ID K7XAQ9_9MONO Unreviewed; 2271 AA.
AC K7XAQ9;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=RNA-directed RNA polymerase L {ECO:0000256|PIRNR:PIRNR000830};
DE Short=Protein L {ECO:0000256|PIRNR:PIRNR000830};
DE AltName: Full=Large structural protein {ECO:0000256|PIRNR:PIRNR000830};
DE AltName: Full=Replicase {ECO:0000256|PIRNR:PIRNR000830};
DE AltName: Full=Transcriptase {ECO:0000256|PIRNR:PIRNR000830};
DE Includes:
DE RecName: Full=RNA-directed RNA polymerase {ECO:0000256|PIRNR:PIRNR000830};
DE EC=2.7.7.48 {ECO:0000256|PIRNR:PIRNR000830};
DE Includes:
DE RecName: Full=GTP phosphohydrolase {ECO:0000256|PIRNR:PIRNR000830};
DE EC=3.6.1.- {ECO:0000256|PIRNR:PIRNR000830};
DE Includes:
DE RecName: Full=GDP polyribonucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000830};
DE EC=2.7.7.88 {ECO:0000256|PIRNR:PIRNR000830};
DE AltName: Full=PRNTase {ECO:0000256|PIRNR:PIRNR000830};
DE Includes:
DE RecName: Full=mRNA (nucleoside-2'-O-)-methyltransferase {ECO:0000256|PIRNR:PIRNR000830};
DE Short=N1-2'-O-MTase {ECO:0000256|PIRNR:PIRNR000830};
DE EC=2.1.1.- {ECO:0000256|PIRNR:PIRNR000830};
DE Includes:
DE RecName: Full=mRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|PIRNR:PIRNR000830};
DE Short=G-N7-MTase {ECO:0000256|PIRNR:PIRNR000830};
GN Name=L {ECO:0000313|EMBL:AFX75110.1};
OS Achimota virus 1.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Pararubulavirus; Pararubulavirus achimotaense.
OX NCBI_TaxID=1261100 {ECO:0000313|EMBL:AFX75110.1, ECO:0000313|Proteomes:UP000119395};
RN [1] {ECO:0000313|EMBL:AFX75110.1, ECO:0000313|Proteomes:UP000119395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23152534; DOI=10.1128/JVI.01202-12;
RA Baker K.S., Todd S., Marsh G.A., Crameri G., Barr J., Kamins A.O.,
RA Peel A.J., Yu M., Hayman D.T., Nadjm B., Mtove G., Amos B., Reyburn H.,
RA Nyarko E., Suu-Ire R., Murcia P.R., Cunningham A.A., Wood J.L., Wang L.F.;
RT "Novel, Potentially Zoonotic Paramyxoviruses from the African Straw-Colored
RT Fruit Bat Eidolon helvum.";
RL J. Virol. 87:1348-1358(2013).
CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the replication of
CC viral genomic RNA. The template is composed of the viral RNA tightly
CC encapsidated by the nucleoprotein (N). The replicase mode is dependent
CC on intracellular N protein concentration. In this mode, the polymerase
CC replicates the whole viral genome without recognizing transcriptional
CC signals, and the replicated genome is not caped or polyadenylated.
CC {ECO:0000256|ARBA:ARBA00003132}.
CC -!- FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription
CC of viral mRNAs, their capping and polyadenylation. The template is
CC composed of the viral RNA tightly encapsidated by the nucleoprotein
CC (N). The viral polymerase binds to the genomic RNA at the 3' leader
CC promoter, and transcribes subsequently all viral mRNAs with a
CC decreasing efficiency. The first gene is the most transcribed, and the
CC last the least transcribed. The viral phosphoprotein acts as a
CC processivity factor. Capping is concommitant with initiation of mRNA
CC transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase)
CC adds the cap structure when the nascent RNA chain length has reached
CC few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and
CC facilitates subsequent guanine-N-7 methylation, both activities being
CC carried by the viral polymerase. Polyadenylation of mRNAs occur by a
CC stuttering mechanism at a slipery stop site present at the end viral
CC genes. After finishing transcription of a mRNA, the polymerase can
CC resume transcription of the downstream gene.
CC {ECO:0000256|PIRNR:PIRNR000830}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001270,
CC ECO:0000256|PIRNR:PIRNR000830};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-methionine = a
CC 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-
CC adenylyl-cytidylyl-adenosine in mRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65440, Rhea:RHEA-COMP:16798, Rhea:RHEA-COMP:16801,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156482,
CC ChEBI:CHEBI:156483; Evidence={ECO:0000256|ARBA:ARBA00024499,
CC ECO:0000256|PIRNR:PIRNR000830};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N(7)-methyl
CC 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65376, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16798,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156483, ChEBI:CHEBI:156484; EC=2.1.1.375;
CC Evidence={ECO:0000256|ARBA:ARBA00024634};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-
CC adenosine in mRNA + S-adenosyl-L-methionine = a 5'-end (5'-
CC triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-
CC adenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:65380, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16801,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156482, ChEBI:CHEBI:156484;
CC Evidence={ECO:0000256|ARBA:ARBA00024452,
CC ECO:0000256|PIRNR:PIRNR000830};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in
CC mRNA + GDP + H(+) = a 5'-end (5'-triphosphoguanosine)-adenylyl-
CC adenylyl-cytidylyl-adenosine in mRNA + diphosphate;
CC Xref=Rhea:RHEA:65436, Rhea:RHEA-COMP:16797, Rhea:RHEA-COMP:16799,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:156484, ChEBI:CHEBI:156503; EC=2.7.7.88;
CC Evidence={ECO:0000256|ARBA:ARBA00024494};
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|PIRNR:PIRNR000830};
CC -!- SUBUNIT: Interacts with the P protein. {ECO:0000256|ARBA:ARBA00011706}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Virion
CC {ECO:0000256|PIRNR:PIRNR000830}. Host cytoplasm
CC {ECO:0000256|PIRNR:PIRNR000830}.
CC -!- SIMILARITY: Belongs to the paramyxovirus L protein family.
CC {ECO:0000256|ARBA:ARBA00007934, ECO:0000256|PIRNR:PIRNR000830}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX051319; AFX75110.1; -; Viral_cRNA.
DR RefSeq; YP_009094458.1; NC_025403.1.
DR GeneID; 21011904; -.
DR KEGG; vg:21011904; -.
DR Proteomes; UP000119395; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12760; -; 1.
DR InterPro; IPR039736; L_poly_C.
DR InterPro; IPR026890; Mononeg_mRNAcap.
DR InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR InterPro; IPR025786; Mononega_L_MeTrfase.
DR InterPro; IPR016269; RNA-dir_pol_paramyxovirus.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR NCBIfam; TIGR04198; paramyx_RNAcap; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 1.
DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
DR PROSITE; PS51590; SAM_MT_MNV_L; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000830};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200,
KW ECO:0000256|PIRNR:PIRNR000830}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR000830};
KW mRNA capping {ECO:0000256|PIRNR:PIRNR000830};
KW mRNA processing {ECO:0000256|PIRNR:PIRNR000830};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000830};
KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000830};
KW RNA-directed RNA polymerase {ECO:0000256|PIRNR:PIRNR000830};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR000830};
KW Transferase {ECO:0000256|PIRNR:PIRNR000830};
KW Viral RNA replication {ECO:0000256|PIRNR:PIRNR000830};
KW Virion {ECO:0000256|PIRNR:PIRNR000830}.
