RDRP_SCVLA
ID RDRP_SCVLA Reviewed; 1505 AA.
AC Q87022; Q87023;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Probable RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=Gag-Pol protein;
GN Name=gag-pol;
OS Saccharomyces cerevisiae virus L-A (ScV-L-A) (ScVL1).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Chrymotiviricetes;
OC Ghabrivirales; Totiviridae; Totivirus.
OX NCBI_TaxID=11008;
OH NCBI_TaxID=4932; Saccharomyces cerevisiae (Baker's yeast).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2651431; DOI=10.1016/s0021-9258(18)83488-3;
RA Icho T., Wickner R.B.;
RT "The double-stranded RNA genome of yeast virus L-A encodes its own putative
RT RNA polymerase by fusing two open reading frames.";
RL J. Biol. Chem. 264:6716-6723(1989).
CC -!- FUNCTION: RNA-dependent RNA polymerase which replicates the viral
CC genome. Catalyzes the transcription of fully conservative plus-strand
CC genomic RNAs that are extruded from the virion into the cytoplasm where
CC they function as mRNAs for translation of viral proteins and also as
CC substrates for encapsidation to form new virions. Once encapsidated,
CC the positive strand is converted to dsRNA by the RNA-directed RNA
CC polymerase. Displays ssRNA-binding activity.
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;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=RNA-directed RNA polymerase; Synonyms=Pol protein;
CC IsoId=Q87022-1; Sequence=Displayed;
CC Name=Major capsid protein; Synonyms=Gag protein;
CC IsoId=P32503-1; Sequence=External;
CC -!- MISCELLANEOUS: One molecule or two of Gag capsid protein is replaced in
CC the virion by Gag-Pol because the fusion protein is essential for RNA
CC encapsidation and replication.
CC -!- MISCELLANEOUS: [Isoform RNA-directed RNA polymerase]: Produced by -1
CC ribosomal frameshifting.
CC -!- SIMILARITY: Belongs to the totiviridae RNA-directed RNA polymerase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50507.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAA50508.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; J04692; AAA50507.1; ALT_SEQ; Genomic_RNA.
DR EMBL; J04692; AAA50508.1; ALT_SEQ; Genomic_RNA.
DR RefSeq; NP_620493.1; NC_003745.1.
DR RefSeq; NP_620495.1; NC_003745.1.
DR SMR; Q87022; -.
DR PRIDE; Q87022; -.
DR GeneID; 940476; -.
DR GeneID; 940478; -.
DR KEGG; vg:940476; -.
DR KEGG; vg:940478; -.
DR Proteomes; UP000000351; Genome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 Gene3D; 3.90.1840.10; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR015302; Major_coat_LA-virus.
DR InterPro; IPR036332; Major_coat_LA-virus_sf.
DR InterPro; IPR001795; RNA-dir_pol_luteovirus.
DR Pfam; PF09220; LA-virus_coat; 1.
DR Pfam; PF02123; RdRP_4; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF82856; SSF82856; 1.
PE 3: Inferred from homology;
KW Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Ribosomal frameshifting; RNA-binding; RNA-directed RNA polymerase;
KW Transferase; Viral RNA replication.
FT CHAIN 1..1505
FT /note="Probable RNA-directed RNA polymerase"
FT /id="PRO_0000402407"
SQ SEQUENCE 1505 AA; 170480 MW; B900A831DD49F72A CRC64;
MLRFVTKNSQ DKSSDLFSIC SDRGTFVAHN RVRTDFKFDN LVFNRVYGVS QKFTLVGNPT
VCFNEGSSYL EGIAKKYLTL DGGLAIDNVL NELRSTCGIP GNAVASHAYN ITSWRWYDNH
VALLMNMLRA YHLQVLTEQG QYSAGDIPMY HDGHVKIKLP VTIDDTAGPT QFAWPSDRST
DSYPDWAQFS ESFPSIDVPY LDVRPLTVTE VNFVLMMMSK WHRRTNLAID YEAPQLADKF
AYRHALTVQD ADEWIEGDRT DDQFRPPSSK VMLSALRKYV NHNRLYNQFY TAAQLLAQIM
MKPVPNCAEG YAWLMHDALV NIPKFGSIRG RYPFLLSGDA ALIQATALED WSAIMAKPEL
VFTYAMQVSV ALNTGLYLRR VKKTGFGTTI DDSYEDGAFL QPETFVQAAL ACCTGQDAPL
NGMSDVYVTY PDLLEFDAVT QVPITVIEPA GYNIVDDHLV VVGVPVACSP YMIFPVAAFD
TANPYCGNFV IKAANKYLRK GAVYDKLEAW KLAWALRVAG YDTHFKVYGD THGLTKFYAD
NGDTWTHIPE FVTDGDVMEV FVTAIERRAR HFVELPRLNS PAFFRSVEVS TTIYDTHVQA
GAHAVYHASR INLDYVKPVS TGIQVINAGE LKNYWGSVRR TQQGLRSGRS YDASCNAYRR
TYSWRCPRRV DRTGGQCFSR VNVIEPSHGP RPTRYILQEP GTYPAWIRFR NRVQAVSRQK
ATHFLFDIVP AAVISDFTTS DTSSFAYKSH TYAVNVTALR FSDTYALYVQ TDTNMTILSP
AARRQASATY SQVAGFCYNT PTVMDSLANI LDVDRNIRPK HFKGLRLYTR SKVTAQHHTH
LRPDELVEAA AKVSPRRKYY LMCVVELLAN LQVDLEAAVA TILAYVLTLS EKFVPIFLDS
RAIWVGEPGP DALTARLKAS SGQIKSIHTA DYEPLTELFE LAVLMNRGVG HVSWQAEKDH
RLNPDVAVVD QARLYSCVRD MFEGSKQTYK YPFMTWDDYT ANRWEWVPGG SVHSQYEEDN
DYIYPGQYTR NKFITVNKMP KHKISRMIAS PPEVRAWTST KYEWGKQRAI YGTDLRSTLI
TNFAMFRCED VLTHKFPVGD QAEAAKVHKR VNMMLDGASS FCFDYDDFNS QHSIASMYTV
LCAFRDTFSR NMSDEQAEAM NWVCESVRHM WVLDPDTKEW YRLQGTLLSG WRLTTFMNTV
LNWAYMKLAG VFDLDDVQDS VHNGDDVMIS LNRVSTAVRI MDAMHRINAR AQPAKCNLFS
ISEFLRVEHG MSGGDGLGAQ YLSRSCATLV HSRIESNEPL SVVRVMEADQ ARLRDLANRT
RVQSAVTAIK EQLDKRVTKI FGVGDDVVRD IHTAHRVCGG ISTDTWAPVE TKIITDNEAY
EIPYEIDDPS FWPGVNDYAY KVWKNFGERL EFNKIKDAVA RGSRSTIALK RKARITSKKN
EFANKSEWER TMYKAYKGLA VSYYANLSKF MSIPPMANIE FGQARYAMQA ALDSSDPLRA
LQVIL
