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POLR_EPMV
ID   POLR_EPMV               Reviewed;        1839 AA.
AC   P20126;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=RNA replicase polyprotein;
DE            EC=2.7.7.48;
OS   Eggplant mosaic virus.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Tymoviridae; Tymovirus.
OX   NCBI_TaxID=12151;
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=4111; Solanum melongena (Eggplant) (Aubergine).
OH   NCBI_TaxID=45840; Solanum seaforthianum (Brazilian nightshade).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2800336; DOI=10.1016/0042-6822(89)90197-9;
RA   Osorio-Keese M.E., Keese P., Gibbs A.;
RT   "Nucleotide sequence of the genome of eggplant mosaic tymovirus.";
RL   Virology 172:547-554(1989).
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   -!- SIMILARITY: Belongs to the tymovirus NS35 RNA replicase polyprotein
CC       family. {ECO:0000305}.
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DR   EMBL; J04374; AAA43039.1; -; Genomic_RNA.
DR   PIR; JQ0102; RRWPEM.
DR   RefSeq; NP_040968.1; NC_001480.1.
DR   MEROPS; C21.001; -.
DR   PRIDE; P20126; -.
DR   GeneID; 1493960; -.
DR   KEGG; vg:1493960; -.
DR   Proteomes; UP000008664; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0008174; F:mRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; 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:0006396; P:RNA processing; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.90.70.100; -; 1.
DR   InterPro; IPR027351; (+)RNA_virus_helicase_core_dom.
DR   InterPro; IPR002588; Alphavirus-like_MT_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008043; Peptidase_C21.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   InterPro; IPR001788; Tymovirus_RNA-dep_RNA_pol.
DR   InterPro; IPR043181; TYMV_endopept_dom.
DR   Pfam; PF05381; Peptidase_C21; 1.
DR   Pfam; PF00978; RdRP_2; 1.
DR   Pfam; PF01443; Viral_helicase1; 1.
DR   Pfam; PF01660; Vmethyltransf; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51743; ALPHAVIRUS_MT; 1.
DR   PROSITE; PS51738; PEPTIDASE_C21; 1.
DR   PROSITE; PS51657; PSRV_HELICASE; 1.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Nucleotidyltransferase;
KW   Protease; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW   Viral RNA replication.
FT   CHAIN           1..1839
FT                   /note="RNA replicase polyprotein"
FT                   /id="PRO_0000222934"
FT   DOMAIN          58..219
FT                   /note="Alphavirus-like MT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01079"
FT   DOMAIN          723..877
FT                   /note="Peptidase C21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   DOMAIN          935..1092
FT                   /note="(+)RNA virus helicase ATP-binding"
FT   DOMAIN          1093..1224
FT                   /note="(+)RNA virus helicase C-terminal"
FT   DOMAIN          1567..1673
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          253..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..269
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..604
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..674
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        776
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   ACT_SITE        862
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01074"
FT   BINDING         965..972
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1839 AA;  204732 MW;  FD8DC1F5115E7861 CRC64;
     MAFQSALEAL NSTTHRDAST NPILNSVVEP LRDSLSLYPW LLPKEAVPHL LSWGIPNSGL
     GVTPHPHPIH KTVETFLLFN HWHALARLPS TVMFMKPSKF QKLAALNPKF QELINFRLTA
     ADTTRYPSTS LTFPSNSICF MHDALMYFSP AQIVDLFTQS PALETLYCSL IVPPESHFTD
     LSLFPEIYTY KISGQTLHYI PENHHSGSYN QPLQAPSWLK ISSILSPSLA LSVTKLESWG
     PVHSILIQRG LPPKPSLSAR PPVLPNQPPR ATTPNSQNQL LHQTSQLFFQ LQQPQLSLVS
     FRIPDCVELP QATFLRQPLR HRLVPTSVYN ALFTYTRAVR TLRTSDPAGF VRTQSNKPEH
     AWVTPNAWDN LQTLSVNAPH RPQVCYHFFS SPVARLKLHF AQHWRAYLLA LTPFLTTSPL
     LLPLFNFNTP FPLPRLLSLF RRSVSSPRLL HSILPSQLRG AAIPNRPLPL WVTKLHHFLD
     SHSLLPTPPI RPRIELQRLP LMSLIPKPKI VLPLLSLLLS SPTIYIHFFQ AQTPQQLHDN
     YHLHLHPSRF ELSWTLQSYH VTQAQSFLPL LLPAPTQAQA SNPAPRPPAF HAIPLPPQPS
     TSSSPPLQEP TLSPHLIHPP LTREPSPLNG CACDSALLPS TAAMTSAEHP TPLNPPTPSP
     TPDVPPPDSP GNPSLLKQVP PEANLHPIHN PDLPSSTTLP SGALTLVPAK TPSIYANPTP
     PSSHPFTPLA DDPTAVGPCL PFHVLHPADY FPLSAEFLTR TRHVPPSSLS HPKLNCLLTC
     FSELSGHSES DLWLSLQSIL PDSQLQNPEV STLGLSTDIL TALCFIYHSS VTLHAPSGVY
     HYGIASSSTV YVIHYQPGPP PHFSLSPRLA ASAPRCNPTN SRLVRQALRF KLNGEFLPFT
     QAYAHESSIT HAKNLISNMK NGFDGIMSSL TDSSKGPSPR EKLTTLDSLI DVAAPREVSL
     IHIAGFAGCG KTHPIQKLLQ TSPFHDFRIS CPTNELRSEW KRDMQPTAEN VWRFSTWESS
     LLKHSEILVI DEIYKLPRGY LDLSILADPT LSLVIILGDP LQGEYHSTSP HSSNHFLPSE
     VHRFKSYIDC YCFWSHRIPK QIASLFGVVC HNTNEGFVRA LTSHPPNSKN LTNATNTALS
     LQQMGHHAIT ISARRVTFTE AHTILLDRHT NLLSPNNCLV ALTRSRTGVY FVGNLHLASN
     SFGTNYMFSQ ALCQGTIDLN NVFPHIMPHL PKMYEPIRSR SNRFVSGSLN FRPTTNSRLL
     SSLTKPTHLP PHIPTNHSLD VLVSNPVLLG ETLDPRLEVL HLPPTRLPLH LDLLPTVPSS
     SSFSSVDHLF PTPISPAICG YTFENLAAFF LPAHDPDLKE VLINDQKSNQ FPYLDAPFEL
     SCQPSSLLAP IHKPASDPTL LPGSIKKRLR FRASSSPYSI TPSDQLLGQH LFSSLCLAYG
     RNPNSVLPFQ PELFSECICI NDYAQLSSKT QATIVANHQR SDPDWRLTAV RIFAKAQHKV
     NDASIFSGWK ACQTLALMHG YIILVLGPVK KYQRIFDSKD RPPHIYYHCG KTPSQLSQWC
     QTHLSGSSYI ANDYTAFDQS QHGEAVVLEC LKMRRLSIPD SLIQLHSHLK CSVDTQFGPL
     TCMRLTGEPG TYDDNSDYNL AVIYSQYSLN GHPILISGDD SVLCGTPPPS PLWPTLKKML
     HLRFKIERTS HPLFCGYYVS PHGAARNPYA LFAKLMICVD DKSLHDKKLS YLSEFSTGHL
     AGDLVTSILP SHLLPYQSAV HDFFCRNCTP AEKILLSLDP IPESKILQLI LKVRWASQAF
     FSYLPQKARE LLVARSSLPS LYSNPKVSQL ESELLPFSQ
 
 
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