FT DOMAIN 664..848
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50526"
FT DOMAIN 1787..2000
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51590"
SQ SEQUENCE 2271 AA; 257727 MW; 5D0DE98EF086D379 CRC64;
MAAPSQIILP EVHLDSPIVQ NKLLYLVRVA GLPLPDLFFE DDHFPGVDWQ RVRREENRLS
SRLESVRSRL LSKLNTARGK NPINKTAPLI RLWPSCLPFI HEFVFPDALA RFSEADRITA
QAIQHLSPGI TALLNSISQK LTHCTELFSH NETKCTEPEY HTRPRNLNDL NNCYVGAEWK
DQFNMWFLIR HQMRLLIMKN NESVNPNLIV EIDYREKAAI ITPELVTLWS SESNFVTYFT
FEMVLMVCDL YEGRMNVIAV AKMSCYLSPL VPRLKKIFSI VDDLCLMLGN QVYPVVASLE
SLVYGQLQLL DPVEEVCGDF YSFICSELVT ALLASDQITL ENAISIAGSL TSCYCGISPD
LVAELLCVMR LWGHPMLTSE KAAEKVRKSM CAPKVIDLET TLKTLAFFNE IIINGYRRKH
NGIWPKCKLP PFASLSLREL KHDNSELSHQ YTLTHWKEIA YIEFEKSFDA DPGDDLSIFM
KDKAISAPKK DWLSVFRKSL IKPLCESLHS PLPEPFNRRL LLNFLNDDSF DPAVELQYVT
SGEYLDDETF CASYSLKEKE IKETGRIFAK LTKKMRSCQV ISESLLASHA GKLFRENGVV
MDHLNLTKSL LTMSQIGLIS RKERRNVREN ITVVSKISKH DKSSVQNPGF KPDHPNVSEV
TEIAAFFLTT DLQKYCLNWR YQSIILFATN LNKLYGYTHL FEWIHLRLMR STLYVGDPFN
PPRFIDTTNL DEVPNEGIFI VSPRGGIEGL CQKMWTMISI AVIILSATEA NTRVMSMVQG
DNQAIAITAK VPRAVPYREK KRIAYENSKL FIERLRANNK GLGHHLKEQE TILSSEFFVY
SKRIFFRGRI LSQALKNVSK LNLIADVLSE CSQTSCANLT TTVMRLTENG VEKDICYFLS
IFLSVRQLVY DLLFPMTTFI EDSITTLYLN HPILIARLCV LPSQLGGLNN YSISRLFNRN
IGDPLTSAIA DLKRFINVGI LPKWILSNLL SRDPGEGTWS TLSSDPYALN INYLYPPTTY
LKKHTQRVLI EHSVNPMLYG IFTDDALQEE NRLSQFLLDR PIVMPRVAHI IIEQTSCGRR
RQIQGYLDTT RTIIRHALSR QPPGYKKVEK ILEYNRLYLA YNQELIAKPN KKRALRAKDE
ELLPVCSIDL SKLLRKLSWS SLLSGRGIDG LETPDPIELV TGYLIQGNDT CLPCLQGDRK
FTWFFVPPGI TLDAPPEDNP PIRVPYIGSR TDERRVASLG YVKGATPALK AALRLAGVYI
WAFGDTDTNW DDAYHLASTR ISITLDQLRA LTPLPTSANL THRLDDGLSQ MKFTPASSYA
YSSYVHISND NQNLEVLQKQ LDSNLIYQQL MILGLGIIET WLQLPQWENK NDLSLHLHTG
GSCCVRPVDM CIVNESDVEV PTLVVPYSNK FVYDQNPLNH EDQLHIGNLS FQANLSGLDL
IPTLEKIPLL AHLVGMQFSH SISGLDESVS LMNDAVVETD YANNWISECL NTQLDKVFYY
AAWSVMLEMS YQMYYLRITG PTAIADYISI VLDRIPGLAL TGISSTINHP KILRRLINLG
IVVPSNSPYL ATLDYQKITT SAIMWGVHKV LSDISAGIDI ELVIPSEDST ELSDRVLNLI
ARKLSLVSLI LTISKDLAYV RGLTPEQKCK SLTDKLMAEL DLYYIDPELA NKLKLMICEP
KISAFPSNHY YLMRKLLNWI RESDEAQCFL SAYYDSFGFL DTMIQIDPLP SNDEENSAMA
TLTKFDFTVS LTNIDKDAEK HCYPKTDPSL QLFMKGVPDP PIHHVLRPIG LSSTSWYKGL
SIINILKRMK IPSGDHLYLA EGSGALMTLI ETYFPGNKIF YNSLFSSGQN PPQRNFKPLP
TQFAESMVYM NIMQQESTLE DGVELFVPLW SGYSKQTDLG TKECVEYILE SVAGNRVTLI
SSDLEEGLGV NPGVISKAMI HTILLAYLLL RENGIFILKV NFTPFSKFSR IISLIYQKFK
DVTILRSAYS DPSHDEFYLV AVASCESTVT DFNQARYISE SIDESSLTLI SSEVISQIHT
ELEIHKNDVL DVINIQIATA QCNENYDDHL LLTRLASVNH LNRVFLTEAS ASLHDMVERI
SAVVTLYLKE TINIIESAQL DRTKLIYNSY NVSNYGKIRT SAKITARLIL DIIIRNWTRL
GNGLRIRVKN SIEQGQFVLS CVMTPATFLK YSTARRYITK TLGLDQLNIE FTQNIQCLLS
RSEQKRVWKD IGCMVFVESQ FTDQISDDIP DSDFIWDEDE QIERGIDGEE I
//
