POLN_EOPV
ID POLN_EOPV Reviewed; 2987 AA.
AC Q6UP17;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Non-structural polyprotein;
DE Contains:
DE RecName: Full=Helicase {ECO:0000303|PubMed:23449794};
DE EC=3.6.4.13 {ECO:0000269|PubMed:23449794};
DE Contains:
DE RecName: Full=3C-like protease {ECO:0000303|PubMed:22534091};
DE Short=3CL-PRO;
DE EC=3.4.22.- {ECO:0000269|PubMed:22534091};
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48 {ECO:0000269|PubMed:20423615};
OS Ectropis obliqua picorna-like virus (EoPV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Iflaviridae; Iflavirus.
OX NCBI_TaxID=240555;
OH NCBI_TaxID=248899; Ectropis obliqua (Tea geometrid moth).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15105531; DOI=10.1099/vir.0.19638-0;
RA Wang X., Zhang J., Lu J., Yi F., Liu C., Hu Y.;
RT "Sequence analysis and genomic organization of a new insect picorna-like
RT virus, Ectropis obliqua picorna-like virus, isolated from Ectropis
RT obliqua.";
RL J. Gen. Virol. 85:1145-1151(2004).
RN [2]
RP FUNCTION (RNA-DIRECTED RNA POLYMERASE), AND CATALYTIC ACTIVITY
RP (RNA-DIRECTED RNA POLYMERASE).
RX PubMed=20423615; DOI=10.5483/bmbrep.2010.43.4.284;
RA Lin M., Ye S., Xiong Y., Cai D., Zhang J., Hu Y.;
RT "Expression and characterization of RNA-dependent RNA polymerase of
RT Ectropis obliqua virus.";
RL BMB Rep. 43:284-290(2010).
RN [3]
RP PROTEIN SEQUENCE OF 2194-2197 AND 2493-2496, FUNCTION (3C-LIKE PROTEASE),
RP ACTIVE SITE (3C-LIKE PROTEASE), PROTEOLYTIC CLEAVAGE (NON-STRUCTURAL
RP POLYPROTEIN), CHARACTERIZATION (3C-LIKE PROTEASE), CATALYTIC ACTIVITY
RP (3C-LIKE PROTEASE), MUTAGENESIS OF HIS-2261; ASP-2299 AND CYS-2383, AND
RP BIOPHYSICOCHEMICAL PROPERTIES (3C-LIKE PROTEASE).
RX PubMed=22534091; DOI=10.1016/j.virol.2012.04.002;
RA Ye S., Xia H., Dong C., Cheng Z., Xia X., Zhang J., Zhou X., Hu Y.;
RT "Identification and characterization of Iflavirus 3C-like protease
RT processing activities.";
RL Virology 428:136-145(2012).
RN [4]
RP FUNCTION (HELICASE), AND CATALYTIC ACTIVITY (HELICASE).
RX PubMed=23449794; DOI=10.1128/jvi.00245-13;
RA Cheng Z., Yang J., Xia H., Qiu Y., Wang Z., Han Y., Xia X., Qin C.F.,
RA Hu Y., Zhou X.;
RT "The nonstructural protein 2C of a Picorna-like virus displays nucleic acid
RT helix destabilizing activity that can be functionally separated from its
RT ATPase activity.";
RL J. Virol. 87:5205-5218(2013).
CC -!- FUNCTION: [Helicase]: Displays RNA helix destabilizing and strand
CC annealing acceleration activity. This activity is necessary at several
CC points during genome replication, for example to separate duplexes that
CC form after genome replication. {ECO:0000305|PubMed:23449794}.
CC -!- FUNCTION: [3C-like protease]: Cysteine protease that generates mature
CC viral proteins from the precursor polyprotein.
CC {ECO:0000269|PubMed:22534091}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates genomic and
CC antigenomic RNA. {ECO:0000269|PubMed:20423615}.
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 ECO:0000269|PubMed:20423615};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:23449794};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5 for 3C-like protease.
CC {ECO:0000269|PubMed:22534091};
CC Temperature dependence:
CC Optimum temperature is 22 degrees Celsius.
CC {ECO:0000269|PubMed:22534091};
CC -!- PTM: [Non-structural polyprotein]: Specific enzymatic cleavages in vivo
CC by the viral 3C-like protease yield three mature proteins.
CC {ECO:0000269|PubMed:22534091}.
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DR EMBL; AY365064; AAQ64627.1; -; Genomic_RNA.
DR RefSeq; NP_919029.1; NC_005092.1.
DR MEROPS; C99.001; -.
DR GeneID; 2943317; -.
