISG15 activity Source: UniProtKB-KW
  5. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
  6. viral genome replication Source: InterPro
  7. 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 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:
Non-structural protein 1
Short name:
nsp1
Alternative name(s):
Leader protein
Non-structural protein 2
Short name:
nsp2
Alternative name(s):
p65 homolog
Alternative name(s):
PL2-PRO
Papain-like proteinase
Short name:
PL-PRO
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
OrganismiBat coronavirus HKU5 (BtCoV) (BtCoV/HKU5/2004)
Taxonomic identifieri694008 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiPipistrellus abramus (Japanese pipistrelle) (Pipistrellus javanicus abramus) [TaxID: 105295]
ProteomesiUP000007451: 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
Transmembranei2196 – 221621Helical; Reviewed prediction
Add
BLAST
Transmembranei2268 – 228821Helical; Reviewed prediction
Add
BLAST
Transmembranei2372 – 239221Helical; Reviewed prediction
Add
BLAST
Transmembranei2396 – 241621Helical; Reviewed prediction
Add
BLAST
Transmembranei2421 – 244121Helical; Reviewed prediction
Add
BLAST
Transmembranei2848 – 286821Helical; Reviewed prediction
Add
BLAST
Transmembranei3119 – 313921Helical; Reviewed prediction
Add
BLAST
Transmembranei3152 – 317221Helical; Reviewed prediction
Add
BLAST
Transmembranei3203 – 322321Helical; Reviewed prediction
Add
BLAST
Transmembranei3650 – 367021Helical; Reviewed prediction
Add
BLAST
Transmembranei3684 – 370421Helical; Reviewed prediction
Add
BLAST
Transmembranei3709 – 372921Helical; Reviewed prediction
Add
BLAST
Transmembranei3760 – 377718Helical; Reviewed prediction
Add
BLAST
Transmembranei3782 – 380221Helical; Reviewed prediction
Add
BLAST
Transmembranei3823 – 384321Helical; Reviewed prediction
Add
BLAST
Transmembranei3855 – 387521Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. host cell membrane Source: UniProtKB-SubCell
  2. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm, Host membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 44814481Replicase polyprotein 1a
PRO_0000338098Add
BLAST
Chaini1 – 195195Non-structural protein 1 Reviewed prediction
PRO_0000338099Add
BLAST
Chaini196 – 851656Non-structural protein 2 Reviewed prediction
PRO_0000338100Add
BLAST
Chaini852 – 28301979Non-structural protein 3 Reviewed prediction
PRO_0000338101Add
BLAST
Chaini2831 – 3338508Non-structural protein 4 Reviewed prediction
PRO_0000338102Add
BLAST
Chaini3339 – 36443063C-like proteinase Reviewed prediction
PRO_0000338103Add
BLAST
Chaini3645 – 3936292Non-structural protein 6 Reviewed prediction
PRO_0000338104Add
BLAST
Chaini3937 – 401983Non-structural protein 7 Reviewed prediction
PRO_0000338105Add
BLAST
Chaini4020 – 4218199Non-structural protein 8 Reviewed prediction
PRO_0000338106Add
BLAST
Chaini4219 – 4328110Non-structural protein 9 Reviewed prediction
PRO_0000338107Add
BLAST
Chaini4328 – 4481154Non-structural protein 11 Reviewed prediction
PRO_0000338109Add
BLAST
Chaini4329 – 4467139Non-structural protein 10 Reviewed prediction
PRO_0000338108Add
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 By similarity.

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

3D structure databases

ProteinModelPortaliP0C6T5.
SMRiP0C6T5. Positions 3937-4007, 4268-4328, 4335-4459.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1186 – 1345160Macro
Add
BLAST
Domaini1628 – 1902275Peptidase C16
Add
BLAST
Domaini3339 – 3644306Peptidase C30
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2158 – 2441284HD1 By similarity
Add
BLAST
Regioni2848 – 3223376HD2 By similarity
Add
BLAST
Regioni3650 – 3875226HD3 By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi964 – 1066103Glu-rich
Add
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 By similarity.

