SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0C6X1

- R1AB_CVH22

UniProt

P0C6X1 - R1AB_CVH22

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Replicase polyprotein 1ab

Gene
rep, 1a-1b
Organism
Human coronavirus 229E (HCoV-229E)
Status
Reviewed - 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.
The papain-like proteinase 1 (PLP1) and papain-like proteinase 2 (PLP2) are responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PLP2 possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. PLP2 also antagonizes innate immune induction of type I interferon by blocking the nuclear translocation of host IRF-3 By similarity.
The main proteinase 3CL-PRO is responsible for the majority of cleavages as it cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu-Gln-CMK. Also contains an ADP-ribose-1''-phosphate (ADRP)-binding function By similarity.
The helicase which contains a zinc finger structure displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Its ATPase activity is strongly stimulated by poly(U), poly(dT), poly(C), poly(dA), but not by poly(G).
The exoribonuclease acts on both ssRNA and dsRNA in a 3' to 5' direction 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.
NendoU is a Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond 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).
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei111 – 1122Cleavage; by PL1-PRO
Sitei897 – 8982Cleavage; by PL1-PRO
Active sitei1054 – 10541For PL1-PRO activity By similarity
Active sitei1205 – 12051For PL1-PRO activity By similarity
Active sitei1701 – 17011For PL2-PRO activity By similarity
Active sitei1863 – 18631For PL2-PRO activity By similarity
Sitei2484 – 24852Cleavage; by PL2-PRO
Sitei2965 – 29662Cleavage; by 3CL-PRO
Active sitei3006 – 30061For 3CL-PRO activity
Active sitei3109 – 31091For 3CL-PRO activity
Sitei3267 – 32682Cleavage; by 3CL-PRO
Sitei3546 – 35472Cleavage; by 3CL-PRO
Sitei3629 – 36302Cleavage; by 3CL-PRO
Sitei3824 – 38252Cleavage; by 3CL-PRO
Sitei3933 – 39342Cleavage; by 3CL-PRO
Sitei4068 – 40692Cleavage; by 3CL-PRO
Sitei4995 – 49962Cleavage; by 3CL-PRO
Sitei5592 – 55932Cleavage; by 3CL-PRO
Sitei6110 – 61112Cleavage; by 3CL-PRO
Sitei6458 – 64592Cleavage; by 3CL-PRO

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1126 – 115732C4-type 1Add
BLAST
Zinc fingeri1780 – 181536C4-type 2; atypicalAdd
BLAST
Zinc fingeri4007 – 402317 By similarityAdd
BLAST
Zinc fingeri4049 – 406214 By similarityAdd
BLAST
Nucleotide bindingi5278 – 52858ATP Inferred

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. endonuclease activity Source: UniProtKB-KW
  4. exoribonuclease activity, producing 5'-phosphomonoesters Source: InterPro
  5. helicase activity Source: UniProtKB-KW
  6. methyltransferase activity Source: InterPro
  7. omega peptidase activity Source: InterPro
  8. RNA binding Source: UniProtKB-KW
  9. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  10. 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. transcription, DNA-templated Source: InterPro
  5. viral protein processing Source: InterPro
  6. viral RNA genome replication Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Exonuclease, Helicase, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase

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, Viral RNA replication

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Replicase polyprotein 1ab
Short name:
pp1ab
Alternative name(s):
ORF1ab polyprotein
Cleaved into the following 15 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
RNA-directed RNA polymerase (EC:2.7.7.48)
Short name:
Pol
Short name:
RdRp
Alternative name(s):
nsp12
p100
Helicase (EC:3.6.4.12, EC:3.6.4.13)
Short name:
Hel
Alternative name(s):
nsp13
p66
p66-HEL
Exoribonuclease (EC:3.1.13.-)
Short name:
ExoN
Alternative name(s):
nsp14
Alternative name(s):
NendoU
nsp15
p41
Alternative name(s):
nsp16
Gene namesi
Name:rep
ORF Names:1a-1b
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 3 : Host membrane; Multi-pass membrane protein Reviewed prediction 1 Publication
Chain Non-structural protein 4 : Host membrane; Multi-pass membrane protein Reviewed prediction 1 Publication
Chain Non-structural protein 6 : Host membrane; Multi-pass membrane protein Reviewed prediction 1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
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.1 Publication
Chain Helicase : Host endoplasmic reticulum-Golgi intermediate compartment Reviewed prediction
Note: The helicase interacts with the N protein in membranous complexes and colocalizes with sites of synthesis of new viral RNA By similarity.1 Publication
Chain Uridylate-specific endoribonuclease : Host cytoplasmhost perinuclear region By similarity 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1925 – 194521Helical; Reviewed predictionAdd
BLAST
Transmembranei1998 – 201821Helical; Reviewed predictionAdd
BLAST
Transmembranei2068 – 208821Helical; Reviewed predictionAdd
BLAST
Transmembranei2095 – 211521Helical; Reviewed predictionAdd
BLAST
Transmembranei2491 – 251121Helical; Reviewed predictionAdd
BLAST
Transmembranei2731 – 275121Helical; Reviewed predictionAdd
BLAST
Transmembranei2755 – 277521Helical; Reviewed predictionAdd
BLAST
Transmembranei2782 – 280221Helical; Reviewed predictionAdd
BLAST
Transmembranei2809 – 282921Helical; Reviewed predictionAdd
BLAST
Transmembranei2834 – 285421Helical; Reviewed predictionAdd
BLAST
Transmembranei3281 – 330121Helical; Reviewed predictionAdd
BLAST
Transmembranei3304 – 332421Helical; Reviewed predictionAdd
BLAST
Transmembranei3328 – 334821Helical; Reviewed predictionAdd
BLAST
Transmembranei3367 – 338721Helical; Reviewed predictionAdd
BLAST
Transmembranei3401 – 342121Helical; Reviewed predictionAdd
BLAST
Transmembranei3422 – 344221Helical; Reviewed predictionAdd
BLAST
Transmembranei3467 – 348721Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. host cell endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB-SubCell
  2. host cell membrane Source: UniProtKB-SubCell
  3. host cell perinuclear region of cytoplasm Source: UniProtKB-SubCell
  4. 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
Mutagenesisi5284 – 52841K → A: Almost complete loss of helicase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 111111Non-structural protein 1PRO_0000037293Add
BLAST
Chaini112 – 897786Non-structural protein 2PRO_0000037294Add
BLAST
Chaini898 – 24841587Non-structural protein 3PRO_0000037295Add
BLAST
Chaini2485 – 2965481Non-structural protein 4PRO_0000037296Add
BLAST
Chaini2966 – 32673023C-like proteinasePRO_0000037297Add
BLAST
Chaini3268 – 3546279Non-structural protein 6PRO_0000037298Add
BLAST
Chaini3547 – 362983Non-structural protein 7PRO_0000037299Add
BLAST
Chaini3630 – 3824195Non-structural protein 8PRO_0000037300Add
BLAST
Chaini3825 – 3933109Non-structural protein 9PRO_0000037301Add
BLAST
Chaini3934 – 4068135Non-structural protein 10PRO_0000037302Add
BLAST
Chaini4069 – 4995927RNA-directed RNA polymerasePRO_0000037303Add
BLAST
Chaini4996 – 5592597HelicasePRO_0000037304Add
BLAST
Chaini5593 – 6110518Exoribonuclease By similarityPRO_0000037305Add
BLAST
Chaini6111 – 6458348Uridylate-specific endoribonuclease By similarityPRO_0000037306Add
BLAST
Chaini6459 – 6758300Putative 2'-O-methyl transferase By similarityPRO_0000037307Add
BLAST

Post-translational modificationi

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

Interactioni

Subunit structurei

3CL-PRO exists as monomer and homodimer. Eight copies of nsp7 and eight copies of nsp8 assemble to form a heterohexadecamer. Nsp9 is a dimer. Nsp10 forms a dodecamer By similarity.