DR KEGG; vg:2943317; -.
DR Proteomes; UP000201482; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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 CDD; cd00205; rhv_like; 2.
DR Gene3D; 2.60.120.20; -; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Direct protein sequencing; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleotidyltransferase; Protease;
KW RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN 1..2987
FT /note="Non-structural polyprotein"
FT /id="PRO_0000442451"
FT CHAIN 1..2193
FT /note="Helicase"
FT /id="PRO_0000442452"
FT CHAIN 2194..2492
FT /note="3C-like protease"
FT /id="PRO_0000442453"
FT CHAIN 2493..2987
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000442454"
FT DOMAIN 1526..1697
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 2222..2417
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT REGION 1159..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1279..1310
FT /evidence="ECO:0000255"
FT COILED 1788..1815
FT /evidence="ECO:0000255"
FT COMPBIAS 1159..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2261
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000269|PubMed:22534091"
FT ACT_SITE 2299
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000269|PubMed:22534091"
FT ACT_SITE 2383
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222,
FT ECO:0000269|PubMed:22534091"
FT BINDING 1553..1560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 2193..2194
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000269|PubMed:22534091"
FT SITE 2492..2493
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000269|PubMed:22534091"
FT MUTAGEN 2261
FT /note="H->A: Complete loss of 3C-like protease activity."
FT /evidence="ECO:0000269|PubMed:22534091"
FT MUTAGEN 2299
FT /note="D->A: Complete loss of 3C-like protease activity."
FT /evidence="ECO:0000269|PubMed:22534091"
FT MUTAGEN 2383
FT /note="C->A: Partial loss of 3C-like protease activity."
FT /evidence="ECO:0000269|PubMed:22534091"
SQ SEQUENCE 2987 AA; 332444 MW; F4A8A7AFA7BECD95 CRC64;
MMTTQTNQLF NRSLNDELGN RTDTITLHPW NVSEYVTSTG LAEAEFEACT GKDLEIQKYL
VTVSEECPCG HPTTFSEIDM SRGMVMASSD NIYSDDIVTL VPTENGYEDS DPCFCENQKE
DCDNCMYLQI LRMAPGKWNM TYGLRHNHQA QLTYYLTEER GFTCEGYTLE ADTSDSEGFG
DTADYTLYCI QYSGKYKQRR QWHVLLDDES CGFCKYRVTT GLIVPEVPRH WTNELGRRQN
LLVPKVLGQY VDFIEAKSPL RLDWLSMSKL VSGKCSLPNF YVNLTTLRTF QVAGGKFLPY
LYNGSAANND LKLPIQVTAQ GDEDTPAGEL SIEQDTHENT TLAESTDAST AYVATEEFSM
MPWITDGPHT YPDLTERWTK AFQFQWTTSQ AQGEIIQRFD LPIEAIQNFI NSPNALPWRQ
HAFYKSDIEL KVQVNSQPGQ SGYLILGAMY EASEGTAIGN RVDHAANIVA MPHMRISAGS
SNSGDMVIPF IRHFPVGCIL NNAFDVPQYF VTLFVAPLLQ LRTGADGPQV VDVTIMIRFP
