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Protein

Replicase polyprotein 1ab

Gene

rep

Organism
Bat coronavirus HKU4 (BtCoV) (BtCoV/HKU4/2004)
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: Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.By similarity
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 similarity
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
RNA-directed RNA polymerase: Responsible for replication and transcription of the viral RNA genome.By similarity
Helicase: Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.By similarity
Guanine-N7 methyltransferase: Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity.By similarity
Uridylate-specific endoribonuclease: Mn2+-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.By similarity
2'-O-methyltransferase: Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.By similarity

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
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 sitei1634For PL-PRO activityPROSITE-ProRule annotation1
Active sitei1800For PL-PRO activityPROSITE-ProRule annotation1
Active sitei3332For 3CL-PRO activityPROSITE-ProRule annotation1
Active sitei3439For 3CL-PRO activityPROSITE-ProRule annotation1
Metal bindingi5359Zinc 1PROSITE-ProRule annotation1
Metal bindingi5362Zinc 1PROSITE-ProRule annotation1
Metal bindingi5370Zinc 2PROSITE-ProRule annotation1
Metal bindingi5373Zinc 1PROSITE-ProRule annotation1
Metal bindingi5380Zinc 1PROSITE-ProRule annotation1
Metal bindingi5383Zinc 2PROSITE-ProRule annotation1
Metal bindingi5387Zinc 2PROSITE-ProRule annotation1
Metal bindingi5393Zinc 2PROSITE-ProRule annotation1
Metal bindingi5404Zinc 3PROSITE-ProRule annotation1
Metal bindingi5409Zinc 3PROSITE-ProRule annotation1
Metal bindingi5426Zinc 3PROSITE-ProRule annotation1
Metal bindingi5429Zinc 3PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1714 – 1751C4-typePROSITE-ProRule annotationAdd BLAST38
Zinc fingeri4355 – 4371By similarityAdd BLAST17
Zinc fingeri4397 – 4410By similarityAdd BLAST14
Nucleotide bindingi5636 – 5643ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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

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 ISG15 by virus, Inhibition of host NF-kappa-B 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

Protein family/group databases

MEROPSiC16.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Replicase polyprotein 1ab
Short name:
pp1ab
Alternative name(s):
ORF1ab polyprotein
Cleaved into the following 15 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
RNA-directed RNA polymerase (EC:2.7.7.48)
Short name:
Pol
Short name:
RdRp
Alternative name(s):
nsp12
Helicase (EC:3.6.4.12, EC:3.6.4.13)
Short name:
Hel
Alternative name(s):
nsp13
Alternative name(s):
nsp14
Alternative name(s):
NendoU
nsp15
Alternative name(s):
nsp16
Gene namesi
Name:rep
ORF Names:1a-1b
OrganismiBat coronavirus HKU4 (BtCoV) (BtCoV/HKU4/2004)
Taxonomic identifieri694007 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiTylonycteris pachypus (Lesser bamboo bat) [TaxID: 258959]
Proteomesi
  • UP000006574 Componenti: Genome

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
Helicase :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei2112 – 2132HelicalSequence analysisAdd BLAST21
Transmembranei2145 – 2165HelicalSequence analysisAdd BLAST21
Transmembranei2222 – 2242HelicalSequence analysisAdd BLAST21
Transmembranei2326 – 2346HelicalSequence analysisAdd BLAST21
Transmembranei2350 – 2370HelicalSequence analysisAdd BLAST21
Transmembranei2375 – 2395HelicalSequence analysisAdd BLAST21
Transmembranei2800 – 2820HelicalSequence analysisAdd BLAST21
Transmembranei3072 – 3092HelicalSequence analysisAdd BLAST21
Transmembranei3105 – 3125HelicalSequence analysisAdd BLAST21
Transmembranei3149 – 3169HelicalSequence analysisAdd BLAST21
Transmembranei3603 – 3623HelicalSequence analysisAdd BLAST21
Transmembranei3637 – 3657HelicalSequence analysisAdd BLAST21
Transmembranei3662 – 3682HelicalSequence analysisAdd BLAST21
Transmembranei3707 – 3727HelicalSequence analysisAdd BLAST21
Transmembranei3735 – 3755HelicalSequence analysisAdd BLAST21
Transmembranei3784 – 3804HelicalSequence analysisAdd BLAST21
Transmembranei3808 – 3828HelicalSequence 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_00002902881 – 195Host translation inhibitor nsp1By similarityAdd BLAST195
ChainiPRO_0000290289196 – 847Non-structural protein 2By similarityAdd BLAST652
ChainiPRO_0000290290848 – 2784Papain-like proteinaseBy similarityAdd BLAST1937
ChainiPRO_00002902912785 – 3291Non-structural protein 4By similarityAdd BLAST507
ChainiPRO_00002902923292 – 35973C-like proteinaseBy similarityAdd BLAST306
ChainiPRO_00002902933598 – 3889Non-structural protein 6By similarityAdd BLAST292
ChainiPRO_00002902943890 – 3972Non-structural protein 7By similarityAdd BLAST83
ChainiPRO_00002902953973 – 4171Non-structural protein 8By similarityAdd BLAST199
ChainiPRO_00002902964172 – 4281Non-structural protein 9By similarityAdd BLAST110
ChainiPRO_00002902974282 – 4420Non-structural protein 10By similarityAdd BLAST139
ChainiPRO_00002902984421 – 5354RNA-directed RNA polymeraseBy similarityAdd BLAST934
ChainiPRO_00002902995355 – 5952HelicaseBy similarityAdd BLAST598
ChainiPRO_00002903005953 – 6475Guanine-N7 methyltransferaseBy similarityAdd BLAST523
ChainiPRO_00002903016476 – 6817Uridylate-specific endoribonucleaseBy similarityAdd BLAST342
ChainiPRO_00002903026818 – 71192'-O-methyltransferaseBy similarityAdd BLAST302

