ID A0A2P1GN50_9MONO Unreviewed; 2055 AA.
AC A0A2P1GN50;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
OS Wenling hoplichthys paramyxovirus.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Hoplichthysvirus;
OC Hoplichthysvirus hoplichthysis.
OX NCBI_TaxID=2116453 {ECO:0000313|EMBL:AVM87400.1};
RN [1] {ECO:0000313|EMBL:AVM87400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XYXMC57250 {ECO:0000313|EMBL:AVM87400.1};
RX PubMed=29618816; DOI=10.1038/s41586-018-0012-7;
RA Shi M., Lin X.D., Chen X., Tian J.H., Chen L.J., Li K., Wang W., Eden J.S.,
RA Shen J.J., Liu L., Holmes E.C., Zhang Y.Z.;
RT "The evolutionary history of vertebrate RNA viruses.";
RL Nature 556:197-202(2018).
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}.
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DR EMBL; MG600062; AVM87400.1; -; Viral_cRNA.
DR Proteomes; UP000297191; 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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR039530; L_methyltransferase_rhabdo.
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; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF14314; Methyltrans_Mon_2nd; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PIRSF; PIRSF000830; RNA_pol_ParamyxoV; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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|PIRNR:PIRNR000830};
KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR000830};
KW Reference proteome {ECO:0000313|Proteomes:UP000297191};
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 609..793
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50526"
FT DOMAIN 1686..1872
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51590"
SQ SEQUENCE 2055 AA; 232496 MW; C1CE6CC2E6D464B5 CRC64;
MYFEEDADEG GVPGHDILLP EIRLGSPICL GKLALIQEIS GIDFAISLRD DAIIKNYRGK
SAISKTGERH VVTDCAKEIR RSLMSRFPKI RSMQPVDPHK FILQSQDRWD RKVAQVSEEN
IETAVREMIS NMDRYTDWIK TISEVWDCKS TEDPKADMIE AMGRYATSMY RGPFSCWNSV
RKQFRAIIHR YESKKASSAT KAKVLDFDRW TLIITCTAMV IVDRRTLTYT IMDLNLVLMA
VDLFESRWVI DMLTDNISEK RSNLRVIWDQ IDRIICDHGP KGYQLVGFLE PLLVGSVEVK
GEIISETQFD FLEKQCEEFL ETAEAIGINE EEAQGLLYDI TAGTGEWCAE KMAMFRTWGH
PPLEASPAAA KIRPHMCSSR LLEPLFLFKE ESFFKREIIN GHIKKQAGMW PSCSIPIWCD
ELRTLRSTGR PIPQNPSSKI MDELLCTNID QIEDVSLDEA ISIYMKDKAI SGPASSFDSS
FQFCGMSYRP SRGNYTKRLV AHFLEQADFD PQQYIDHIQS GDYLMDKESY LSYSLKEREI
KETARIFGKM DALTRGSQVV GEHMIAVGLA KYQDANTMVM KEAQFLKRLA KMNNISMVSE
TSEGIYPQSA GFVNLDIVKY CLSQRLESNA LIFSVMDKLL GLEKFFRWHH LYMSGRTACV
TDPFCPPFQT KYIGLDEQPN EGIFIKNPAG AVEGYQQKAW TMISVTDLNI VGQEMGTEIF
AVAQGDNQSI AVTVKNSKDK NVVDCKKSAL EESIRFKYHL QKLLIKKGQR LKMSETFVSP
DLFVYSKRIY KNARTLPQSL KGAINMKLWG DKIVDEVRSG LSNIGSGCYK YIAQGGNIPR
GLTIAKMRSF EQIMNGANLS LNQYGSRDIE MRLRGARGLL SELCSVPIQL GGYDYLPLSK
CVMKNPGDPL TTALAELKIK LKSRLLDPDV AVNFLNQPLE KPTWRRLGLD PYGLNCKSTM
SISSVLQRVT AKNILARSPN PMLKGLFAGN FEEEDEEMAK SLLDQARVYP RSAKAILDDT
PTGERMKLCK MCDTTKTVIM QCSEKGGINM SDYTLIKRFD SEQINYYFQI RLGEGCREVF
EERDLGKCSV VLSRELRKYS WEGLLGGREL EGLDVAPPIE CTKGERVVAG KACSLCQGGN
KDYATFLLPE DTLSSNYDAL KKGVRTPYVG SSTLELTRMS LINTKELSRA VRKGTRMATL
IIWLFGDSEE SWDLACKFAN LRFPCTKSEL KLVTARHAAG NMLHRLHDND TATGFMGMKE
SNVAPFIQMS TDGLASLSDT GSEDTNFIYQ NALHIGIFMI EDSVGKEVTR YGNNEELYHL
HVETGCCVKS QVYTPLRELG KLEIEIPAPL KENKFIYDSG GLTSIVGKFE EIREIQESGI
ELEDMDSDSL SKLMGLTVGK FIMGNIITGS RKREFGGLAD QGTEEDVGGL LSECAMTKVK
WIFDGMAIEC IESLLVESLV SGCKTTSDVI NFLRCRLRSI PFKSYSKLSS VLTSKKVRKQ
EERIQPRRAG PNSRSMWTYP EIQTRILCAV DELLDNPEML DEMPIITDRL EGIKPRRTRS
TTIRCLLSLM ENGNLNTREI RTNVKNDNEL FLRFIQQSIP PRFIKELSPK GIVTGNLTYV
MRQCLIILRD RNFVIGNHKK TIIQTKVTCT AEDQDIRTGN LSGKEITGDL VWKYEDKKKI
GCYLLRQSGV NSTSALKLWN SLSDLPIKNG KVLCLGEGSG SIAALIKSLG ARHIYFNSLM
LGNFGSQRTP EYFPSEYLYI HGEEDITIIN SGRQDSTDLT RDECKDLILS TVNEVSGITC
DAESGDDTES ILRTVRSLIS IVLKEGGWTI IKVMMRNEST KYMINWCNCQ FQDVVLQRSP
YSNPSNSEFY LICKKFTRSG TINRGTVSGQ ELIHEARDVY LRSKEKCVNL ILTTNKKNTT
PGNNELLRNG WANSMTASRD LFGNLMDKHE IPTHSLEREV LTEHGMSGWA KKKMTRIREE
IILRMRDMII IRIMNTSRAK IAEWETIPED IRTVTRNEFL KGITKKVAKR ISIKESTTVE
IDWSFQKLLM KCHPE
//