NCEFYGQRTT EQIVTAQGWA PDLTQDGDVE SNPGPFLSGL LGTVAAVGKT VAGAGSSIGS
IATGVSGVAN GIGSIGSAAG KVIGGVESLL RPLFPKKDMD RPQNIIEPTN FYLQQNTSLS
LATGTNNVKL LQLQAENSVS HPPGFVPVDD QFNNRFILSV FGLSDYFQWF SGSASGTLLY
SFDVTPLKSF TRGIPLQPEF YLTPMAALSG QYGGYHGDME MRLTFAVSKF HSGRVFIVYS
PDVVPTFDNI GAYYNVLLDV QDQSVYTFKI PYQVPTPYAP IFESLQGDTG TFLTPAVSAG
NVRCMAYGFV SIFVENQLRV MQTAAPTIDV LVELRGADNF HLVLPAGGKF RSLSTITTTE
APVVTAMGDE RREPHTVNPP PRRIMPVWAA QLNESYDCRD VVKRYHDWFD IVSPAVVAGR
GFTDMYMNVT VFHVPVPAFD AAPIQNVQFT DMLVGSSILN KSMVLARERI NLATNNTISI
RVPWTNYASM ISNSINPASG RSNTMAPYSN GRVVVYIEYL SSYTTTLGAF RVVWDVTAGS
ASTRPDTYTP DMLTLLHDGF RFAKGDFNYQ MDFTPVPSGA NTAIRMRCFR AYGDGGNLYV
FQGFPKMLGT YTPRQAISGV TPTRGGLQRQ NIIGGGQRDL TQDGDIESNP GPTQSKPTGA
QPPPDDILTD EDREGLEGGS IRISFFEKLG DYCKRALGWS GERIVEFIRE LRSIKKHVGS
IPGMTRISEL ITTIKELSVV TNGLNRMSAA VEELNEQIKK TREKVETFVG GVGGKLNSLD
TGDLVSNGIE YVAYILNIYN SKSVGMTLIN VAALLSKMGL GRYLVNDLVD RLGTFAKGED
TEEIEREYTS LIITGVLGAF GLGTMNVEKE GFVKPFLSNV KDFFRNGFAV KKFLDSHFKC
INDICGWVRS KIFGKVDKGG LTVDLLVWCE RVQVLAEVYN YDTILNDPEF AETLLSLQDE
AFEFDRLFIA SRIRPPNQYS MYRTKLQRAI DLLGQQGTMQ KSKPVPFCLW VYGHSGCGKS
HVCDNVLTEI GSALGINTAN PIYTRSPDVE FWNGYTGQKL ISWQDFAKIT TGETYRKQVS
ELSSLIEPTP FNPPFAALED KRKIADAWAV YVSSNKAFPE VQNMGMEDSA LFYRRRHALV
KMRINPEIIQ EYARREPPIS LEDKYKGQTV YYPSNIPSED FATRGPYFHV QFAFHVTSLS
TAEPTEWLGY DGFIAEVTRR AIDHRQREVD ACIQRRGIYS KLRRSAPTGV EFREEVRTLK
EELDRLTQER VAEAHGSDNA VKNLATTMDY EKRATFEETE ALGSVILQYR LDPNCDCTNQ
AIMKAATSNE PRKICEVSFC EKCEPVNQRK KNVYKAMSEQ LEGVAVSNPF GGIAMIERGD
SARIPRAGRQ YTPLDYARQA TIGTLKWIQG KGLPAGYAYW SEIMPVCCHK KEILELAYFE
NVGDNIELVL DLSSMKARHG VSFPLFHKLE WFDLRKLDAW ATTGFKVILP VVCEQSKFNW
NNCIEVKPGE RGRIPITPKW APELIGRVTL EEFKRSWSCD AVQKPSVSYY KIEKDLIRFL
VSGTYVQIEG VENMTAGLNH LMSLHTKDTV AFCNSFFYWK SGGKLRAAKF YPFVNGMLKD
MSFIFSNIMI AVGAVMLAYK VYRLIRNSSE CVEAQAKDYD QKTEAPKIPK VNFVQSTPVV
VAAKGDEELS IIHNSLCQLR KGSMRLLGVR LCSNFVLAPQ HLAWVPGEFG ISLHSSGAWS
TELIFEATSV KYSCVKGFDY AVYRFVTLPA GRNIVNYFTT RAQGATLKSE ATLMTLSGAS
LQLRPVRISQ YTGALTYDNA SFPGTGTSMI GWQYWLGAQS VRCGSLIMSN NLLCGFHVAQ
NLKTGDAYAV SICKEMLVEA LRILGATPFD MKMKRTTPIT TVGEPKMQPP ETAVVIPLGK
AIEPVRYSGK SNLEKSIMHG ELAEPFRIPA AQSATAKGEC IGYDIVMKGC EKQFKPPKPI
DPEEVEKIGD YLIERLVPQS IPLIPTISEP LSLGEAIAGI DGIPLMCGMK LNTSIGWPLC
NEYPKGTKKS NIIRVDREEG EVHVDVVAFD DYAKANTLRK QAILPPTTFM DFPKDELLKP
GKDTRLINGA PLHHTLDMRR YLMEFFAAIT TINNKIAVGI DVHSGDWALI HGGADDVVDE
DYSGFGPGFH SQWLTVVCPI AVAWCKHHKK VDKEYEDVVN CLIMELQNAY HVAGDLVYQV
LCGSPSGAFA TDRINSLANL CYHCLCHLRK YGTLTGFWSH YTLVYGDDTR RRETAYTGDE
FQECMASVGI VVNRDKSGVT SFLKRQFIPI DHRDVRVMLA PLPRPIVEDI LNWVRKPYAS
KLSALEETVG SYLSEIFHHG QDEFNNSRSK IQAILARHGS HPELPTFDDL FRQKYLSNGV
WPVLMPLANA LGPIPAAESE PTHKVTSGQV VCVPHEAGEC CAITLGG