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
Sitei195 – 196CleavageSequence analysis2
Sitei847 – 848Cleavage; by PL-PROSequence analysis2
Sitei2784 – 2785Cleavage; by PL-PROSequence analysis2
Sitei3291 – 3292Cleavage; by 3CL-PROSequence analysis2
Sitei3597 – 3598Cleavage; by 3CL-PROSequence analysis2
Sitei3889 – 3890Cleavage; by 3CL-PROSequence analysis2
Sitei3972 – 3973Cleavage; by 3CL-PROSequence analysis2
Sitei4171 – 4172Cleavage; by 3CL-PROSequence analysis2
Sitei4281 – 4282Cleavage; by 3CL-PROSequence analysis2
Sitei4420 – 4421Cleavage; by 3CL-PROSequence analysis2
Sitei5354 – 5355Cleavage; by 3CL-PROSequence analysis2
Sitei5952 – 5953Cleavage; by 3CL-PROSequence analysis2
Sitei6475 – 6476Cleavage; by 3CL-PROSequence analysis2
Sitei6817 – 6818Cleavage; by 3CL-PROSequence analysis2

Proteomic databases

PRIDEiP0C6W3.

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. Nsp10 forms a dodecamer and interacts with nsp14 and nsp16; these interactions enhance nsp14 and nsp16 enzymatic activities. Nsp14 interacts (via N-terminus) with DDX1.By similarity

Structurei

Secondary structure

17119
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3302 – 3305Combined sources4
Beta strandi3308 – 3313Combined sources6
Beta strandi3316 – 3323Combined sources8
Beta strandi3326 – 3330Combined sources5
Helixi3331 – 3334Combined sources4
Helixi3337 – 3339Combined sources3
Beta strandi3340 – 3342Combined sources3
Helixi3345 – 3351Combined sources7
Helixi3354 – 3356Combined sources3
Beta strandi3357 – 3361Combined sources5
Beta strandi3363 – 3365Combined sources3
Beta strandi3367 – 3369Combined sources3
Beta strandi3371 – 3377Combined sources7
Beta strandi3380 – 3387Combined sources8
Beta strandi3394 – 3397Combined sources4
Beta strandi3405 – 3412Combined sources8
Beta strandi3415 – 3423Combined sources9
Helixi3436 – 3438Combined sources3
Beta strandi3442 – 3447Combined sources6
Beta strandi3450 – 3462Combined sources13
Beta strandi3465 – 3469Combined sources5
Beta strandi3475 – 3478Combined sources4
Beta strandi3481 – 3484Combined sources4
Helixi3495 – 3507Combined sources13
Helixi3521 – 3530Combined sources10
Helixi3540 – 3549Combined sources10
Helixi3553 – 3565Combined sources13
Beta strandi3575 – 3577Combined sources3
Helixi3584 – 3590Combined sources7
Turni3591 – 3593Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4YO9X-ray2.30A/B3292-3597[»]
4YOGX-ray2.00A/B3292-3597[»]
4YOIX-ray1.82A/B3292-3597[»]
4YOJX-ray1.90A/B3292-3597[»]
ProteinModelPortaliP0C6W3.
SMRiP0C6W3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1152 – 1321MacroPROSITE-ProRule annotationAdd BLAST170
Domaini1593 – 1864Peptidase C16PROSITE-ProRule annotationAdd BLAST272
Domaini3292 – 3597Peptidase C30PROSITE-ProRule annotationAdd BLAST306
Domaini5034 – 5196RdRp catalyticPROSITE-ProRule annotationAdd BLAST163
Domaini5355 – 5438CV ZBDPROSITE-ProRule annotationAdd BLAST84
Domaini5611 – 5792(+)RNA virus helicase ATP-bindingAdd BLAST182
Domaini5793 – 5967(+)RNA virus helicase C-terminalAdd BLAST175

