POLR_NORAV
ID POLR_NORAV Reviewed; 2104 AA.
AC Q27YG9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 23-FEB-2022, entry version 64.
DE RecName: Full=Replication polyprotein;
DE Includes:
DE RecName: Full=Membrane protein;
DE Includes:
DE RecName: Full=Helicase;
DE EC=3.6.4.-;
DE Includes:
DE RecName: Full=Protease;
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
GN ORFNames=ORF2;
OS Nora virus.
OC Viruses; Riboviria; unclassified Riboviria; unclassified ssRNA viruses;
OC unclassified ssRNA positive-strand viruses.
OX NCBI_TaxID=363716;
OH NCBI_TaxID=7227; Drosophila melanogaster (Fruit fly).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16963764; DOI=10.1099/vir.0.81997-0;
RA Habayeb M.S., Ekengren S.K., Hultmark D.;
RT "Nora virus, a persistent virus in Drosophila, defines a new picorna-like
RT virus family.";
RL J. Gen. Virol. 87:3045-3051(2006).
RN [2]
RP SEQUENCE REVISION TO 1708-1721.
RA Ekstrom J.-O., Habayeb M., Hultmark D.;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The peptidase activity is involved in polyprotein maturation,
CC possibly along with hosts proteases. Transmembrane protein may be
CC surface viral glycoprotein. RNA-directed RNA polymerase replicates the
CC viral genome (Probable). {ECO:0000305}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC {ECO:0000305}.
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DR EMBL; DQ321720; ABC55268.2; -; Genomic_RNA.
DR SMR; Q27YG9; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR SUPFAM; SSF56672; SSF56672; 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; Membrane;
KW Nucleotide-binding; Nucleotidyltransferase; RNA-directed RNA polymerase;
KW Transferase; Transmembrane; Transmembrane helix; Viral RNA replication.
FT CHAIN 1..2104
FT /note="Replication polyprotein"
FT /id="PRO_0000283695"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 329..501
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1838..1965
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1499..1520
FT /note="Viral peptidase"
FT /evidence="ECO:0000255"
FT COILED 289..313
FT /evidence="ECO:0000255"
SQ SEQUENCE 2104 AA; 239183 MW; 8C286C774AD588C3 CRC64;
MLIEAFINSL LQNLGIMMSF RDLVASPWIL LVIAIPLCAF ASSASMVREM LFRHKITENI
LKGTGVEELF NPFGIIIKYF LYFAILYAFI KYIRNNINVI TEKVNFIRRV VSNPTGTTGR
RGVLGRCVEQ IVEYPTFFIT MVYELQQIKN KKDLISKITM ISSILKLPLG IWESTVGRML
DRPAIEGTEE MLEDVLPIVA MGLTITKTQI GDVPVESFLV NLDRNQKACE NIIKRMQPLM
IKMGMMKDSS YDTILQVAKE VNELSEAETW MKTTLKLNPN EFLQTQGAVR VGEIREKVAT
LRNKLNTLQT KELRSDKVVT ECQKHLASLE VLLIEVKVLE NSNQTRVKPV GVTIQGEKQI
GKTNLVAILS RKICEYVQEH GDISFRNATK WTTWSRQCRD EFDTGYTGQE ITYVDDAFQQ
KDNKDHLMWF TFISNTAVGT NQADLKQKGL PYRSKLVFTT CNKSPDKSVT IEDIEALHAR
FPHTICLRRN KNKMPKRGAI DESYDWVDFY YGPMSKAVSA IGSNTTSTLK TMSLSEIVKI
IGDDLIIQNN FYNSTIKDVG ITGQEQMDGA QLERRQRMRE LRDHLLRIRS GDENMPFLDE
TFELNSRPIQ TDEKFIPLKD NLDEEVMYGG ISDQLLTRFD NIIERSLEGY DVESRELGVE
PLTTLNHVRS NMLSYRAWNL INSMCINKTE TFSAWLGRYI TECVEGVAEN LVTTKVKIRI
NPFTGLQLIA AKRMLQENKL IDMDEIPSTS ANSYETVYDQ IKNFVNDELS LMETDVVDLA
LAKISLSQIR SNIKRSTWLD VNDWILALKH KISGKSFAKH MDLYPSSLDS FLLTLKDWEV
EDRIKFNSIY KQKVLFVQSR FSLYCWSPFI SRGTRFVKVT SRFRELVDKL ETGILFHEIK
SVTNGIRWLG GAGNNGHVGE RVRVIAHTAQ FPKKSYPQNG FPINEELHRE WIQLVINSDY
KYHSLIGEEK VNILWNLIRL QPQREVENFK VYLEDLQASP PKTGTICAKV VNDIKAEVTS
SYRQFNNYYT RLTKDGMHTL LSMLSRIGVP ISDYWNDLLV DKAPAITAVT VGAITSLAII
TIVKTFQYAI AGEEQSKGEK RAKQKNIATT KLQKLKFTLG KEQAEGDSIE HVKEFDGDVK
FETIEKLFDH IDEHPNLNIV GLNLVAPENP IAIYAAREES YDFSFSEPRP PQWKKVVTFK
EDSKRIISLQ LRGEDTEDNI LDEIEHAIKV SHGMPYAEWI FNGWFKKESN DNILYCVELD
LVTAKTQSGP VGWTRAQTKN LKDLEIQLNK GKPIDVKSVV LGAPQASTQA TDTMDVLVNK
HLVKVHCLSY ENLNNLALNG TQVFALASDN ILIVPAHAAR QNKWIRFSRA TQTGHYGVAK
VDERRIDFTR DIAIAIILTR AEAEQKLCEL GYSIQLTNIS KEKFHFPLIT KYLLTADQSE
VEWMNCTTLH YFAKNKTVGL GRTTSFQVSE FLCGNEYISK KLVACAQGLQ SSVELSRLGD
CGSPIVLASG KKAGKLIGFH GYHSPNLQTW YGAMLTVEDL GIINGVEEHF DDPWAKLITQ
GLPVDLPIGP EVEYVGNLIR PSLPVTNDSL DHWHKSPFAD QFEEQLAPGR LNPYDSYIEG
DLPTNLEGRK SLILGPNSEM AKTLPELDQG ILDWIVDQLV VEQVATFKAE NLLTKVSDDI
DEMLDYALNG NVDNTYVRGM EVNKASGLPW SLSGSPKKSD FIDVDEATGV RSFKVNANGD
ALKNRVILKL QQAKMGNRIL SFSSSKLKDQ PIKIAQAKSG RTRVFHCIPV DLILFSGALY
GPYKEAYTKA GLKCYHAVGI DPKSVGWQQL ATYMTKHPNY FDADYKNYDK YLHRQVFKAV
RKIQRSVIQQ VCPDKWDKAR AVEELDAIDT YVVDYQTVYK TNRGNKSGSY TTTIDNCLAN
DIYGLYAWVK TTGLRSLWDY RQNVSSVAFG DDIIKSVSDE YKDKYNYCTY RDVLNATGHI
MTPGSKDGEE KPFTSFENLQ FLKRGFKLEN GMVLAPLLQR SIEGPFVWTD IREDQITVWV
NLVQEQLIEA ALWGEEYYNE LCQKLKCGTN RTLNGALAVL LNTSWEVTFQ KFCNRYYGIK
RGDL