POLN_DCVEB
ID POLN_DCVEB Reviewed; 1759 AA.
AC O36966;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Replicase polyprotein;
DE Contains:
DE RecName: Full=Protein 1A;
DE Contains:
DE RecName: Full=Protein 2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Contains:
DE RecName: Full=Protein 3A;
DE Contains:
DE RecName: Full=Protein 3B;
DE Contains:
DE RecName: Full=3C-like protease;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase 3D-POL;
DE EC=2.7.7.48;
GN ORFNames=ORF1;
OS Drosophila C virus (strain EB) (DCV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Dicistroviridae; Cripavirus.
OX NCBI_TaxID=865617;
OH NCBI_TaxID=7227; Drosophila melanogaster (Fruit fly).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9460942; DOI=10.1099/0022-1317-79-1-191;
RA Johnson K.N., Christian P.D.;
RT "The novel genome organization of the insect picorna-like virus Drosophila
RT C virus suggests this virus belongs to a previously undescribed virus
RT family.";
RL J. Gen. Virol. 79:191-203(1998).
RN [2]
RP FUNCTION OF PROTEIN 1A.
RX PubMed=17079687; DOI=10.1101/gad.1482006;
RA van Rij R.P., Saleh M.C., Berry B., Foo C., Houk A., Antoniewski C.,
RA Andino R.;
RT "The RNA silencing endonuclease Argonaute 2 mediates specific antiviral
RT immunity in Drosophila melanogaster.";
RL Genes Dev. 20:2985-2995(2006).
RN [3]
RP FUNCTION OF PROTEIN 1A.
RX PubMed=20400949; DOI=10.1038/nsmb.1810;
RA Nayak A., Berry B., Tassetto M., Kunitomi M., Acevedo A., Deng C.,
RA Krutchinsky A., Gross J., Antoniewski C., Andino R.;
RT "Cricket paralysis virus antagonizes Argonaute 2 to modulate antiviral
RT defense in Drosophila.";
RL Nat. Struct. Mol. Biol. 17:547-554(2010).
CC -!- FUNCTION: Protein 1A functions as a suppressor of RNA-mediated gene
CC silencing, an antiviral defense mechanism of insect cells. Binds to
CC long dsRNA and to a lesser extent, to siRNA.
CC -!- FUNCTION: RNA-directed RNA polymerase replicates genomic and
CC antigenomic RNA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- PTM: Protein 1A might be expressed through a ribosomal skip from one
CC codon to the next without formation of a peptide bond.
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DR EMBL; AF014388; AAC58807.1; -; Genomic_RNA.
DR PIR; T03725; T03725.
DR RefSeq; NP_044945.1; NC_001834.1.
DR SMR; O36966; -.
DR GeneID; 1449523; -.
DR KEGG; vg:1449523; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR024387; Pept_C3G_Picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF12381; Peptidase_C3G; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SMART; SM00358; DSRM; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 4: Predicted;
KW ATP-binding; Coiled coil; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; RNA-binding; RNA-directed RNA polymerase;
KW Suppressor of RNA silencing; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN 1..1759
FT /note="Replicase polyprotein"
FT /id="PRO_0000399911"
FT CHAIN 1..121
FT /note="Protein 2A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000399913"
FT CHAIN 1..97
FT /note="Protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000399912"
FT CHAIN 122..263
FT /note="Protein 2B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000399914"
FT CHAIN 264..701
FT /note="Protein 2C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000399915"
FT CHAIN 702..?
FT /note="Protein 3A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000399916"
FT CHAIN ?..901
FT /note="Protein 3B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000399917"
FT CHAIN 902..1209
FT /note="3C-like protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000399918"
FT CHAIN 1210..1759
FT /note="RNA-directed RNA polymerase 3D-POL"
FT /evidence="ECO:0000255"
FT /id="PRO_0000399919"
FT DOMAIN 23..90
FT /note="DRBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 421..595
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 950..1191
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1483..1622
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT COILED 113..140
FT /evidence="ECO:0000255"
FT ACT_SITE 994
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1054
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1152
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 449..456
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 97..98
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000255"
FT SITE 701..702
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000255"
FT SITE 818..819
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000255"
FT SITE 901..902
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000255"
FT SITE 1209..1210
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1759 AA; 202942 MW; 49C391F9B0C1AAA9 CRC64;
MESDKSMACL NRILMNKMMF VEDKISTLKM VADYYQKEVK YDFDAVESPR EAPVFRCTCR
FLGYTIMTQG IGKKNPKQEA ARQMLLLLSG DVETNPGPVQ SRPVYYRYND PRYTRLEKAI
ERRDDKIKTL IKELRRQIKN RKIYSQGMFD KLTKQISDGI KDGVGSEQMN GNLTRICDFL
ENTLPGLQAN IQATVIDTTD KYVSLKEDIM KIVLVILLVR LLMVWKKYRA SLCVILIFIF
KFYGFDQKLI DLIMDLKNKI FSQGALEDTV EEVVYHPWFH TCGKIIFAVM AFLTIKKIPG
KQDWDSYITR LDRIPKSIEG AKKITDYCSE YFNIANDQIK MMVLGKTKEE LQRANGLYGE
IQAWAQEVRQ YLELDQRNKI DLDTETANRV EQLWIKGLKF KSEPLLSKEM SALVHTTLLP
AKQLYEYVSC SPVKGGGPRM RPICLWLVGE SGVGKTEMVY PLCIDVLREM GMIKKDDFHH
QVYGRQVETE FWDGYKGQKI VIYDDAFQKK DDKTAANPEI FEVIRSCNTF PQHLHMAALH
DKNTFSAAEL LLYTTNDYNV KLESITFPDA FFNRMGDMAY KVSPKKEYGI ETEKGNSGKT
YLKLDKSKLD KTKAIDLSVY EFQKIVRDEK SDAGWIDSGS PLDYEDFAKL VCSKWKEAKQ
SSMNKLKFLE EYAIRAQVGS EENSEYGDCI DFVDDIAKRL QKGETLEEIE FDYASDPEMF
TQYYHFKSTI KPASRWQKYK DRMDICLSDC KTYLAKKYEE IKKILAEHPI LTILGMIGVA
LSALAMYYWF SKSLDPVEAE VAPSGDAKTV RLPRKLVEIG ASGDVKTQKI VKPVVETEWH
RNNKGEIEIS CDECGMHRMS AFNNMTDEEF DNCTYEDLNK DQKRELAQWS TKDSWLGRFF
LSRDRKNKVG IWAEVGQSGD VKTNKAQIKR VEAGAEELVT VALTQGCSDD AAHNLMIDVF
QKNTYRMSYF RGDKRYQLGN CTFVRGWSFI MPYHFVQAVF ARRLPPNTII SLSQQMSEDL
MQIPLSHFFS AGVDNFYLTD NCVRLPFKNG DFRDCVMVNL HSRMCTPHRD LVRHFILTSD
QGKLKGSFSG AMATFHVNNM GLYRVYNWLN AVRPCDKKIE IFHPEDGFEY PEESYIQRDC
YEYNAPTRTG DCGSIIGLYN KYLERKIIGM HIAGNDAEEH GYACPLTQEC LETAFSALVN
KNKKNISSQF YYEIPNMVDP LGDSSVPEGK FYALGKSSIR VGQAVNSSII PSRIYGKLSV
PTMKPALLKP TILNNKVHNP LLSGLKKCGV DTAVLSDDEV LSASQDVCRV MLNQYNKNLN
KTKYQRILTY EEAIRGTQDD EFMCAINRTT SPGFPYAQMK RNAPGKQQWM GFGEEFDFTS
NYALALRKDV EQLIEDCASG KISNVIFVDT LKDERRDIAK VNVGKTRVFS AGPQHFVVAF
RQYFLPFAAW LMHNRISNEV AVGTNVYSSD WERIAKRLKT KGSHVIAGDF GNFDGSLVAQ
ILWAIFWEIF VVWLKQFIDI ENSEGKRILC ICLGLWSHLV HSVHIYEDNV YMWTHSQPSG
NPFTVIINCL YNSIIMRLSW IRVMEKFQPR LKSMKWFNEY VALITYGDDN VLNIDAKVVE
WFNQINISEV MTEMRHEYTD EAKTGDIVKS RKLEDIFFLK RKFRFSPELQ RHVAPLKIEV
IYEMLNWSRR SIDPDEILMS NIETAFREVV YHGKEEYDKL RSAVLALKVP QELPENPQIL
TYNQYLHDIE YLADPLYDF