Structurei

Secondary structure

1
6758
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 – 133713
Beta strandi1345 – 13506
Beta strandi1353 – 13597
Helixi1367 – 138014
Beta strandi1381 – 13833
Beta strandi1385 – 13873
Helixi1393 – 13953
Helixi1399 – 140911
Beta strandi1415 – 14195
Helixi1422 – 143312
Helixi3829 – 38313
Beta strandi3834 – 38429
Helixi3843 – 38453
Beta strandi3847 – 38559
Beta strandi3858 – 38603
Beta strandi3862 – 38698
Beta strandi3873 – 38786
Beta strandi3881 – 38833
Beta strandi3885 – 38895
Beta strandi3893 – 38975
Beta strandi3904 – 39118
Helixi3916 – 393015

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P9SX-ray2.54A/B2966-3265[»]
2J97X-ray1.75A3825-3933[»]
2J98X-ray1.80A3825-3933[»]
B3830-3933[»]
3EJGX-ray1.78A1270-1434[»]
ProteinModelPortaliP0C6X1.
SMRiP0C6X1. Positions 2966-3265, 3827-3932, 3940-4064.

Miscellaneous databases

EvolutionaryTraceiP0C6X1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1016 – 1268253Peptidase C16 1Add
BLAST
Domaini1269 – 1436168MacroAdd
BLAST
Domaini1663 – 1914252Peptidase C16 2Add
BLAST
Domaini2966 – 3267302Peptidase C30Add
BLAST
Domaini4675 – 4837163RdRp catalyticAdd
BLAST
Domaini4996 – 507984CV MBDAdd
BLAST
Domaini5253 – 5434182(+)RNA virus helicase ATP-bindingAdd
BLAST
Domaini5435 – 5607173(+)RNA virus helicase C-terminalAdd
BLAST

Region

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

Domaini

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

Sequence similaritiesi

Contains 1 Macro domain.

Zinc finger

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

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR009466. NSP11.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR027417. P-loop_NTPase.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR007094. RNA-dir_pol_PSvirus.
IPR009469. RNA_pol_N_coronovir.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases-like.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view]
PfamiPF06478. Corona_RPol_N. 1 hit.
PF01661. Macro. 1 hit.
PF09401. NSP10. 1 hit.
PF06471. NSP11. 1 hit.
PF06460. NSP13. 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.
SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51653. CV_MBD. 1 hit.
PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 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 1ab (identifier: P0C6X1-1) [UniParc]FASTAAdd to Basket

Also known as: pp1ab

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

MACNRVTLAV ASDSEISANG CSTIAQAVRR YSEAASNGFR ACRFVSLDLQ     50
DCIVGIADDT YVMGLHGNQT LFCNIMKFSD RPFMLHGWLV FSNSNYLLEE 100
FDVVFGKRGG GNVTYTDQYL CGADGKPVMS EDLWQFVDHF GENEEIIING 150
HTYVCAWLTK RKPLDYKRQN NLAIEEIEYV HGDALHTLRN GSVLEMAKEV 200
KTSSKVVLSD ALDKLYKVFG SPVMTNGSNI LEAFTKPVFI SALVQCTCGT 250
KSWSVGDWTG FKSSCCNVIS NKLCVVPGNV KPGDAVITTQ QAGAGIKYFC 300
GMTLKFVANI EGVSVWRVIA LQSVDCFVAS STFVEEEHVN RMDTFCFNVR 350
NSVTDECRLA MLGAEMTSNV RRQVASGVID ISTGWFDVYD DIFAESKPWF 400
VRKAEDIFGP CWSALASALK QLKVTTGELV RFVKSICNSA VAVVGGTIQI 450
LASVPEKFLN AFDVFVTAIQ TVFDCAVETC TIAGKAFDKV FDYVLLDNAL 500
VKLVTTKLKG VRERGLNKVK YATVVVGSTE EVKSSRVERS TAVLTIANNY 550
SKLFDEGYTV VIGDVAYFVS DGYFRLMASP NSVLTTAVYK PLFAFNVNVM 600
GTRPEKFPTT VTCENLESAV LFVNDKITEF QLDYSIDVID NEIIVKPNIS 650
LCVPLYVRDY VDKWDDFCRQ YSNESWFEDD YRAFISVLDI TDAAVKAAES 700
KAFVDTIVPP CPSILKVIDG GKIWNGVIKN VNSVRDWLKS LKLNLTQQGL 750
LGTCAKRFKR WLGILLEAYN AFLDTVVSTV KIGGLTFKTY AFDKPYIVIR 800
DIVCKVENKT EAEWIELFPH NDRIKSFSTF ESAYMPIADP THFDIEEVEL 850
LDAEFVEPGC GGILAVIDEH VFYKKDGVYY PSNGTNILPV AFTKAAGGKV 900
SFSDDVEVKD IEPVYRVKLC FEFEDEKLVD VCEKAIGKKI KHEGDWDSFC 950
KTIQSALSVV SCYVNLPTYY IYDEEGGNDL SLPVMISEWP LSVQQAQQEA 1000
TLPDIAEDVV DQVEEVNSIF DIETVDVKHD VSPFEMPFEE LNGLKILKQL 1050
DNNCWVNSVM LQIQLTGILD GDYAMQFFKM GRVAKMIERC YTAEQCIRGA 1100
MGDVGLCMYR LLKDLHTGFM VMDYKCSCTS GRLEESGAVL FCTPTKKAFP 1150
YGTCLNCNAP RMCTIRQLQG TIIFVQQKPE PVNPVSFVVK PVCSSIFRGA 1200
VSCGHYQTNI YSQNLCVDGF GVNKIQPWTN DALNTICIKD ADYNAKVEIS 1250
VTPIKNTVDT TPKEEFVVKE KLNAFLVHDN VAFYQGDVDT VVNGVDFDFI 1300
VNAANENLAH GGGLAKALDV YTKGKLQRLS KEHIGLAGKV KVGTGVMVEC 1350
DSLRIFNVVG PRKGKHERDL LIKAYNTINN EQGTPLTPIL SCGIFGIKLE 1400
TSLEVLLDVC NTKEVKVFVY TDTEVCKVKD FVSGLVNVQK VEQPKIEPKP 1450
VSVIKVAPKP YRVDGKFSYF TEDLLCVADD KPIVLFTDSM LTLDDRGLAL 1500
DNALSGVLSA AIKDCVDINK AIPSGNLIKF DIGSVVVYMC VVPSEKDKHL 1550
DNNVQRCTRK LNRLMCDIVC TIPADYILPL VLSSLTCNVS FVGELKAAEA 1600
KVITIKVTED GVNVHDVTVT TDKSFEQQVG VIADKDKDLS GAVPSDLNTS 1650
