Q9IJX4 (POLN_CRPVC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Replicase polyprotein

Cleaved into the following 8 chains:

1. Protein 1A
   Alternative name(s):
   CrPV-1A
2. Protein 2A
3. Protein 2B
4. Protein 2C
5. Protein 3A
6. Protein 3B
7. 3C-like protease
   EC=3.4.22.-
8. RNA-directed RNA polymerase 3D-POL
   EC=2.7.7.48

Gene names

ORF Names:

ORF1

Organism

Cricket paralysis virus (isolate Teleogryllus commodus/Australia/CrPVVIC/1968) (CrPV) [Reference proteome]

Taxonomic identifier

928300 [NCBI]

Taxonomic lineage

Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Dicistroviridae › Cripavirus › Cricket paralysis virus

Virus host

Teleogryllus oceanicus (black field cricket) [TaxID: 128161]

Protein attributes

Sequence length	1771 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein 1A functions as a suppressor of RNA-mediated gene silencing, an antiviral defense mechanism of insect cells. Inhibits siRNA function, but does not interfere with miRNA pathway. Does not bind to dsRNA or siRNA. Ref.3 RNA-directed RNA polymerase replicates genomic and antigenomic RNA. Ref.3
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
Subunit structure	Protein 1A interacts with host AGO2; this interaction may block the RNA-induced silencing complexes (RISC) activity. Ref.3
Post-translational modification	Protein 1A might be expressed through a ribosomal skip from one codon to the next without formation of a peptide bond.
Sequence similarities	Contains 1 RdRp catalytic domain. Contains 1 SF3 helicase domain.

Ontologies

Keywords
Biological process	Host-virus interaction Viral RNA replication
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase Nucleotidyltransferase Protease RNA-directed RNA polymerase Suppressor of RNA silencing Thiol protease Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral genome replication Inferred from electronic annotation. Source: InterPro virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA helicase activity Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1771	1771	Replicase polyprotein		PRO_0000398372
	Chain	1 – 190	190	Protein 2A Potential		PRO_0000398373
	Chain	1 – 166	166	Protein 1A Potential		PRO_0000398374
	Chain	191 – 328	138	Protein 2B Potential		PRO_0000398375
	Chain	329 – 739	411	Protein 2C Potential		PRO_0000398376
	Chain	740 – ?		Protein 3A Potential		PRO_0000398377
	Chain	? – 908		Protein 3B Potential		PRO_0000398378
	Chain	909 – 1220	312	3C-like protease Potential		PRO_0000398379
	Chain	1221 – 1771	551	RNA-directed RNA polymerase 3D-POL Potential		PRO_0000398380
Regions
	Domain	482 – 656	175	SF3 helicase
	Domain	1495 – 1634	140	RdRp catalytic
	Nucleotide binding	510 – 517	8	ATP Potential
	Coiled coil	1 – 29	29	Potential
	Coiled coil	1385 – 1413	29	Potential
Sites
	Active site	1162	1	Potential
	Site	166 – 167	2	Cleavage; by ribosomal skip Potential
	Site	190 – 191	2	Cleavage; by 3C-like protease Potential
	Site	328 – 329	2	Cleavage; by 3C-like protease Potential
	Site	739 – 740	2	Cleavage; by 3C-like protease Potential
	Site	884 – 885	2	Cleavage; by 3C-like protease Potential
	Site	908 – 909	2	Cleavage; by 3C-like protease Potential
	Site	1220 – 1221	2	Cleavage; by 3C-like protease Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9IJX4 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 78C5969469EAA716	FASTA	1,771	203,830
	10 20 30 40 50 60 MSFQQTNNNA TNNINSLEEL AAQELIAAQF EGNLDGFFCT FYVQSKPQLL DLESECYCMD 70 80 90 100 110 120 DFDCGCDRIK REEELRKLIF LTSDVYGYNF EEWKGLVWKF VQNYCPEHRY GSTFGNGLLI 130 140 150 160 170 180 VSPRFFMDHL DWFQQWKLVS SNDECRAFLR KRTQLLMSGD VESNPGPVQS RPVYACDNDP 190 200 210 220 230 240 RAIRLEKALQ RRDEKISTLI KKLRQEIKNN RIYTQGFFDD LKGAKGEVGQ LNGNLTRICD 250 260 270 280 290 300 FLENSLPTLT AQIQTTVLTT TDKYVNLKED LLKVAILLVL VRLLMVWKKY RAALIVIILF 310 320 330 340 350 360 VMHFYGFDKQ ILDIVLDLKD KILQTTTQAG TETLEEVVYH PWFDTCGKLI FAVLAFFAIK 370 380 390 400 410 420 KIPGKQDWDN YISRLDRIPK AIEGSKKIVD YCSEYFNLSV DEVKKVVLGK ELKGTQGLYD 430 440 450 460 470 480 EIHVWAKEIR HYLDLDERNK ITLDTETAAK VEDLYKRGLK YSEEKIPDRD IARFITTMLF 490 500 510 520 530 540 PAKSLYEQVL LSPVKGGGPK MRPITVWLTG ESGIGKTQMI YPLCIDILRE MGIVKPDAYK 550 560 570 580 590 600 HQAYARQVET EYWDGYNGQK IVIYDDAFQL KDDKTKPNPE IFEVIRTCNT FPQHLHMAAL 610 620 630 640 650 660 QDKNMYSQAE VLLYTTNQFQ VQLESITFPD AFYNRMKTHA YRVQIKQEKS IWVRNARGEE 670 680 690 700 710 720 YNALDVTKLN KDEAIDLSVY EFQKMRFDDE SATKWIDDGE PISYDEFART ICKAWKEEKE 730 740 750 760 770 780 KTFHQLQWLE AYASRTVAQG GSETSEYYDV WDETYFSNLL SQGFMAGKSL IEMEAEFASD 790 800 810 820 830 840 AETFNAYIEY KKNIPKETKW SKWMTILDEQ ISALSTKIRE LKNKAYKFIS EHPYLTALGF 850 860 870 880 890 900 IGVMISAFAM YSFFERTLTD DTITSEVGSS GDNKTQKISK RVVEVGGSGD VKTTKPAKTA 910 920 930 940 950 960 VEVGSSGDSK TMKNKITKVE VGSSGDSKTQ KQRNTKVEVG KELEKEAETQ GCSDPAAHAL 970 980 990 1000 1010 1020 VLDVLQKNTY CLYYERMVKG EMKRYRLATA TFLRGWVCMM PYHFIETLYA RKVAPSTNIY 1030 1040 1050 1060 1070 1080 FSQPNCDDVI VVPVSHFIAP NAERVELTTA CTRIHYKDET PRDCVLVNLH RRMCHPHRDI 1090 1100 1110 1120 1130 1140 LKHFVKKSDQ GNLRGVFQGT LATFHQSANE LCRAYQWLQA IRPLDQEITI YHEDTDMFDY 1150 1160 1170 1180 1190 1200 ESESYTQRDC YEYNAPTQTG NCGSIVGLYN KRMERKLIGM HIPGNVSECH GYACPLTQEA 1210 1220 1230 1240 1250 1260 IMDGLNRLEK LDPVNNITVQ CCFEPPSDIK DTMSGETPEG KFCAIGKSNI KVGQAVKTTL 1270 1280 1290 1300 1310 1320 LKSCIYGMLS KPITKPAHLT RTRLPNGEIV DPLMKGLKKC GVDTAVLDAE IVESAALDVK 1330 1340 1350 1360 1370 1380 QVVLTQYNSM LDVNKYRRFL TYEEATQGTG DDDFMKGIAR QTSPGYRYFQ MPRKLPGKQD 1390 1400 1410 1420 1430 1440 WMGSGEQYDF TSQRAQELRR DVEELIDNCA KGIIKDVVFV DTLKDERRPI EKVDAGKTRV 1450 1460 1470 1480 1490 1500 FSAGPQHFVV AFRKYFLPFA AYLMNNRIDN EIAVGTNVYS TDWERIAKRL KKHGNKVIAG 1510 1520 1530 1540 1550 1560 DFGNFDGSLV AQFFGQSCGK SFYPWFKTFN DVNTEDGKRN LMICIGLWTH IVHSVHSYGD 1570 1580 1590 1600 1610 1620 NVYMWTHSQP SGNPFTVIIN CLYNSMIMRI VWILLARKLA PEMQSMKKFR ENVSMISYGD 1630 1640 1650 1660 1670 1680 DNCLNISDRV VEWFNQITIS EQMKEIKHEY TDEGKTGDMV KFPSLSEIHF LKKRFVFSHQ 1690 1700 1710 1720 1730 1740 LQRTVAPLQK DVIYEMLNWT RNTIDPNEIL MMNINTAFRE IVYHGKSEYQ KLRSGIEDLA 1750 1760 1770 MKGILPQQPQ ILTFKAYLWD ATMLADEVYD F