Sequence similaritiesi

Contains 1 Macro domain.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

InterProiIPR002589. Macro_dom.
IPR024375. Nsp3_coronavir.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
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.
PF11633. SUD-M. 1 hit.
PF08715. Viral_protease. 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. Align

Isoform Replicase polyprotein 1a (identifier: P0C6T5-1) [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

MSFVAGVAPQ GARGKYRAEL NTEKRTDHVS LKASLCDAGD LVLKISPWFM     50
DGESAYKHVS EQLSKGSKLL FVPQTLKGFI RHLPGPRVYL VERLTGGTYS 100
DPFMVNQLAY QNAAGEGVIG TTLQGKRVGM FFPFDADLVT GEFQFLLRKK 150
GFGGNRFRDA PWDYNWTPYS DLMDALEADP CGKYSQSLLK KLVGGDFTPI 200
DQYMCGKNGK PIAEFAALMA SEGITKLADV EAEVKSRTDS DRYIVFKNKL 250
YRIVWNVQRK DVAYSKQSAF TMNSIVQLDT MEDVPRHSFT IGSEIQVIAP 300
STAVQANGHL NLKQRLLYAF YGKQAVSEPN YIYHSAYVDC TSCGKGSWLT 350
GNAVQGFACD CGAHYCANDV DLQSSGLVRK NAVLLTTCPC NKDGECKHTL 400
PQLVSMMTDK CDVEVVGKTF ILTYGGVIYA YMGCSGGTMH FIPRAKSCVS 450
KIGDAIFTGC TGTWSKVCET ANLFLERAQH AINFVNEFVL TETVVALLSG 500
TTSSIEELRD LCRNATFEKV RDYLTPRGWI VTMGSYIEGV INVGAAGVCN 550
AALNAPFIVL SGLGESFKKV AATPWKLCSS LRETLDHYAD SITYRVFPYD 600
IPCDVTDYTA LLLDCAVLTG ASAYFVARYV DEKVEQLTNL VFSSCQSAVA 650
AFVQACMSTY KATAKFISDM FTLIKVVSER LYVYTSVGFV VVGDYSSQLL 700
KQFMHILSKA MQLLHTTVSW AGSKLPSVVY NGRDSLVFPS GTYYCVSTQG 750
RSLQDQFDLV IPGDLSKKQI GILEPTPNST TVDKKINTNV VEVVVGQLEP 800
TKEHSPELVV GDYVIISNKI FVRSVEDSET VFYPLCTDGK IVPTLFRLKG 850
GAPPKGVKFG GEQTKEITAV RSVSVDYDVH PVLDALLAGS ELATFTVEKD 900
LPVKDFVDVV KDEVIELLSK LLRGYNVDGF DLEDFADTPC YVYNAEGDLA 950
WSSTMTFSVN PVEEVEEECD DDYVEDEYLS EEMLVEEDEN SWAAAVEAVI 1000
PMEDVQLDTL VAEIDVSEPA DDVAEQASTE EVEVPSACVL EASQVANAAE 1050
VESCEAEVSS SIPLHEDANA AKANDCAEGM PALDSTETVS KLSVDTPVGD 1100
VTQDDATSSN ATVISEDVHT ATHSKGLVAV PEVVPEKALG TSVERMRSTS 1150
EWTVVETSLK QETAVIVKND SSAKPQRVKK PKAENPLKNF KHIVLNNDVT 1200
LVFGDAIAVA RATEDCILVN AANTHLKHGG GIAAAIDRAS GGLVQAESDD 1250
YVNFYGPLNV GDSTLLKGHG LATGILHVVG PDARANQDIQ LLKRCYKAFN 1300
KYPLVVSPLI SAGIFCVEPR VSLEYLLSVV HTKTYVVVNS EKVYNDLAAP 1350
KPPTGLTYSH EGWRGIIRNA KSFGFTCFIC TDQSANAKLL KGRGVDLTKK 1400
TQTVDGVKYY LYSSKDPLTD IITAANACKG ICAMPIGYVT HGLDLAQAGQ 1450
QVKKITVPYV CLLASKDQVP ILNSDVAVQT PEQSFINTVI ANGGYHCWHL 1500
VTGELIVKGV SYRKLLNWSD QTICYADNKF YVVKGQIALP FDSLEKCRTY 1550
LTSRAAQQKN VDVLVTIDGV NFRTVVLNNT TTYRVQLGSV FYKGSDISDT 1600
IPTEKMSGEA VYLADNLSEA EKAVLSEVYG TADTAFLHRY YSLLALVKKW 1650
KYTVHDGVKS LKLNSNNCYV NVTMLMLDML KEIKFIVPAL QAAYLKHKGG 1700
DSTEFIALIM AYGDCTYGEP DDASRLLHTI LSKAELTTQA KMVWRQWCNV 1750
CGVQDTTTTG LKACIYVGMN SLDELHATHE ECCQCGDVRK RQLVEHNAPW 1800
LLLSGLNEAK VMTPTSQSAG PDYTAFNVFQ GVETSVGHYL HVRVKDNLLY 1850
KYDSGSLSKT SDMKCKMTDV YYPKQRYSAD CNVVVYSLDG NTWADVDPDL 1900
SAFYMKDGKY FTKKPVIEYS PATILSGSVY TNSCLVGHDG TIGSDAISSS 1950
FNNLLGFDNS KPVSKKLTYS FFPDFEGDVI LTEYSTYDPI YKNGAMLHGK 2000
PILWVNNSKF DSALNKFNRA TLRQVYDIAP VTLENKYTVL QDNQIQQVEV 2050