ELLTKAIDVD WVEFYGFKDA VTFATVDHSA FAYESAVVNG IRVLKTSDNN 1700
CWVNAVCIAL QYSKPHFISQ GLDAAWNKFV LGDVEIFVAF VYYVARLMKG 1750
DKGDAEDTLT KLSKYLANEA QVQLEHYSSC VECDAKFKNS VASINSAIVC 1800
ASVKRDGVQV GYCVHGIKYY SRVRSVRGRA IIVSVEQLEP CAQSRLLSGV 1850
AYTAFSGPVD KGHYTVYDTA KKSMYDGDRF VKHDLSLLSV TSVVMVGGYV 1900
APVNTVKPKP VINQLDEKAQ KFFDFGDFLI HNFVIFFTWL LSMFTLCKTA 1950
VTTGDVKIMA KAPQRTGVVL KRSLKYNLKA SAAVLKSKWW LLAKFTKLLL 2000
LIYTLYSVVL LCVRFGPFNF CSETVNGYAK SNFVKDDYCD GSLGCKMCLF 2050
GYQELSQFSH LDVVWKHITD PLFSNMQPFI VMVLLLIFGD NYLRCFLLYF 2100
VAQMISTVGV FLGYKETNWF LHFIPFDVIC DELLVTVIVI KVISFVRHVL 2150
FGCENPDCIA CSKSARLKRF PVNTIVNGVQ RSFYVNANGG SKFCKKHRFF 2200
CVDCDSYGYG STFITPEVSR ELGNITKTNV QPTGPAYVMI DKVEFENGFY 2250
RLYSCETFWR YNFDITESKY SCKEVFKNCN VLDDFIVFNN NGTNVTQVKN 2300
ASVYFSQLLC RPIKLVDSEL LSTLSVDFNG VLHKAYIDVL RNSFGKDLNA 2350
NMSLAECKRA LGLSISDHEF TSAISNAHRC DVLLSDLSFN NFVSSYAKPE 2400
EKLSAYDLAC CMRAGAKVVN ANVLTKDQTP IVWHAKDFNS LSAEGRKYIV 2450
KTSKAKGLTF LLTINENQAV TQIPATSIVA KQGAGDAGHS LTWLWLLCGL 2500
VCLIQFYLCF FMPYFMYDIV SSFEGYDFKY IENGQLKNFE APLKCVRNVF 2550
ENFEDWHYAK FGFTPLNKQS CPIVVGVSEI VNTVAGIPSN VYLVGKTLIF 2600
TLQAAFGNAG VCYDIFGVTT PEKCIFTSAC TRLEGLGGNN VYCYNTALME 2650
GSLPYSSIQA NAYYKYDNGN FIKLPEVIAQ GFGFRTVRTI ATKYCRVGEC 2700
VESNAGVCFG FDKWFVNDGR VANGYVCGTG LWNLVFNILS MFSSSFSVAA 2750
MSGQILLNCA LGAFAIFCCF LVTKFRRMFG DLSVGVCTVV VAVLLNNVSY 2800
IVTQNLVTMI AYAILYFFAT RSLRYAWIWC AAYLIAYISF APWWLCAWYF 2850
LAMLTGLLPS LLKLKVSTNL FEGDKFVGTF ESAAAGTFVI DMRSYEKLAN 2900
SISPEKLKSY AASYNRYKYY SGNANEADYR CACYAYLAKA MLDFSRDHND 2950
ILYTPPTVSY GSTLQAGLRK MAQPSGFVEK CVVRVCYGNT VLNGLWLGDI 3000
VYCPRHVIAS NTTSAIDYDH EYSIMRLHNF SIISGTAFLG VVGATMHGVT 3050
LKIKVSQTNM HTPRHSFRTL KSGEGFNILA CYDGCAQGVF GVNMRTNWTI 3100
RGSFINGACG SPGYNLKNGE VEFVYMHQIE LGSGSHVGSS FDGVMYGGFE 3150
DQPNLQVESA NQMLTVNVVA FLYAAILNGC TWWLKGEKLF VEHYNEWAQA 3200
NGFTAMNGED AFSILAAKTG VCVERLLHAI QVLNNGFGGK QILGYSSLND 3250
EFSINEVVKQ MFGVNLQSGK TTSMFKSISL FAGFFVMFWA ELFVYTTTIW 3300
VNPGFLTPFM ILLVALSLCL TFVVKHKVLF LQVFLLPSII VAAIQNCAWD 3350
YHVTKVLAEK FDYNVSVMQM DIQGFVNIFI CLFVALLHTW RFAKERCTHW 3400
CTYLFSLIAV LYTALYSYDY VSLLVMLLCA ISNEWYIGAI IFRICRFGVA 3450
FLPVEYVSYF DGVKTVLLFY MLLGFVSCMY YGLLYWINRF CKCTLGVYDF 3500
CVSPAEFKYM VANGLNAPNG PFDALFLSFK LMGIGGPRTI KVSTVQSKLT 3550
DLKCTNVVLM GILSNMNIAS NSKEWAYCVE MHNKINLCDD PETAQELLLA 3600
LLAFFLSKHS DFGLGDLVDS YFENDSILQS VASSFVGMPS FVAYETARQE 3650
YENAVANGSS PQIIKQLKKA MNVAKAEFDR ESSVQKKINR MAEQAAAAMY 3700
KEARAVNRKS KVVSAMHSLL FGMLRRLDMS SVDTILNMAR NGVVPLSVIP 3750
ATSAARLVVV VPDHDSFVKM MVDGFVHYAG VVWTLQEVKD NDGKNVHLKD 3800
VTKENQEILV WPLILTCERV VKLQNNEIMP GKMKVKATKG EGDGGITSEG 3850
NALYNNEGGR AFMYAYVTTK PGMKYVKWEH DSGVVTVELE PPCRFVIDTP 3900
TGPQIKYLYF VKNLNNLRRG AVLGYIGATV RLQAGKQTEF VSNSHLLTHC 3950
SFAVDPAAAY LDAVKQGAKP VGNCVKMLTN GSGSGQAITC TIDSNTTQDT 4000
YGGASVCIYC RAHVAHPTMD GFCQYKGKWV QVPIGTNDPI RFCLENTVCK 4050
VCGCWLNHGC TCDRTAIQSF DNSYLNRVRG SSAARLEPCN GTDIDYCVRA 4100
FDVYNKDASF IGKNLKSNCV RFKNVDKDDA FYIVKRCIKS VMDHEQSMYN 4150
LLKGCNAVAK HDFFTWHEGR TIYGNVSRQD LTKYTMMDLC FALRNFDEKD 4200
CEVFKEILVL TGCCSTDYFE MKNWFDPIEN EDIHRVYAAL GKVVANAMLK 4250
CVAFCDEMVL KGVVGVLTLD NQDLNGNFYD FGDFVLCPPG MGIPYCTSYY 4300
SYMMPVMGMT NCLASECFMK SDIFGQDFKT FDLLKYDFTE HKEVLFNKYF 4350
KYWGQDYHPD CVDCHDEMCI LHCSNFNTLF ATTIPNTAFG PLCRKVFIDG 4400
VPVVATAGYH FKQLGLVWNK DVNTHSTRLT ITELLQFVTD PTLIVASSPA 4450
LVDKRTVCFS VAALSTGLTS QTVKPGHFNK EFYDFLRSQG FFDEGSELTL 4500
KHFFFTQKGD AAIKDFDYYR YNRPTMLDIG QARVAYQVAA RYFDCYEGGC 4550
ITSREVVVTN LNKSAGWPLN KFGKAGLYYE SISYEEQDAI FSLTKRNILP 4600
TMTQLNLKYA ISGKERARTV GGVSLLATMT TRQFHQKCLK SIVATRNATV 4650
VIGTTKFYGG WDNMLKNLMA DVDDPKLMGW DYPKCDRAMP SMIRMLSAMI 4700
LGSKHVTCCT ASDKFYRLSN ELAQVLTEVV YSNGGFYFKP GGTTSGDATT 4750
AYANSVFNIF QAVSSNINCV LSVNSSNCNN FNVKKLQRQL YDNCYRNSNV 4800
DESFVDDFYG YLQKHFSMMI LSDDSVVCYN KTYAGLGYIA DISAFKATLY 4850
YQNGVFMSTA KCWTEEDLSI GPHEFCSQHT MQIVDENGKY YLPYPDPSRI 4900
ISAGVFVDDI TKTDAVILLE RYVSLAIDAY PLSKHPKPEY RKVFYALLDW 4950
VKHLNKTLNE GVLESFSVTL LDEHESKFWD ESFYASMYEK STVLQAAGLC 5000
VVCGSQTVLR CGDCLRRPML CTKCAYDHVF GTDHKFILAI TPYVCNTSGC 5050
NVNDVTKLYL GGLNYYCVDH KPHLSFPLCS AGNVFGLYKS SALGSMDIDV 5100
FNKLSTSDWS DIRDYKLAND AKESLRLFAA ETVKAKEESV KSSYAYATLK 5150
EIVGPKELLL LWESGKAKPP LNRNSVFTCF QITKDSKFQV GEFVFEKVDY 5200
GSDTVTYKST ATTKLVPGML FILTSHNVAP LRAPTMANQE KYSTIYKLHP 5250
SFNVSDAYAN LVPYYQLIGK QRITTIQGPP GSGKSHCSIG IGVYYPGARI 5300
VFTACSHAAV DSLCAKAVTA YSVDKCTRII PARARVECYS GFKPNNNSAQ 5350
YVFSTVNALP EVNADIVVVD EVSMCTNYDL SVINQRISYK HIVYVGDPQQ 5400
LPAPRVLISK GVMEPIDYNV VTQRMCAIGP DVFLHKCYRC PAEIVNTVSE 5450
LVYENKFVPV KEASKQCFKI FERGSVQVDN GSSINRRQLD VVKRFIHKNS 5500
TWSKAVFISP YNSQNYVAAR LLGLQTQTVD SAQGSEYDYV IFAQTSDTAH 5550
ACNANRFNVA ITRAKKGIFC IMSDRTLFDA LKFFEITMTD LQSESSCGLF 5600
KDCARNPIDL PPSHATTYLS LSDRFKTSGD LAVQIGNNNV CTYEHVISYM 5650
GFRFDVSMPG SHSLFCTRDF AMRHVRGWLG MDVEGAHVTG DNVGTNVPLQ 5700
VGFSNGVDFV AQPEGCVLTN TGSVVKPVRA RAPPGEQFTH IVPLLRKGQP 5750
WSVLRKRIVQ MIADFLAGSS DVLVFVLWAG GLELTTMRYF VKIGAVKHCQ 5800
CGTVATCYNS VSNDYCCFKH ALGCDYVYNP YVIDIQQWGY VGSLSTNHHA 5850
ICNVHRNEHV ASGDAIMTRC LAVYDCFVKN VDWSITYPMI ANENAINKGG 5900
RTVQSHIMRA AIKLYNPKAI HDIGNPKGIR CAVTDAKWYC YDKNPINSNV 5950
KTLEYDYMTH GQMDGLCLFW NCNVDMYPEF SIVCRFDTRT RSTLNLEGVN 6000
GGSLYVNNHA FHTPAYDKRA MAKLKPAPFF YYDDGSCEVV HDQVNYVPLR 6050
ATNCITKCNI GGAVCSKHAN LYRAYVESYN IFTQAGFNIW VPTTFDCYNL 6100
WQTFTEVNLQ GLENIAFNVV NKGSFVGADG ELPVAISGDK VFVRDGNTDN 6150
LVFVNKTSLP TNIAFELFAK RKVGLTPPLS ILKNLGVVAT YKFVLWDYEA 6200
ERPLTSFTKS VCGYTDFAED VCTCYDNSIQ GSYERFTLST NAVLFSATAV 6250
KTGGKSLPAI KLNFGMLNGN AIATVKSEDG NIKNINWFVY VRKDGKPVDH 6300
YDGFYTQGRN LQDFLPRSTM EEDFLNMDIG VFIQKYGLED FNFEHVVYGD 6350
VSKTTLGGLH LLISQVRLSK MGILKAEEFV AASDITLKCC TVTYLNDPSS 6400
KTVCTYMDLL LDDFVSVLKS LDLTVVSKVH EVIIDNKPWR WMLWCKDNAV 6450
ATFYPQLQSA EWKCGYSMPG IYKTQRMCLE PCNLYNYGAG LKLPSGIMFN 6500
VVKYTQLCQY FNSTTLCVPH NMRVLHLGAG SDYGVAPGTA VLKRWLPHDA 6550
IVVDNDVVDY VSDADFSVTG DCATVYLEDK FDLLISDMYD GRTKAIDGEN 6600
VSKEGFFTYI NGFICEKLAI GGSIAIKVTE YSWNKKLYEL VQRFSFWTMF 6650
CTSVNTSSSE AFVVGINYLG DFAQGPFIDG NIIHANYVFW RNSTVMSLSY 6700
NSVLDLSKFN CKHKATVVVQ LKDSDINEMV LSLVRSGKLL VRGNGKCLSF 6750
SNHLVSTK 6758

Note: Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.

Length:6,758
Mass (Da):754,163
Last modified:June 10, 2008 - v1
Checksum:iB7EC2ABD7FE4EC1A
GO
Isoform Replicase polyprotein 1a (identifier: P0C6U2-1) [UniParc]FASTAAdd to Basket

Also known as: pp1a, ORF1a polyprotein

The sequence of this isoform can be found in the external entry P0C6U2.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by conventional translation.

Length:4,085
Mass (Da):454,215
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1982 – 19821A → Q Ref 1 Publication
Sequence conflicti1982 – 19821A → Q 1 1 Publication
Sequence conflicti4042 – 40421F → S Ref 1 Publication
Sequence conflicti4042 – 40421F → S 1 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF304460 Genomic RNA. Translation: AAG48591.1.
PIRiS28600.
RefSeqiNP_073549.1. NC_002645.1. [P0C6X1-1]

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: AAG48591.1 .
PIRi S28600.
RefSeqi NP_073549.1. NC_002645.1. [P0C6X1-1 ]

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 [» ]
2J97 X-ray 1.75 A 3825-3933 [» ]
2J98 X-ray 1.80 A 3825-3933 [» ]
B 3830-3933 [» ]
3EJG X-ray 1.78 A 1270-1434 [» ]
ProteinModelPortali P0C6X1.
SMRi P0C6X1. 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 P0C6X1.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR027351. (+)RNA_virus_helicase_core_dom.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR009466. NSP11.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR027417. P-loop_NTPase.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR007094. RNA-dir_pol_PSvirus.
IPR009469. RNA_pol_N_coronovir.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases-like.
IPR009003. Trypsin-like_Pept_dom.
IPR014827. Viral_protease.
[Graphical view ]
Pfami PF06478. Corona_RPol_N. 1 hit.
PF01661. Macro. 1 hit.
PF09401. NSP10. 1 hit.
PF06471. NSP11. 1 hit.
PF06460. NSP13. 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.
SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEi PS51653. CV_MBD. 1 hit.
PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 2 hits.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[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] OF 1-4085.
  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. "Identification and subcellular localization of a 41 kDa, polyprotein 1ab processing product in human coronavirus 229E-infected cells."
    Heusipp G., Groetzinger C., Herold J., Siddell S.G., Ziebuhr J.
    J. Gen. Virol. 78:2789-2794(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF P41, SUBCELLULAR LOCATION.
  5. "The human coronavirus 229E superfamily 1 helicase has RNA and DNA duplex-unwinding activities with 5'-to-3' polarity."
    Seybert A., Hegyi A., Siddell S.G., Ziebuhr J.
    RNA 6:1056-1068(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF HELICASE, MUTAGENESIS OF LYS-5284.
  6. "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.
  7. Erratum
    Herold J., Siddell S.G., Gorbalenya A.E.
    J. Biol. Chem. 274:21490-21490(1999)
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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 nameiR1AB_CVH22
AccessioniPrimary (citable) accession number: P0C6X1
Secondary accession number(s): Q05002, Q9DLN0, Q9DLN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: July 9, 2014
This is version 57 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

Similar proteinsi