References

[1]	"Naturally occurring dicistronic cricket paralysis virus RNA is regulated by two internal ribosome entry sites." Wilson J.E., Powell M.J., Hoover S.E., Sarnow P. Mol. Cell. Biol. 20:4990-4999(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Cleavage sites of the 'P3 region' in the nonstructural polyprotein precursor of a dicistrovirus." Nakashima N., Nakamura Y. Arch. Virol. 153:1955-1960(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[3]	"Cricket paralysis virus antagonizes Argonaute 2 to modulate antiviral defense in Drosophila." Nayak A., Berry B., Tassetto M., Kunitomi M., Acevedo A., Deng C., Krutchinsky A., Gross J., Antoniewski C., Andino R. Nat. Struct. Mol. Biol. 17:547-554(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF PROTEIN 1A, INTERACTION WITH HOST AGO2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF218039 Genomic RNA. Translation: AAF80998.1.
RefSeq	NP_647481.1. NC_003924.1.
3D structure databases
ProteinModelPortal	Q9IJX4.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59000N.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	944541.
Family and domain databases
InterPro	IPR004004. Helic/Pol/Pept_Calicivir-typ. IPR000605. Helicase_SF3_ssDNA/RNA_vir. IPR014759. Helicase_SF3_ssRNA_vir. IPR024387. Pept_C3G_Picornavir. IPR001205. RNA-dir_pol_C. IPR007094. RNA-dir_pol_PSvirus. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF12381. Peptidase_C3G. 1 hit. PF00680. RdRP_1. 1 hit. PF00910. RNA_helicase. 1 hit. [Graphical view]
PRINTS	PR00918. CALICVIRUSNS.
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50507. RDRP_SSRNA_POS. 1 hit. PS51218. SF3_HELICASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POLN_CRPVC

Accession

Primary (citable) accession number: Q9IJX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program