EAPKEDAKPQ SPVQVAEDID NKLPIIKCKG LKKPFVKDGY SFVNDPQGVN 2100
VIDTLGIDDL RALYVDRNLR LIVLKENNWS ALFNIHTVEK GDLSVIAASG 2150
SITRRVKILL GASSLFAQFA SVTVNVTTAM GKALGRMTRN VITNTGIIGQ 2200
GFALLKMLLI LPFTFWKSKN QSTVKVEVGA LRTAGIVTTN VVKQCASAAY 2250
DVLVVKFKRI DWKSTLRLLF LICTTGLLLS SLYYLFLFHQ VLTSDVMLDG 2300
AEGMLATYRE LRSYLGIHSL CDGMVEAYRN VSYDVNDFCS NRSALCNWCL 2350
IGQDSLTRYS AFQMIQTHVT SYVINIDWVW FVMEFALAYV LYTSTFNVLL 2400
LVVSSQYFFS YTGAFVNWRS YNYLVSGYFF CVTHIPLLGL VRIYNFLACL 2450
WFLRRFYNHV INGCKDTACL LCYKRNRLTR VEASTVVCGS KRTFYIVANG 2500
GTSFCCRHNW NCVDCDTAGI GNTFICEEVA NDLTTSLRRL VKPTDKSHYY 2550
VESVTVKDSV VQLHYSREGA SCYERYPLCY FTNLDKLKFK EVCKTPTGIP 2600
EHNFLIYDSS DRGQENLARS ACVYYSQVLS KPMLLVDSNM VTTVGDSREI 2650
ASKMLDSYVN SFISLFGVNR DKLDKLVATA RDCVKRGDDF QTVIKTFTDA 2700
ARGPAGVESD VETSSIVDAL QYAYKHDLQL TTEGFNNYVP SYIKPDSVAT 2750
ADLGCLIDLN AASVNQTSIR NANGACIWNS SDYMKLSDSL KRQIRIACRK 2800
CNIPFRLTTS RLRSADNILS VKFSATKLSG GAPKWLLKLR DFTWKSYCVV 2850
TLVVFAMAVL SYLCLPAFNM SQVSFHEDRI LTYKVVENGI IRDITPSDTC 2900
FANKYQSFSK WFNEHYGGLF NNDISCPVTV AVIAGVAGAR VPNLPANVAW 2950
VGRQIVLFVS RVFASSNNVC YTPTAEIPYE RFSDSGCVLA SECTLFRDAE 3000
GKINPYCYDP TVLPGASAYD QMKPHVRYDM YDSDMYIKFP EVVFESTLRI 3050
TKTLATRYCR FGSCEDANEG VCITTNGSWA IYNDHYANKP GVYCGDNYFD 3100
IVRRLGLSLF QPVTYFQLST SLALGVMLCI FLTIAFYYVN KVKRALADYT 3150
QCAVVAVAAA LLNSLCLCFV VSNPLLVLPY TALYYYATFY LTGEPAFVMH 3200
VSWFVMFGTV VPIWMVFAYI VGVCLRHLLW VMAYFSKKHV EVFTDGKLNC 3250
SFQDAAANIF VINKDTYVAL RNSITQDSYN RYLSMFNKYK YYSGAMDTAS 3300
YREASAAHLC KALQVYSETG SDVLFQPPNC SVTSSVLQSG LVKMAAPSGV 3350
VENCMVQVTC GSMTLNGLWL DNYVWCPRHV MCPADQLSDP NYDALLVSKT 3400
NLSFIVQKNV GAPANLRVVG HTMVGTLLKL TVESANPQTP AYTFTTVKPG 3450
ASFSVLACYN GRPTGVFMVN MRQNSTIKGS FLCGSCGSVG YTQEGNVINF 3500
CYMHQMELSN GTHTGCAFDG VMYGAFEDRQ VHQVQLSDKY CTINIVAWLY 3550
AAILNGCNWF VKPNKTGIAT FNEWAMSNQF TEFIGTQSVD MLAHKTGVSV 3600
EQLLYAIQTL HKGFQGKTIL GNSMLEDEFT PDDVNMQVMG VVMQSGVKRI 3650
SYGLVHWLFT TLLLAYVATL QLTKFTIWNY LFEVIPLQLT PLVLCVMACV 3700
MLTVKHKHTF LTLFLLPTAI CLTYANIVYE PQTPVSSALI AVANWLNPAS 3750
VYMRTTHTDL GVYLSLCFAL AVVVRRLYRP NASNLALALG SAMVWFYTYT 3800
TGDCSSPLTY LMFLTTLTSD YTVTVFLAVN VAKFFARVVF LYAPHAGFIF 3850
PEVKLVLLMY LAVGYFCTVY FGVFSLLNLK LRVPLGVYDY TVSTQEFRYL 3900
TGNGLHAPRN SWEALRLNMK LIGIGGTPCI KIASVQSKLT DLKCTSVVLL 3950
SVLQQLHLEA NSKAWAHCVK LHNDILAATD PTEAFDNFVC LFATLMSFSA 4000
NVDLEALASD LLDHPSVLQA TLSEFSHLAS YAELEAAQSS YQKALNSGDA 4050
SPQVLKALQK AVNIAKNAYE KDKAVARKLE RMAEQAMTSM YKQARAEDKK 4100
AKIVSAMQTM LFGMIKKLDN DVLNGVISNA RNGCVPLSVV PLCASNKLRV 4150
VIPDITIWNK VVTWPSLSYA GALWDISLIN NVDGEVVKSS DVTETNESLT 4200
WPLVLECTRA ASSAVTLQNN EIRPSGLKTM VVSAGIDHAN CNTSSLAYYE 4250
PVEGRKMLMG ILSENAHLKW AKVEGRDGFV NIELQPPCKF LIAGPKGPEV 4300
RYLYFVKNLN NLHRGQLLGH IAATVRLQAG SNTEFAINSS VLSAVTFSVD 4350
PGKAYLDFVN AGGAPLTNCV KMLTPKTGTG IAVSVKPEAN ADQDTYGGAS 4400
VCLYCRAHIE HPDVTGVCKF KGKFVQVPLH IRDPVGFCLQ NTPCNVCQFW 4450
IGHGCNCDAL RGTTIPQSKD SNFLNESGVL L 4481

Note: Produced by conventional translation.

Length:4,481
Mass (Da):494,801
Last modified:June 10, 2008 - v1
Checksum:i6EA797D2808AF75F
GO
Isoform Replicase polyprotein 1ab (identifier: P0C6W4-1) [UniParc]FASTAAdd to Basket

Also known as: pp1ab

The sequence of this isoform can be found in the external entry P0C6W4.
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:7,182
Mass (Da):799,932
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF065509 Genomic RNA. No translation available.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF065509 Genomic RNA. No translation available.

3D structure databases

ProteinModelPortali P0C6T5.
SMRi P0C6T5. Positions 3937-4007, 4268-4328, 4335-4459.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR002589. Macro_dom.
IPR024375. Nsp3_coronavir.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
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.
PF11633. SUD-M. 1 hit.
PF08715. Viral_protease. 1 hit.
[Graphical view ]
SUPFAMi SSF101816. SSF101816. 1 hit.
SSF144246. SSF144246. 1 hit.
SSF50494. SSF50494. 1 hit.
PROSITEi PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Comparative analysis of twelve genomes of three novel group 2c and group 2d coronaviruses reveals unique group and subgroup features."
    Woo P.C.Y., Wang M., Lau S.K.P., Xu H.F., Poon R.W.S., Guo R., Wong B.H.L., Gao K., Tsoi H.-W., Huang Y., Li K.S.M., Lam C.S.F., Chan K.-H., Zheng B.-J., Yuen K.-Y.
    J. Virol. 81:1574-1585(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate HKU5-1.

Entry informationi

Entry nameiR1A_BCHK5
AccessioniPrimary (citable) accession number: P0C6T5
Secondary accession number(s): A3EXC9
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

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi