UniProtKB - Q5XXP4 (POLN_CHIK3)
Polyprotein P1234
Functioni
Miscellaneous
Catalytic activityi
- [nsP1 protein]-L-histidine + N7-methyl-GTP = [nsP1 protein]-Nτ-(N7-methylguanosine 5'-phospho)-L-histidine + diphosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a 5'-end diphospho-(purine-ribonucleoside) in mRNA + H+ + phosphateBy similarityEC:3.1.3.33By similarity
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H+ + phosphateBy similarityEC:3.6.1.15By similarity
- EC:3.6.4.13By similarity
- EC:2.7.7.48PROSITE-ProRule annotation
- 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H+ + L-aspartyl-[protein]By similarityThis reaction proceeds in the forwardBy similarity direction.
- 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose + H+ + L-glutamyl-[protein]By similarityThis reaction proceeds in the forwardBy similarity direction.
- EC:2.7.7.19By similarity
- EC:3.1.3.84By similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
Protein has several cofactor binding sites:- Mg2+By similarity, Mn2+By similarityNote: For nsP4 adenylyltransferase activity; Mn2+ supports catalysis at 60% of the levels observed with Mg2+.By similarity
- Mg2+Note: For nsP4 RNA-directed RNA polymerase activity.By similarity
- Mg2+By similarityNote: For nsP1 guanylylation.By similarity
- Mg2+Note: For nsP2 RNA triphosphatase activity.By similarity
- Mg2+Note: For nsP2 NTPase activity.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 37 | Involved in the phosphoramide link with 7-methyl-GMPBy similarity | 1 | |
Active sitei | 1013 | For cysteine protease nsP2 activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1083 | For cysteine protease nsP2 activityPROSITE-ProRule annotation | 1 | |
Binding sitei | 1343 | ADP-riboseBy similarity | 1 | |
Binding sitei | 1357 | ADP-riboseBy similarity | 1 | |
Binding sitei | 1365 | ADP-riboseBy similarity | 1 | |
Binding sitei | 1445 | ADP-riboseBy similarity | 1 | |
Binding sitei | 1446 | ADP-riboseBy similarity | 1 | |
Binding sitei | 1447 | ADP-riboseBy similarity | 1 | |
Metal bindingi | 1595 | ZincBy similarity | 1 | |
Metal bindingi | 1597 | ZincBy similarity | 1 | |
Metal bindingi | 1620 | ZincBy similarity | 1 | |
Metal bindingi | 1638 | ZincBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 721 – 728 | NTPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- cysteine-type peptidase activity Source: UniProtKB-KW
- GTP binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- mRNA methyltransferase activity Source: InterPro
- polynucleotide 5'-phosphatase activity Source: UniProtKB-EC
- polynucleotide adenylyltransferase activity Source: UniProtKB-EC
- RNA binding Source: UniProtKB-KW
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- RNA helicase activity Source: UniProtKB-EC
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
Keywordsi
Names & Taxonomyi
Protein namesi | Recommended name: Polyprotein P1234Short name: P1234 Alternative name(s): Non-structural polyprotein Cleaved into the following 7 chains: mRNA-capping enzyme nsP1 (EC:2.1.1.-By similarity, EC:2.7.7.-By similarity) Alternative name(s): Non-structural protein 1 Protease nsP2 (EC:3.1.3.33By similarity, EC:3.4.22.-By similarity, EC:3.6.1.15By similarity, EC:3.6.4.13By similarity) Alternative name(s): Non-structural protein 2 Short name: nsP2 RNA-directed RNA polymerase nsP4 (EC:2.7.7.19By similarity, EC:2.7.7.48PROSITE-ProRule annotation) Alternative name(s): Non-structural protein 4 Short name: nsP4 |
Organismi | Chikungunya virus (strain 37997) (CHIKV) |
Taxonomic identifieri | 371095 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Kitrinoviricota › Alsuviricetes › Martellivirales › Togaviridae › Alphavirus › |
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 |
|
Subcellular locationi
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated Note: Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.Curated
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated Note: Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.Curated
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated Note: Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.Curated
- Host cytoplasmic vesicle membrane By similarity; Lipid-anchor By similarity
- Host cell membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity
- host filopodium 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 and its filopodial extensions. Only the palmitoylated nsP1 localizes to the host filopodia (By similarity). NsP1 is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity
- Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity
- Host nucleus By similarity
- Host cytoplasm 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). Shuttles between cytoplasm and nucleus (By similarity). NsP2 is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity
- Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein Curated Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' form aggregates in cytoplasm (By similarity). NsP3' is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity
- Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein Curated Note: In the late phase of infection, the polyprotein is quickly cleaved before localization to cellular membranes. Then nsP3 and nsP3' form aggregates in cytoplasm (By similarity). NsP3 is also part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex (By similarity).By similarity
- Host cytoplasmic vesicle membrane ; Peripheral membrane protein By similarity Note: NsP4 is part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex.By similarity
GO - Cellular componenti
- host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
- host cell filopodium Source: UniProtKB-SubCell
- host cell nucleus Source: UniProtKB-SubCell
- host cell plasma membrane Source: UniProtKB-SubCell
- membrane Source: UniProtKB-KW
Keywords - Cellular componenti
Host cell membrane, Host cell projection, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000308396 | 1 – 2474 | Polyprotein P1234Add BLAST | 2474 | |
ChainiPRO_0000227765 | 1 – 1863 | Polyprotein P123'Add BLAST | 1863 | |
ChainiPRO_0000446648 | 1 – 1856 | Polyprotein P123Add BLAST | 1856 | |
ChainiPRO_0000227766 | 1 – 535 | mRNA-capping enzyme nsP1Add BLAST | 535 | |
ChainiPRO_0000227767 | 536 – 1333 | Protease nsP2Add BLAST | 798 | |
ChainiPRO_0000227768 | 1334 – 1863 | Non-structural protein 3'Add BLAST | 530 | |
ChainiPRO_0000446649 | 1334 – 1856 | Non-structural protein 3Add BLAST | 523 | |
ChainiPRO_0000227769 | 1864 – 2474 | RNA-directed RNA polymerase nsP4Add 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
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 535 – 536 | Cleavage; by protease nsP2By similarity | 2 | |
Sitei | 1333 – 1334 | Cleavage; by protease nsP2By similarity | 2 | |
Sitei | 1863 – 1864 | Cleavage; by protease nsP2By similarity | 2 |
Keywords - PTMi
Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugationProteomic databases
PRIDEi | Q5XXP4 |
Interactioni
Subunit structurei
Interacts with non-structural protein 3 (By similarity).
Interacts with RNA-directed RNA polymerase nsP4 (By similarity).
Interacts with protease nsP2 (By similarity). interacts with itself (By similarity).
By similarityInteracts with mRNA-capping enzyme nsP1 (By similarity).
Interacts with host DDX1 (By similarity).
Interacts with host DDX3 (By similarity).
Interacts (via C-terminus) with host G3BP1; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP1 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (By similarity).
Interacts (via C-terminus) with host G3BP2; this interaction inhibits the formation of host stress granules on viral mRNAs and the nsp3-G3BP2 complexes bind viral RNAs and probably orchestrate the assembly of viral replication complexes (By similarity).
By similarityInteracts with mRNA-capping enzyme nsP1 (By similarity).
Interacts with protease nsP2 (By similarity). interacts with itself (By similarity).
By similarityInteracts with RNA-directed RNA polymerase nsP4 (By similarity).
Interacts with mRNA-capping enzyme nsP1 (By similarity).
Interacts with KPNA1/karyopherin-alpha1; this interaction probably allows the active transport of protease nsP2 into the host nucleus (By similarity).
By similarityFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 28 – 259 | Alphavirus-like MTPROSITE-ProRule annotationAdd BLAST | 232 | |
Domaini | 690 – 842 | (+)RNA virus helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST | 153 | |
Domaini | 843 – 991 | (+)RNA virus helicase C-terminalPROSITE-ProRule annotationAdd 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 | 1058 – 1067 | Nuclear export signalBy similarity | 10 | |
Motifi | 1182 – 1186 | Nuclear localization signalBy similarity | 5 | |
Motifi | 1812 – 1815 | FGDF; binding to host G3BP1By similarity | 4 | |
Motifi | 1830 – 1833 | FGDF; binding to host G3BP1By similarity | 4 |
Domaini
Family and domain databases
DisProti | DP01188 |
Gene3Di | 3.40.220.10, 1 hit |
InterProi | View protein in InterPro IPR027351, (+)RNA_virus_helicase_core_dom IPR002588, Alphavirus-like_MT_dom IPR002620, Alphavirus_nsp2pro IPR043502, DNA/RNA_pol_sf IPR002589, Macro_dom IPR043472, Macro_dom-like 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 SSF52949, SSF52949, 1 hit SSF56672, SSF56672, 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 |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY726732 Genomic RNA Translation: AAU43880.1 |
Keywords - Coding sequence diversityi
RNA suppression of terminationSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY726732 Genomic RNA Translation: AAU43880.1 |
3D structure databases
ModBasei | Search... |
Proteomic databases
PRIDEi | Q5XXP4 |
Family and domain databases
DisProti | DP01188 |
Gene3Di | 3.40.220.10, 1 hit |
InterProi | View protein in InterPro IPR027351, (+)RNA_virus_helicase_core_dom IPR002588, Alphavirus-like_MT_dom IPR002620, Alphavirus_nsp2pro IPR043502, DNA/RNA_pol_sf IPR002589, Macro_dom IPR043472, Macro_dom-like 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 SSF52949, SSF52949, 1 hit SSF56672, SSF56672, 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... |
MobiDBi | 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: | December 2, 2020 | |
This is version 109 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |