Non-structural polyprotein

Functionⁱ

P123 is short-lived polyproteins, accumulating during early stage of infection. It localizes the viral replication complex to the cytoplasmic surface of modified endosomes and lysosomes. By interacting with nsP4, it starts viral genome replication into antigenome. After these early events, P123 is cleaved sequentially into nsP1, nsP2 and nsP3. This sequence of delayed processing would allow correct assembly and membrane association of the RNA polymerase complex (By similarity).By similarity

nsP1 is a cytoplasmic capping enzyme. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and nsP1, whereas eukaryotic capping enzymes form a covalent complex only with GMP. nsP1 capping would consist in the following reactions: GTP is first methylated and then forms the m7GMp-nsP1 complex, from which 7-methyl-GMP complex is transferred to the mRNA to create the cap structure. Palmitoylated nsP1 is remodeling host cell cytoskeleton, and induces filopodium-like structure formation at the surface of the host cell (By similarity).By similarity

nsP2 has two separate domain with different biological activities. The N-terminal section is part of the RNA polymerase complex and has RNA trisphosphatase and RNA helicase activity. The C-terminal section harbors a protease that specifically cleaves and releases the four mature proteins. Also inhibits cellular transcription by inducing rapid degradation of POLR2A, a catalytic subunit of the RNAPII complex. The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).By similarity

nsP3 is essential for minus strand and subgenomic 26S mRNA synthesis.By similarity

nsP4 is an RNA dependent RNA polymerase. It replicates genomic and antigenomic RNA by recognizing replications specific signals. Transcribes also a 26S subgenomic mRNA by initiating RNA synthesis internally on antigenomic RNA. This 26S mRNA codes for structural proteins (By similarity).By similarity

Caution

There is no stop codon readthrough before nsP4.Curated

Catalytic activityⁱ

S-adenosyl-L-methionine + GTP = m₇GTP.

m7GTP + [nsP1 protein] = m7GMP-[nsP1 protein] + diphosphate.

m7GMP-[nsP1 protein] + (5')pp-Pur-mRNA = m₇G(5')ppp-Pur-mRNA + [nsP1 protein].

(5')ppp-mRNA + H₂O = (5')pp-mRNA + phosphate.

A 5'-phosphopolynucleotide + H₂O = a polynucleotide + phosphate.

NTP + H₂O = NDP + phosphate.

ATP + H₂O = ADP + phosphate.

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	1013	For cysteine protease nsP2 activityPROSITE-ProRule annotation		1
Active siteⁱ	1083	For cysteine protease nsP2 activityPROSITE-ProRule annotation		1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	721 – 728	ATPSequence analysis		8

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
cysteine-type peptidase activity Source: UniProtKB-KW
GTP binding Source: UniProtKB-KW
helicase activity Source: UniProtKB-KW
mRNA methyltransferase activity Source: InterPro
polynucleotide 5'-phosphatase activity Source: UniProtKB-EC
RNA binding Source: UniProtKB-KW
RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

7-methylguanosine mRNA capping Source: UniProtKB-KW
suppression by virus of host RNA polymerase II activity Source: UniProtKB-KW
transcription, DNA-templated Source: InterPro
viral RNA genome replication Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Helicase, Hydrolase, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase
Biological process	Eukaryotic host gene expression shutoff by virus, Eukaryotic host transcription shutoff by virus, Host gene expression shutoff by virus, Host-virus interaction, Inhibition of host RNA polymerase II by virus, mRNA capping, mRNA processing, Viral RNA replication
Ligand	ATP-binding, GTP-binding, Nucleotide-binding, S-adenosyl-L-methionine

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Non-structural polyprotein Alternative name(s): Polyprotein nsP1234 Short name: P1234 Cleaved into the following 5 chains: P123 mRNA-capping enzyme nsP1 (EC:2.1.1.-, EC:2.7.7.-) Alternative name(s): Non-structural protein 1 Protease nsP2 (EC:3.1.3.33, EC:3.4.22.-, EC:3.6.1.15, EC:3.6.4.13) Alternative name(s): Non-structural protein 2 Short name: nsP2 Non-structural protein 3 Short name: nsP3 RNA-directed RNA polymerase nsP4 (EC:2.7.7.48) Alternative name(s): Non-structural protein 4 Short name: nsP4
Organismⁱ	Chikungunya virus (strain 37997) (CHIKV)
Taxonomic identifierⁱ	371095 [NCBI]
Taxonomic lineageⁱ	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Togaviridae › Alphavirus › Chikungunya virus
Virus hostⁱ	Aedes aegypti (Yellowfever mosquito) (Culex aegypti) [TaxID: 7159] Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta) [TaxID: 7160] Aedes furcifer (Mosquito) [TaxID: 299627] Aedes polynesiensis (Polynesian tiger mosquito) [TaxID: 188700] Cercopithecus [TaxID: 9533] Homo sapiens (Human) [TaxID: 9606] Macaca (macaques) [TaxID: 9539] Pan troglodytes (Chimpanzee) [TaxID: 9598] Papio (baboons) [TaxID: 9554] Presbytis [TaxID: 9573]
Proteomesⁱ	UP000008450 Componentⁱ: Genome

Subcellular locationⁱ

Non-structural polyprotein :

Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

Note:

Located on the cytoplasmic surface of modified endosomes and lysosomes, also called cytopathic vacuoles type I (CPVI). These vacuoles contain numerous small circular invaginations (spherules) which may be the sites of RNA synthesis.

P123 :

Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

mRNA-capping enzyme nsP1 :

Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Host cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

Note:

In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then a fraction of nsP1 localizes to the inner surface of the plasma membrane (By similarity).By similarity

Protease nsP2 :

Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Host nucleus By similarity

Note:

In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then approximately half of nsP2 is found in the nucleus (By similarity).By similarity

Non-structural protein 3 :

Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Host cytoplasm By similarity

Note:

In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' seems to aggregate in cytoplasm (By similarity).By similarity

RNA-directed RNA polymerase nsP4 :

Host endosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Host lysosome membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

GO - Cellular componentⁱ

host cell endosome membrane Source: UniProtKB-SubCell
host cell lysosomal membrane Source: UniProtKB-SubCell
host cell nucleus Source: UniProtKB-SubCell
host cell plasma membrane Source: UniProtKB-SubCell
membrane Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Host cell membrane, Host cytoplasm, Host endosome, Host lysosome, Host membrane, Host nucleus, Membrane

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
ChainⁱPRO_0000308396	1 – 2474	Non-structural polyproteinAdd BLAST	2474
ChainⁱPRO_0000227765	1 – 1863	P123By similarityAdd BLAST	1863
ChainⁱPRO_0000227766	1 – 535	mRNA-capping enzyme nsP1By similarityAdd BLAST	535
ChainⁱPRO_0000227767	536 – 1333	Protease nsP2By similarityAdd BLAST	798
ChainⁱPRO_0000227768	1334 – 1863	Non-structural protein 3By similarityAdd BLAST	530
ChainⁱPRO_0000227769	1864 – 2474	RNA-directed RNA polymerase nsP4By similarityAdd BLAST	611

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Lipidationⁱ	417	S-palmitoyl cysteine; by hostBy similarity		1
Lipidationⁱ	419	S-palmitoyl cysteine; by hostBy similarity		1

Post-translational modificationⁱ

Specific enzymatic cleavages in vivo yield mature proteins. The polyprotein is synthesized as P1234 by stop codon readthrough. This polyprotein is processed differently depending on the stage of infection. In early stages, P1234 is first cleaved in trans, through its nsP2 protease activity, releasing P123 and nsP4. P123 and nsP4 start to replicate the viral genome into its antigenome. After these early events, nsP1 is cleaved in cis by nsP2 protease, releasing P23 polyprotein. Cleavage of nsP1 exposes an 'activator' at the N-terminus of P23 which induces its cleavage into nsP2 and nsP3 by the viral protease. This sequence of delayed processing would allow correct assembly and membrane association of the RNA-polymerase complex. In the late stage of infection, the presence of free nsP2 in the cytoplasm cleaves P1234 quickly into P12 and P34, then into the four nsP (By similarity).By similarity

nsP1 is palmitoylated by host.By similarity

nsP4 is ubiquitinated; targets the protein for rapid degradation via the ubiquitin system.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	535 – 536	Cleavage; by nsP2By similarity	2
Siteⁱ	1333 – 1334	Cleavage; by nsP2By similarity	2
Siteⁱ	1863 – 1864	Cleavage; by nsP2By similarity	2

Keywords - PTMⁱ

Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEⁱ	Q5XXP4

PRIDEⁱ

Q5XXP4

Expressionⁱ

Inductionⁱ

Viral replication produces dsRNA in the late phsae of infection, resulting in a strong activation of host EIF2AK2/PKR, leading to almost complete phosphorylation of EIF2A. This inactivates completely cellular translation initiation, resulting in a dramatic shutoff of proteins synthesis. Translation of viral non-structural polyprotein and all cellular proteins are stopped in infected cell between 2 and 4 hours post infection. Only the 26S mRNA is still translated into viral structural proteins, presumably through a unique mechanism of enhancer element which counteract the translation inhibition mediated by EIF2A. By doing this, the virus uses the cellular defense for its own advantage: shutoff of cellular translation allows to produce big amounts of structural proteins needed for the virus to bud out of the doomed cell.

Interactionⁱ

Subunit structureⁱ

P123 interacts with nsP4; nsP1, nsP2, nsP3 and nsP4 interact with each other, and with uncharacterized host factors.By similarity

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q5XXP4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	28 – 259	Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST	232
Domainⁱ	690 – 842	(+)RNA virus helicase ATP-bindingAdd BLAST	153
Domainⁱ	843 – 991	(+)RNA virus helicase C-terminalAdd BLAST	149
Domainⁱ	1004 – 1327	Peptidase C9PROSITE-ProRule annotationAdd BLAST	324
Domainⁱ	1334 – 1493	MacroPROSITE-ProRule annotationAdd BLAST	160
Domainⁱ	2228 – 2343	RdRp catalyticPROSITE-ProRule annotationAdd BLAST	116

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	244 – 263	nsP1 membrane-bindingBy similarityAdd BLAST		20
Regionⁱ	1005 – 1024	Nucleolus localization signalBy similarityAdd BLAST		20

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	1182 – 1186	Nuclear localization signalBy similarity		5

Phylogenomic databases

Database of Orthologous Groups More...OrthoDBⁱ	VOG09000007

OrthoDBⁱ

VOG09000007

Family and domain databases

InterProⁱ	View protein in InterPro IPR027351 (+)RNA_virus_helicase_core_dom IPR002588 Alphavirus-like_MT_dom IPR002620 Alphavirus_nsp2pro IPR002589 Macro_dom IPR027417 P-loop_NTPase IPR007094 RNA-dir_pol_PSvirus IPR001788 Tymovirus_RNA-dep_RNA_pol
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01661 Macro, 1 hit PF01707 Peptidase_C9, 1 hit PF00978 RdRP_2, 1 hit PF01443 Viral_helicase1, 1 hit PF01660 Vmethyltransf, 1 hit
SMARTⁱ	View protein in SMART SM00506 A1pp, 1 hit
SUPFAMⁱ	SSF52540 SSF52540, 1 hit
PROSITEⁱ	View protein in PROSITE PS51743 ALPHAVIRUS_MT, 1 hit PS51154 MACRO, 1 hit PS51520 NSP2PRO, 1 hit PS51657 PSRV_HELICASE, 1 hit PS50507 RDRP_SSRNA_POS, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

Q5XXP4-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MDPVYVDIDA DSAFLKALQR AYPMFEVEPR QVTPNDHANA RAFSHLAIKL 
        60         70         80         90        100
IEQEIDPDST ILDIGSAPAR RMMSDRKYHC VCPMRSAEDP ERLANYARKL 
       110        120        130        140        150
ASAAGKVLDR NISEKIGDLQ AVMAVPDAET PTFCLHTDVS CRQRADVAIY 
       160        170        180        190        200
QDVYAVHAPT SLYHQAIKGV RVAYWIGFDT TPFMYNAMAG AYPSYSTNWA 
       210        220        230        240        250
DEQVLKAKNI GLCSTDLTEG RRGKLSIMRG KKMKPCDRVL FSVGSTLYPE 
       260        270        280        290        300
SRKLLKSWHL PSVFHLKGKL SFTCRCDTVV SCEGYVVKRI TISPGLYGKT 
       310        320        330        340        350
TGYAVTHHAD GFLMCKTTDT VDGERVSFSV CTYVPATICD QMTGILATEV 
       360        370        380        390        400
TPEDAQKLLV GLNQRIVVNG RTQRNTNTMK NYLLPVVAQA FSKWAKECRK 
       410        420        430        440        450
DMEDEKLLGI RERTLTCCCL WAFKKQKTHT VYKRPDTQSI QKVPAEFDSF 
       460        470        480        490        500
VVPSLWSSGL SIPLRTRIKW LLSKVPKTDL IPYSGDAKEA RDAEKEAEEE 
       510        520        530        540        550
REAELTREAL PPLQAAQDDV QVEIDVEQLE DRAGAGIIET PRGAIKVTAQ 
       560        570        580        590        600
PTDHVVGEYL VLSPQTVLRS QKLSLIHALA EQVKTCTHSG RAGRYAVEAY 
       610        620        630        640        650
DGRILVPSGY AISPEDFQSL SESATMVYNE REFVNRKLHH IALHGPALNT 
       660        670        680        690        700
DEESYELVRA ERTEHEYVYD VDQRRCCKKE EAAGLVLVGD LTNPPYHEFA 
       710        720        730        740        750
YEGLRIRPAC PYKTAVIGVF GVPGSGKSAI IKNLVTRQDL VTSGKKENCQ 
       760        770        780        790        800
EISTDVMRQR NLEISARTVD SLLLNGCNRP VDVLYVDEAF ACHSGTLLAL 
       810        820        830        840        850
IALVRPRQKV VLCGDPKQCG FFNMMQMKVN YNHNICTQVY HKSISRRCTL 
       860        870        880        890        900
PVTAIVSSLH YEGKMRTTNE YNKPIVVDTT GSTKPDPGDL VLTCFRGWVK 
       910        920        930        940        950
QLQIDYRGHE VMTAAASQGL TRKGVYAVRQ KVNENPLYAS TSEHVNVLLT 
       960        970        980        990       1000
RTEGKLVWKT LSGDPWIKTL QNPPKGNFKA TIKEWEVEHA SIMAGICNHQ 
      1010       1020       1030       1040       1050
VTFDTFQNKA NVCWAKSLVP ILETAGIKLN DRQWSQIIQA FKEDRAYSPE 
      1060       1070       1080       1090       1100
VALNEICTRM YGVDLDSGLF SKPLVSVHYA DNHWDNRPGG KMFGFNPEAA 
      1110       1120       1130       1140       1150
SILERKYPFT KGKWNTNKQI CVTTRRIEDF NPNTNIIPAN RRLPHSLVAE 
      1160       1170       1180       1190       1200
HRPVKGERME WLVNKINGHH VLLVSGYNLV LPTKRVTWVA PLGIRGADYT 
      1210       1220       1230       1240       1250
YNLELGLPAT LGRYDLVIIN IHTPFRIHHY QQCVDHAMKL QMLGGDSLRL 
      1260       1270       1280       1290       1300
LKPGGSLLIR AYGYADRTSE RVVCVLGRKF RSSRALKPPC VTSNTEMFFL 
      1310       1320       1330       1340       1350
FSNFDNGRRN FTTHVMNNQL NAAFVGQATR AGCAPSYRVK RMDIAKNDEE 
      1360       1370       1380       1390       1400
CVVNAANPRG LPGDGVCKAV YKKWPESFKN SATPVGTAKT VMCGTYPVIH 
      1410       1420       1430       1440       1450
AVGPNFSNYS ESEGDRELAA AYREVAKEVT RLGVNSVAIP LLSTGVYSGG 
      1460       1470       1480       1490       1500
KDRLTQSLNH LFTALDSTDA DVVIYCRDKE WEKKIAEAIQ MRTQVELLDE 
      1510       1520       1530       1540       1550
HISVDCDIIR VHPDSSLAGR KGYSTTEGSL YSYLEGTRFH QTAVDMAEVY 
      1560       1570       1580       1590       1600
TMWPKQTEAN EQVCLYALGE SIESIRQKCP VDDADASSPP KTVPCLCRYA 
      1610       1620       1630       1640       1650
MTPERVTRLR MNHVTSIIVC SSFPLPKYKI EGVQKVKCSK VMLFDHNVPS 
      1660       1670       1680       1690       1700
RVSPREYKSP QETAQEVSST TSLTHSQFDL SVDGEELPAP SDLEADAPIP 
      1710       1720       1730       1740       1750
EPTPDDRAVL TLPPTIDNFS AVSDWVMNTA PVAPPRRRRG KNLNVTCDER 
      1760       1770       1780       1790       1800
EGNVLPMASV RFFRADLHSI VQETAEIRDT AASLQAPLSV ATEPNQLPIS 
      1810       1820       1830       1840       1850
FGAPNETFPI TFGDFDEGEI ESLSSELLTF GDFSPGEVDD LTDSDWSTCS 
      1860       1870       1880       1890       1900
DTDDELXLDR AGGYIFSSDT GPGHLQQRSV RQTVLPVNTL EEVQEEKCYP 
      1910       1920       1930       1940       1950
PKLDEVKEQL LLKKLQESAS MANRSRYQSR KVENMKATIV QRLKGGCKLY 
      1960       1970       1980       1990       2000
LMSETPKVPT YRTTYPAPVY SPPINIRLSN PESAVAACNE FLARNYPTVA 
      2010       2020       2030       2040       2050
SYQITDEYDA YLDMVDGSES CLDRATFNPS KLRSYPKQHS YHAPTIRSAV 
      2060       2070       2080       2090       2100
PSPFQNTLQN VLAAATKRNC NVTQMRELPT LDSAVFNVEC FKKFACNQEY 
      2110       2120       2130       2140       2150
WKEFAASPIR ITTENLTTYV TKLKGPKAAA LFAKTHNLLP LQEVPMDRFT 
      2160       2170       2180       2190       2200
VDMKRDVKVT PGTKHTEERP KVQVIQAAEP LATAYLCGIH RELVRRLNAV 
      2210       2220       2230       2240       2250
LLPNVHTLFD MSAEDFDAII AAHFKPGDAV LETDIASFDK SQDDSLALTA 
      2260       2270       2280       2290       2300
LMLLEDLGVD HPLLDLIEAA FGEISSCHLP TGTRFKFGAM MKSGMFLTLF 
      2310       2320       2330       2340       2350
VNTLLNITIA SRVLEDRLTR SACAAFIGDD NIIHGVVSDE LMAARCATWM 
      2360       2370       2380       2390       2400
NMEVKIIDAV VSQKAPYFCG GFILYDTVAG TACRVADPLK RLFKLGKPLA 
      2410       2420       2430       2440       2450
AGDEQDDDRR RALADEVVRW QRTGLTDELE KAVHSRYEVQ GISVVVMSMA 
      2460       2470 
TFASSRSNFE KLRGPVVTLY GGPK

Length:2,474

Mass (Da):275,933

Last modified:November 23, 2004 - v1

Checksum:ⁱ0699DB0485FB3097

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY726732 Genomic RNA Translation: AAU43880.1

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

AY726732 Genomic RNA Translation: AAU43880.1

Keywords - Coding sequence diversityⁱ

RNA suppression of termination

Protein	Similar proteins		Species	Score	Length	Source
Q5XXP4	Non-structural polyprotein	)	CHIKS		2474	UniRef90_Q8JUX6
Non-structural polyprotein P1234		CHIKV		2474
Nonstructural polyprotein		synthetic recombinant Chikungunya virus strain LS3-GFP		2474
Nonstructural polyprotein		synthetic recombinant Chikungunya virus strain LS3-MCS		2474
Nonstructural polyprotein		synthetic recombinant Chikungunya virus strain LS3		2474
+635

Protein	Similar proteins		Species	Score	Length	Source
Q5XXP4	Non-structural polyprotein	)	SFV		2432	UniRef50_P08411
Non-structural polyprotein	)	MAYAB		2436
Non-structural polyprotein		SAGV		2466
Non-structural polyprotein		GETV		2466
Non-structural polyprotein		ONNVG		2514
+769

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY726732 Genomic RNA Translation: AAU43880.1

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

AY726732 Genomic RNA Translation: AAU43880.1

3D structure databases

ProteinModelPortalⁱ	Q5XXP4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Proteomic databases

PRIDEⁱ	Q5XXP4

PRIDEⁱ

Q5XXP4

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Phylogenomic databases

OrthoDBⁱ	VOG09000007

OrthoDBⁱ

VOG09000007

Family and domain databases

InterProⁱ	View protein in InterPro IPR027351 (+)RNA_virus_helicase_core_dom IPR002588 Alphavirus-like_MT_dom IPR002620 Alphavirus_nsp2pro IPR002589 Macro_dom IPR027417 P-loop_NTPase IPR007094 RNA-dir_pol_PSvirus IPR001788 Tymovirus_RNA-dep_RNA_pol
Pfamⁱ	View protein in Pfam PF01661 Macro, 1 hit PF01707 Peptidase_C9, 1 hit PF00978 RdRP_2, 1 hit PF01443 Viral_helicase1, 1 hit PF01660 Vmethyltransf, 1 hit
SMARTⁱ	View protein in SMART SM00506 A1pp, 1 hit
SUPFAMⁱ	SSF52540 SSF52540, 1 hit
PROSITEⁱ	View protein in PROSITE PS51743 ALPHAVIRUS_MT, 1 hit PS51154 MACRO, 1 hit PS51520 NSP2PRO, 1 hit PS51657 PSRV_HELICASE, 1 hit PS50507 RDRP_SSRNA_POS, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	POLN_CHIK3
Accessionⁱ	Q5XXP4Primary (citable) accession number: Q5XXP4
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
	Last sequence update:	November 23, 2004
	Last modified:	April 25, 2018
	This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Viral Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q5XXP4 (POLN_CHIK3)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Caution

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Sites

Keywords - PTMi

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Motif

Phylogenomic databases

Family and domain databases

Sequence databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