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2112 – 2395HD1By similarityAdd BLAST284
Regioni2800 – 3169HD2By similarityAdd BLAST370
Regioni3603 – 3828HD3By similarityAdd BLAST226

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi960 – 1049Glu-richAdd BLAST90
Compositional biasi4161 – 4166Poly-Ser6
Compositional biasi5359 – 5384Cys-richAdd BLAST26

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 CV ZBD (coronavirus zinc-binding) domain.PROSITE-ProRule annotation
Contains 1 Macro domain.PROSITE-ProRule annotation
Contains 1 peptidase C16 domain.PROSITE-ProRule annotation
Contains 1 peptidase C30 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1714 – 1751C4-typePROSITE-ProRule annotationAdd BLAST38
Zinc fingeri4355 – 4371By similarityAdd BLAST17
Zinc fingeri4397 – 4410By similarityAdd BLAST14

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
IPR032505. Corona_NSP4_C.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR032592. NAR_dom.
IPR009466. NSP11.
IPR024375. Nsp3_coronavir.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR027417. P-loop_NTPase.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR009003. Peptidase_S1_PA.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009469. RNA_pol_N_coronovir.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases.
IPR014827. Viral_protease.
[Graphical view]
PfamiPF16348. Corona_NSP4_C. 1 hit.
PF06478. Corona_RPol_N. 1 hit.
PF01661. Macro. 1 hit.
PF16251. NAR. 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.
PF00680. RdRP_1. 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.
SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51653. CV_ZBD. 1 hit.
PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 1 hit.
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. AlignAdd to basket

Isoform Replicase polyprotein 1ab (identifier: P0C6W3-1) [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

