ID D2VSR9_NAEGR Unreviewed; 942 AA.
AC D2VSR9;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=RNA-dependent RNA polymerase {ECO:0000256|RuleBase:RU363098};
DE EC=2.7.7.48 {ECO:0000256|RuleBase:RU363098};
GN ORFNames=NAEGRDRAFT_72038 {ECO:0000313|EMBL:EFC40243.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC40243.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC40243.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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:0000256|ARBA:ARBA00024517,
CC ECO:0000256|RuleBase:RU363098};
CC -!- SIMILARITY: Belongs to the RdRP family. {ECO:0000256|ARBA:ARBA00005762,
CC ECO:0000256|RuleBase:RU363098}.
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DR EMBL; GG738894; EFC40243.1; -; Genomic_DNA.
DR RefSeq; XP_002672987.1; XM_002672941.1.
DR AlphaFoldDB; D2VSR9; -.
DR EnsemblProtists; EFC40243; EFC40243; NAEGRDRAFT_72038.
DR GeneID; 8860062; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_72038; -.
DR eggNOG; KOG0988; Eukaryota.
DR InParanoid; D2VSR9; -.
DR OrthoDB; 2735303at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProt.
DR InterPro; IPR007855; RNA-dep_RNA_pol_euk-typ.
DR PANTHER; PTHR23079; RNA-DEPENDENT RNA POLYMERASE; 1.
DR PANTHER; PTHR23079:SF55; RNA-DIRECTED RNA POLYMERASE; 1.
DR Pfam; PF05183; RdRP; 1.
PE 3: Inferred from homology;
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU363098};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU363098};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW ECO:0000256|RuleBase:RU363098};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363098}.
SQ SEQUENCE 942 AA; 109669 MW; 6CB40F070E1A3AAF CRC64;
MRDEDLQTIT GWEDWNVLGF GKNVWKIVVK IDNVQYSELS AKISYMCDST MDLAKNPLEY
LMKRYRYFAR ELELFESQAN QTLFQSLFNS NVAGGYEQFF GEFYPLVCHV KNRWKKMEGN
NGKYAIIGDG TNRYSILNSF SRLARILMSL NLGKCLMVVK FDFTSKEDLK ALSECKKEYC
LSYGIVHEGH KYCLLGTSNS GLKGDSCIFY NSTLLNLEIL KQMLGTFEKA EEHGPRKVAS
RVGLSMGTST PSIVEWKQDD IQIISDDIAV TDGAGMAVED FFEQVLENTY SVPYFFMDKL
FESDTKQGRL FEKNFKNISA MQVRILGAKG VIQKVNKSMW AELLKKHKLP SNTKVILRNS
MVKFEGNYSI YNKIDILNVA RVHGGNINRN IMSCLLQMTT NEEEMEKLFK NFYETQLMEI
VENKDNPEYL CNVLLSQSGE TSQESIARDL IMAEHSLDNY FISSVVKDNI ESKFESMVSD
KLSMKCKHPG FLSGMGVYDE SSTLKHDEVH IPCSKLIRSL DYAKIDKVLV YRNPLAYEGD
IQCLKLVKHP PTEFLQSRRD VIVFGHNPNY KKVPEPLCYM AGGDLDGDLY EIIFDPEIVK
LFDQNLKPKL NYNDGAATNK VTKTVKNSLS MEDVRKTVLE MMEQSSKISE VYLKTMCWRE
DSSKVGIDIK LKLSKMYHDS IDTIKGSAFN AKQLYEIPKK DSPKWMELCK LKITDQSHIE
LDTFEARMFD LIRNIFNRMV FSDTKQLDTV FENPSEIYSS EWQRWKDEFK EAYSQWRLYW
STRKNDEIVL SDKFSAHKQK LFESIKDCLE EDKINWEKVF IKHDGDSLDK LNHKAAYWLF
HTYNQYIEED DNEFNLEERF KSLIRSPFVY TCCLFNLNCF KLFNNQEEKM PHIVSPRFTI
RIKQSRNEKV SKTILLECPL NNYFLDLSYC FPLSKEREFP SF
//