ID B0CNU3_LACBS Unreviewed; 1268 AA.
AC B0CNU3;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=RNA-dependent RNA polymerase {ECO:0000256|RuleBase:RU363098};
DE EC=2.7.7.48 {ECO:0000256|RuleBase:RU363098};
GN ORFNames=LACBIDRAFT_301565 {ECO:0000313|EMBL:EDR15354.1};
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN [1] {ECO:0000313|EMBL:EDR15354.1, ECO:0000313|Proteomes:UP000001194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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; DS547091; EDR15354.1; -; Genomic_DNA.
DR RefSeq; XP_001873562.1; XM_001873527.1.
DR AlphaFoldDB; B0CNU3; -.
DR GeneID; 6068993; -.
DR KEGG; lbc:LACBIDRAFT_301565; -.
DR HOGENOM; CLU_003387_0_0_1; -.
DR InParanoid; B0CNU3; -.
DR OrthoDB; 2735303at2759; -.
DR Proteomes; UP000001194; 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:SF14; RNA-DEPENDENT 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:UP000001194};
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}.
FT REGION 40..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 140609 MW; 692A7A22539C4698 CRC64;
MSRSSTPMVT RTGSGDLDVD SDYFNDEDAL FCSAVAGLSN ESFDNSPLRA PKKRYSDKTR
GTPSGSTPNV ASSFHATRTP ESNPFAKELF ATAVKKAASS ASATRRQNPI PITPSKTPAK
YPVKQTPVDV SSTIRKELAK IDISDSSSPS PPAKRLFVKP LASKSDEKRK MIVVGDTDSD
TEELFTDTDC SPINPSSNSS FAYPLSGSNS SFSFVSSQSS SSGPSSQEGK LDRHGANSSP
QKARTPFTEG VPLKSTFFCK PNTQLTSDAP ISTTPPLPVA TTQSVTPATP IPESVTEFCK
KSLSTKLDSY IIAHCSTTQS IFEDHNIAWG TQYELARGVT HCTWTWEQVR EQVPNLTGPN
TTAAYKVRAV MRGKAIPLKK QNFAVWAELD REQDAIKENL SRGLGLMGPW KGDPDWHGGQ
VQQLAQLVKV NGSLKVQLEP LEKRRSHRFA RFYGSRRIIQ LRIPDDMVTK DNATVKQFLS
QKFILLGRIF VPFHSKDGGV YMVETDQNSG RIPKGSCGDQ YRLSFDAFMR WHNPLEYNFK
QAASKFVTRY ALGLSNSIPA LEFSVENIIF IRDIYAEDWH GEDHKAPAEK IMTDGCGFIN
LTAMKIIKKK FNYDSLPTGI QGRIAGAKGM WIRHPTDDSL EPKIWIRDSQ NKIKLSELDK
AHRIFDLLSV SKPSSSIALS QQSILNLSFN GIPDDVLVKL LEQGIVDEVM PLLDWKRPNA
MTVLWDAINK SAGVSGSRTQ RVAAGASRAL GFQRQDWGHD DVVADQDAET QDISGTTYTG
RNEYSKAPLA LHEMTMELIQ AGFHPSQCKI LQDKIKFMVQ QTINSSVEKY RIPIKESTGG
YIVADPTGLL EEGQIYYRSS VPMTDPDTEM DYFVLQGEVV LGRYPIRLPS DMQKVTAVDI
PELFNWPDVI IVSTKGKFSL ASLLSGGDQD GDELLVIKDK LIVDSFKNQP LTVIPSGLME
SDFEREVESV PDFCCRALSL EEAASHKAFQ EVLLLNLNVS QVGLYSTFHE NAIWKYGYSH
PETVRLAYIF CILLDSSKTG HRLKSGIFEK DRKRYVGQEE PSGILHRLLK AGRTKGDELI
QAFHDACKEN LVKDKAILEP YNTASNYALV TFDTNKVVGQ MFLDELTRIR KHVDDAHLEF
GKSANHHTPD TPTPGTPSKK SKKAKSYRAT ADQDDKMLAA AQKYAEPLEG IILTRDLESV
MASYAYAASK SPHFAFTVAF QQICTIKAKS CKGGIAPSTR EFDEARKITA SFLRALNRGT
DDNYYGSY
//