        10         20         30         40         50
MLSKASVTTQ GARGKYRAEL YNEKRSDHVA CTVPLCDTDD MACKLTPWFE
60 70 80 90 100
DGETAFNQVS SILKEKGKIL FVPMHMQRAM KFLPGPRVYL VERLTGGMLS
110 120 130 140 150
KHFLVNQLAY KDQVGAAMMR TTLNAKPLGM FFPYDSSLET GEYTFLLRKN
160 170 180 190 200
GLGGQLFRER PWDRKETPYV EILDDLEADP TGKYSQNLLK KLIGGDCIPI
210 220 230 240 250
DQYMCGKNGK PIADYAKIVA KEGLTTLADI EVDVKSRMDS DRFIVLNKKL
260 270 280 290 300
YRVVWNVTRR NVPYPKQTAF TIVSVVQCDD KDSVPEHTFT IGSQILMVSP
310 320 330 340 350
LKATNNKNFN LKQRLLYTFY GKDAVQQPGY IYHSAYVDCN ACGRGTWCTG
360 370 380 390 400
NAIQGFACDC GANYSANDVD LQSSGLVPRN ALFLANCPCA NNGACSHSAA
410 420 430 440 450
QVYNILDGKA CVEVGGKSFT LTFGGVVYAY MGCCDGTMYF VPRAKSCVSR
460 470 480 490 500
IGDAIFTGCT GTWDKVVETA NLFLEKAQRS LNFCQQFALT EVVLAILSGT
510 520 530 540 550
TSTFEELRDL CHNASYEKVR DHLVNHGFVV TIGDYIRDAI NIGANGVCNA
560 570 580 590 600
TINAPFIAFT GLGESFKKVS AIPWKICSNL KSALDYYSSN IMFRVFPYDI
610 620 630 640 650
PCDVSNFVEL LLDCGKLTVA TSYFVLRYLD EKFDTVLGTV SSACQTALSS
660 670 680 690 700
FLNACVAASR ATAGFINDMF KLFKVLMHKL YVYTSCGYVA VAEHSSKIVQ
710 720 730 740 750
QVLDIMSKAM KLLHTNVSWA GTKLSAIIYE GREALLFNSG TYFCLSTKAK
760 770 780 790 800
TLQGQMNLVL PGDYNKKTLG ILDPVPNADT IDVNANSTVV DVVHGQLEPT
810 820 830 840 850
NEHGPSMIVG NYVLVSDKLF VRTEDEEFYP LCTNGKVVST LFRLKGGMPS
860 870 880 890 900
KKVTFGDVNT VEVTAYRSVS ITYDIHPVLD ALLSSSKLAT FTVEKDLLVE
910 920 930 940 950
DFVDVIKDEV LTLLTPLLRG YDIDGFDVED FIDVPCYVYN QDGDCAWSSN
960 970 980 990 1000
MTFSINPVED VEEVEEFIED DYLSDELPIA DDEEAWARAV EEVMPLDDIL
1010 1020 1030 1040 1050
VAEIELEEDP PLETALESVE AEVVETAEAQ EPSVESIDST PSTSTVVGEN
1060 1070 1080 1090 1100
DLSVKPMSRV AETDDVLELE TAVVGGPVSD VTAIVTNDIV SVEQAQQCGV
1110 1120 1130 1140 1150
SSLPIQDEAS ENQVHQVSDL QGNELLCSET KVEIVQPRQD LKPRRSRKSK
1160 1170 1180 1190 1200
VDLSKYKHTV INNSVTLVLG DAIQIASLLP KCILVNAANR HLKHGGGIAG
1210 1220 1230 1240 1250
VINKASGGDV QEESDEYISN NGPLHVGDSV LLKGHGLADA ILHVVGPDAR
1260 1270 1280 1290 1300
NNEDAALLKR CYKAFNKHTI VVTPLISAGI FSVDPKVSFE YLLANVTTTT
1310 1320 1330 1340 1350
YVVVNNEDIY NTLATPSKPD GLVYSFEGWR GTVRTAKNYG FTCFICTEYS
1360 1370 1380 1390 1400
ANVKFLRTKG VDTTKKIQTV DGVSYYLYSA RDALTDVIAA ANGCSGICAM
1410 1420 1430 1440 1450
PFGYVTHGLD LAQSGNYVRQ VKVPYVCLLA SKEQIPIMNS DVAIQTPETA
1460 1470 1480 1490 1500
FINNVTSNGG YHSWHLVSGD LIVKDVCYKK LLHWSGQTIC YADNKFYVVK
1510 1520 1530 1540 1550
NDVALPFSDL EACRAYLTSR AAQQVNIEVL VTIDGVNFRT VILNDTTTFR
1560 1570 1580 1590 1600
KQLGATFYKG VDISDAFPTV KMGGESLFVA DNLSESEKVV LKEYYGTSDV
1610 1620 1630 1640 1650
TFLQRYYSLQ PLVQQWKFVV HDGVKSLKLS NYNCYINATI MMIDMLHDIK
1660 1670 1680 1690 1700
FVVPALQNAY LRYKGGDPYD FLALIMAYGD CTFDNPDDEA KLLHTLLAKA
1710 1720 1730 1740 1750
ELTVSAKMVW REWCTVCGIR DIEYTGMRAC VYAGVNSMEE LQSVFNETCV
1760 1770 1780 1790 1800
CGSVKHRQLV EHSAPWLLVS GLNEVKVSTS TDPIYRAFNV FQGVETSVGH
1810 1820 1830 1840 1850
YVHIRVKDGL FYKYDSGSLT KTSDMKCKMT SVWYPTVRYT ADCNVVVYDL
1860 1870 1880 1890 1900
DGVTKVEVNP DLSNYYMKDG KYYTSKPTIK YSPATILPGS VYSNSCLVGV
1910 1920 1930 1940 1950
DGTPGSDTIS KFFNDLLGFD ETKPISKKLT YSLLPNEDGD VLLSEFSNYN
1960 1970 1980 1990 2000
PVYKKGVMLK GKPILWVNNG VCDSALNKPN RASLRQLYDV APIVLDNKYT
2010 2020 2030 2040 2050
VLQDNTSQLV EHNVPVVDDV PITTRKLIEV KCKGLNKPFV KGNFSFVNDP
2060 2070 2080 2090 2100
NGVTVVDTLG LTELRALYVD INTRYIVLRD NNWSSLFKLH TVESGDLQIV
2110 2120 2130 2140 2150
AAGGSVTRRA RVLLGASSLF ASFAKITVTA TTAACKTAGR GFCKFVVNYG
2160 2170 2180 2190 2200
VLQNMFVFLK MLFFLPFNYL WPKKQPTVDI GVSGLRTAGI VTTNIVKQCG
2210 2220 2230 2240 2250
TAAYYMLLGK FKRVDWKATL RLFLLLCTTI LLLSSIYHLV LFNQVLSSDV
2260 2270 2280 2290 2300
MLEDATGILA IYKEVRSYLG IRTLCDGLVV EYRNTSFDVM EFCSNRSVLC
2310 2320 2330 2340 2350
QWCLIGQDSL TRYSALQMLQ THITSYVLNI DWIWFALEFF LAYVLYTSSF
2360 2370 2380 2390 2400
NVLLLVVTAQ YFFAYTSAFV NWRAYNYIVS GLFFLVTHIP LHGLVRVYNF
2410 2420 2430 2440 2450
LACLWFLRKF YSHVINGCKD TACLLCYKRN RLTRVEASTI VCGTKRTFYI
2460 2470 2480 2490 2500
AANGGTSYCC KHNWNCVECD TAGVGNTFIC TEVANDLTTT LRRLIKPTDQ
2510 2520 2530 2540 2550
SHYYVDSVVV KDAVVELHYN RDGSSCYERY PLCYFTNLEK LKFKEVCKTP
2560 2570 2580 2590 2600
TGIPEHNFLI YDTNDRGQEN LARSACVYYS QVLCKPMLLV DVNLVTTVGD
2610 2620 2630 2640 2650
SREIAIKMLD SFINSFISLF SVSRDKLEKL INTARDCVRR GDDFQNVLKT
2660 2670 2680 2690 2700
FTDAARGHAG VESDVETTMV VDALQYAHKN DIQLTTECYN NYVPGYIKPD
2710 2720 2730 2740 2750
SINTLDLGCL IDLKAASVNQ TSMRNANGAC VWNSGDYMKL SDSFKRQIRI
2760 2770 2780 2790 2800
ACRKCNIPFR LTTSKLRAAD NILSVKFSAT KIVGGAPSWL LRVRDLTVKG
2810 2820 2830 2840 2850
YCILTLFVFT VAVLSWFCLP SYSIATVNFN DDRILTYKVI ENGIVRDIAP
2860 2870 2880 2890 2900
NDVCFANKYG HFSKWFNENH GGVYRNSMDC PITIAVIAGV AGARVANVPA
2910 2920 2930 2940 2950
NLAWVGKQIV LFVSRVFANT NVCFTPINEI PYDTFSDSGC VLSSECTLFR
2960 2970 2980 2990 3000
DAEGNLNPFC YDPTVLPGAS SYADMKPHVR YDMYDSDMYI KFPEVIVEST
3010 3020 3030 3040 3050
LRITKTLATQ YCRFGSCEES AAGVCISTNG SWALYNQNYS TRPGIYCGDD
3060 3070 3080 3090 3100
YFDIVRRLAI SLFQPVTYFQ LSTSLAMGLV LCVFLTAAFY YINKVKRALA
3110 3120 3130 3140 3150
DYTQCAVVAV VAALLNSLCL CFIVANPLLV APYTAMYYYA TFYLTGEPAF
3160 3170 3180 3190 3200
IMHISWYVMF GAVVPIWMLA SYTVGVMLRH LFWVLAYFSK KHVDVFTDGK
3210 3220 3230 3240 3250
LNCSFQDAAS NIFVIGKDTY VALRNAITQD SFVRYLSLFN KYKYYSGAMD
3260 3270 3280 3290 3300
TASYREACAA HLCKALQTYS ETGSDILYQP PNCSVTSSVL QSGLVKMSAP
3310 3320 3330 3340 3350
SGAVENCIVQ VTCGSMTLNG LWLDNTVWCP RHIMCPADQL TDPNYDALLI
3360 3370 3380 3390 3400
SKTNHSFIVQ KHIGAQANLR VVAHSMVGVL LKLTVDVANP STPAYTFSTV
3410 3420 3430 3440 3450
KPGASFSVLA CYNGKPTGVF TVNLRHNSTI KGSFLCGSCG SVGYTENGGV
3460 3470 3480 3490 3500
INFVYMHQME LSNGTHTGSS FDGVMYGAFE DKQTHQLQLT DKYCTINVVA
3510 3520 3530 3540 3550
WLYAAVLNGC KWFVKPTRVG IVTYNEWALS NQFTEFVGTQ SIDMLAHRTG
3560 3570 3580 3590 3600
VSVEQMLAAI QSLHAGFQGK TILGQSTLED EFTPDDVNMQ VMGVVMQSGV
3610 3620 3630 3640 3650
KRISYGFIHW LISTFVLAYV SVMQLTKFTM WTYLFETIPT QMTPLLLGFM
3660 3670 3680 3690 3700
ACVMFTVKHK HTFMSLFLLP VALCLTYANI VYEPQTLISS TLIAVANWLT
3710 3720 3730 3740 3750
PTSVYMRTTH FDFGLYISLS FVLAIIVRRL YRPSMSNLAL ALCSGVMWFY
3760 3770 3780 3790 3800
TYVIGDHSSP ITYLMFITTL TSDYTITVFA TVNLAKFISG LVFFYAPHLG
3810 3820 3830 3840 3850
FILPEVKLVL LIYLGLGYMC TMYFGVFSLL NLKLRVPLGV YDYSVSTQEF
3860 3870 3880 3890 3900
RFLTGNGLHA PRNSWEALIL NFKLLGIGGT PCIKVATVQS KLTDLKCTSV
3910 3920 3930 3940 3950
VLLTVLQQLH LESNSKAWSY CVKLHNEILA AVDPTEAFER FVCLFATLMS
3960 3970 3980 3990 4000
FSANVDLDAL ANDLFENSSV LQATLTEFSH LATYAELETA QSSYQKALNS
4010 4020 4030 4040 4050
GDASPQVLKA LQKAVNVAKN AYEKDKAVAR KLERMAEQAM TSMYKQARAE
4060 4070 4080 4090 4100
DKKAKIVSAM QTMLFGMIKK LDNDVLNGVI ANARNGCVPL SIVPLCASNK
4110 4120 4130 4140 4150
LRVVIPDISV WNKVVNWPSV SYAGSLWDIT VINNVDNEVV KPTDVVETNE
4160 4170 4180 4190 4200
SLTWPLVIEC SRSSSSAVKL QNNEIHPKGL KTMVITAGVD QVNCNSSAVA
4210 4220 4230 4240 4250
YYEPVQGHRM VMGLLSENAH LKWAKVEGKD GFINIELQPP CKFLIAGPKG
4260 4270 4280 4290 4300
PEIRYLYFVK NLNNLHRGQL LGHIAATVRL QAGANTEFAS NSTVLTLVAF
4310 4320 4330 4340 4350
AVDPAKAYLD YVGSGGTPLS NYVKMLAPKT GTGVAISVKP EATADQETYG
4360 4370 4380 4390 4400
GASVCLYCRA HIEHPDVSGV CKYKTRFVQI PAHVRDPVGF LLKNVPCNVC
4410 4420 4430 4440 4450
QYWVGYGCNC DALRNNTVPQ SKDTNFLNRV RGSSVNARLE PCSSGLTTDV
4460 4470 4480 4490 4500
VYRAFDICNF KARVAGIGKY YKTNTCRFVQ VDDEGHKLDS YFIVKRHTMS
4510 4520 4530 4540 4550
NYELEKRCYD LLKDCDAVAI HDFFIFDVDK TKTPHIVRQS LTEYTMMDLV
4560 4570 4580 4590 4600
YALRHFDQNN CEVLKSILVK YGCCEQSYFD NKLWFDFVEN PSVIGVYHKL
4610 4620 4630 4640 4650
GERIRQAMLN TVKMCDHMVK SGLVGVLTLD NQDLNGKWYD FGDFVITQPG
4660 4670 4680 4690 4700
AGVAIVDSYY SYLMPVLSMT NCLAAETHKD CDFNKPLIEW PLLEYDYTDY
4710 4720 4730 4740 4750
KIGLFNKYFK YWDQTYHPNC VNCSDDRCIL HCANFNVLFS MVLPNTSFGP
4760 4770 4780 4790 4800
IVRKIFVDGV PFIVSCGYHY KELGLVMNMD FNIHRHRLAL KELMMYAADP
4810 4820 4830 4840 4850
AMHIASASAL WDLRTPCFSV AALTTGLTFQ TVRPGNFNKD FYDFVVSRGF
4860 4870 4880 4890 4900
FKEGSSVTLK HFFFAQDGHA AITDYSYYAY NLPTMVDIKQ MLFCMEVVDK
4910 4920 4930 4940 4950
YFDIYDGGCL NASEVIVNNL DKSAGHPFNK FGKARVYYES MSYQEQDELF
4960 4970 4980 4990 5000
AVTKRNVLPT ITQMNLKYAI SAKNRARTVA GVSILSTMTN RQYHQKMLKS
5010 5020 5030 5040 5050
MAATRGATCV IGTTKFYGGW DFMLKTLYKD VESPHLMGWD YPKCDRAMPN
5060 5070 5080 5090 5100
MCRILASLIL ARKHSTCCTN SDRFYRLANE CAQVLSEYVL CGGGYYVKPG
5110 5120 5130 5140 5150
GTSSGDATTA YANSVFNILQ ATTANVSALM SANGNTIIDR EIKDMQFDLY
5160 5170 5180 5190 5200
INVYRKVVPD PKFVDKYYAF LNKHFSMMIL SDDGVVCYNS DYAAKGYVAS
5210 5220 5230 5240 5250
IQNFKETLYY QNNVFMSEAK CWVETNLEKG PHEFCSQHTL YIKDGDDGYF
5260 5270 5280 5290 5300
LPYPDPSRIL SAGCFVDDIV KTDGTVMMER YVSLAIDAYP LTKHDDTEYQ
5310 5320 5330 5340 5350
NVFWVYLQYI EKLYKDLTGH MLDSYSVMLC GDDSAKFWEE GFYRDLYSSP
5360 5370 5380 5390 5400
TTLQAVGSCV VCHSQTSLRC GTCIRRPFLC CKCCYDHVIA TPHKMVLSVS
5410 5420 5430 5440 5450
PYVCNAPGCD VSDVTKLYLG GMSYYCNDHR PVCSFPLCAN GLVFGLYKNM
5460 5470 5480 5490 5500
CTGSSSIMEF NRLATCDWSD SGDYTLANTT TEPLKLFAAE TLRATEEASK
5510 5520 5530 5540 5550
QSYAIATIKE IVGERELILV WEVGKSKPPL NRNYVFTGYH LTKNSKVQLG
5560 5570 5580 5590 5600
EYVFERIDYS DAVSYKSSTT YKLAVGDIFV LTSHSVATLS APTIVNQERY
5610 5620 5630 5640 5650
LKITGIYPTI TVPEEFANHV VNFQKAGFSK YVTVQGPPGT GKSHFAIGLA
5660 5670 5680 5690 5700
IYYPTARIVY TACSHAAVDA LCEKAFKYLN IAKCSRIIPA KARVECYDRF
5710 5720 5730 5740 5750
KVNDTNSQYL FSTVNALPEI SVDILVVDEV SMCTNYDLSI INSRVKAKHI
5760 5770 5780 5790 5800
VYVGDPAQLP APRTLLIRGT LEPENFNSVT RLMCNLGPDI FLSVCYRCPK
5810 5820 5830 5840 5850
EIVSTVSALV YNNKLSAKKD ASGQCFKILF KGSVTHDASS AINRPQLNFV
5860 5870 5880 5890 5900
KTFIAANPNW SKAVFISPYN SQNAVARSML GLTTQTVDSS QGSEYPYVIF
5910 5920 5930 5940 5950
CQTADTAHAN NLNRFNVAVT RAQKGILCVM TSQVLFDSLE FAELSLNNYK
5960 5970 5980 5990 6000
LQSQIVTGLF KDCSREDTGL PPAYAPTYLS VDAKYKTTDE LCVNLNITPN
6010 6020 6030 6040 6050
VTYSRVISRM GFKLDATIPG YPKLFITRDE AIRQVRSWVG FDVEGAHASR
6060 6070 6080 6090 6100
NACGTNVPLQ LGFSTGVNFV VQPVGVVDTE WGSMLTTISA RPPPGEQFKH
6110 6120 6130 6140 6150
LVPLMNKGAT WPIVRRRIVQ MLSDTLDKLS DYCTFVCWAH GFELTSASYF
6160 6170 6180 6190 6200
CKIGKEQRCS MCSRRASTFS SPLQSYACWS HSSGYDYVYN PFFVDVQQWG
6210 6220 6230 6240 6250
YVGNLATNHD RYCGIHAGAH VASSDAIMTR CLAIYDCFIE RVDWDVTYPY
6260 6270 6280 6290 6300
ISHEQKLNSC CRTVERNVVR SAVLSGKFEK IYDIGNPKGI AIISEPVEWH
6310 6320 6330 6340 6350
FYDAQPLSNK VKKLFYTDDV SKQFEDGLCL FWNCNVSKYP SNAVVCRFDT
6360 6370 6380 6390 6400
RVHSEFNLPG CNGGSLYVNK HAFHTPAYDI NAFRDLKPLP FFYYSTTPCE
6410 6420 6430 6440 6450
VHGSGNMLED IDYVPLKSAV CITACNLGGA VCRKHAAEYR DYMEAYNIVS
6460 6470 6480 6490 6500
AAGFRLWVYK TFDIYNLWST FVKVQGLENI AFNVIKQGHF TGVDGELPVA
6510 6520 6530 6540 6550
VVNDKIFTKN GTDDVCIFKN ETALPTNVAF ELYAKRAVRS HPDLNLLRNL
6560 6570 6580 6590 6600
EVDVCYNFVL WDYDRNNIYG TTTIGVCKYT DIDVNPNLNM CFDIRDKGSL
6610 6620 6630 6640 6650
ERFMSMPNGV LISDRKIKNY PCISGPKHAY FNGAILRNID AKQPVIFYLY
6660 6670 6680 6690 6700
KKVNNEFVSF SDTFYTCGRT VGDFTVLTPM EEDFLVLDSD VFIKKYGLED
6710 6720 6730 6740 6750
YAFEHVVYGD FSHTTLGGLH LLIGLYKKMR EGHILMEEML KDRATVHNYF
6760 6770 6780 6790 6800
ITDSNTASYK AVCSVIDLRL DDFVTIIKEM DLDVVSKVVK VPIDLTMIEF
6810 6820 6830 6840 6850
MLWCRDGKVQ TFYPRLQATN DWKPGLTMPS LFKVQQMNLE PCLLANYKQS
6860 6870 6880 6890 6900
IPMPNGVHMN VAKYMQLCQY LNTCTLAVPA NMRVIHFGAG CEKGVAPGTS
6910 6920 6930 6940 6950
VLRQWLPLDA VLIDNDLNEF VSDADITIFG DCVTVHVGQQ VDLLISDMYD
6960 6970 6980 6990 7000
PCTKAVGEVN QTKALFFVYL CNFIKNNLAL GGSVAIKITE HSWSADLYKI
7010 7020 7030 7040 7050
MGRFAYWTVF CTNANASSSE GFLIGINFLG ELKEEIDGNV MHANYIFWRN
7060 7070 7080 7090 7100
STPMNLSTYS LFDLSRFPLK LKGTPVLQLK ESQINELVIS LLSQGKLLIR
7110
DNDTLNVSTD VLVNFRKRL
Note: Produced by -1 ribosomal frameshifting at the 1a-1b genes boundary.
Length:7,119
Mass (Da):795,200
Last modified:June 10, 2008 - v1
Checksum:iE85475854586DD79
GO
Isoform Replicase polyprotein 1a (identifier: P0C6T4-1) [UniParc]FASTAAdd to basket
Also known as: pp1a, ORF1a polyprotein
The sequence of this isoform can be found in the external entry P0C6T4.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.
Length:4,434
Mass (Da):491,823
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF065505 Genomic RNA. Translation: ABN10838.1.
RefSeqiYP_001039952.1. NC_009019.1. [P0C6W3-1]

Genome annotation databases

GeneIDi4835998.
KEGGivg:4835998.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EF065505 Genomic RNA. Translation: ABN10838.1.
RefSeqiYP_001039952.1. NC_009019.1. [P0C6W3-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4YO9X-ray2.30A/B3292-3597[»]
4YOGX-ray2.00A/B3292-3597[»]
4YOIX-ray1.82A/B3292-3597[»]
4YOJX-ray1.90A/B3292-3597[»]
ProteinModelPortaliP0C6W3.
SMRiP0C6W3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC16.011.

Proteomic databases

PRIDEiP0C6W3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi4835998.
KEGGivg:4835998.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR027351. (+)RNA_virus_helicase_core_dom.
IPR032505. Corona_NSP4_C.
IPR009461. Coronavirus_NSP16.
IPR027352. CV_MBD_dom.
IPR002589. Macro_dom.
IPR032592. NAR_dom.
IPR009466. NSP11.
IPR024375. Nsp3_coronavir.
IPR014828. NSP7.
IPR014829. NSP8.
IPR014822. NSP9.
IPR027417. P-loop_NTPase.
IPR008740. Peptidase_C30.
IPR013016. Peptidase_C30/C16.
IPR009003. Peptidase_S1_PA.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009469. RNA_pol_N_coronovir.
IPR018995. RNA_synth_NSP10_coronavirus.
IPR029063. SAM-dependent_MTases.
IPR014827. Viral_protease.
[Graphical view]
PfamiPF16348. Corona_NSP4_C. 1 hit.
PF06478. Corona_RPol_N. 1 hit.
PF01661. Macro. 1 hit.
PF16251. NAR. 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.
PF00680. RdRP_1. 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.
SSF52540. SSF52540. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51653. CV_ZBD. 1 hit.
PS51442. M_PRO. 1 hit.
PS51154. MACRO. 1 hit.
PS51124. PEPTIDASE_C16. 1 hit.
PS51657. PSRV_HELICASE. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiR1AB_BCHK4
AccessioniPrimary (citable) accession number: P0C6W3
Secondary accession number(s): A3EX93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: November 30, 2016
This is version 69 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. 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.