UniProtKB - Q77SJ8 (L_HIRRV)
RNA-directed RNA polymerase L
L
Functioni
RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concommitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene.
By similarityRNA-directed RNA polymerase that catalyzes the replication of viral genomic RNA. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing transcriptional signals, and the replicated genome is not caped or polyadenylated.
By similarityCatalytic activityi
- EC:2.7.7.48PROSITE-ProRule annotation
- a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + 2 S-adenosyl-L-methionine = a 5'-end (N7-methyl 5'-triphosphoguanosine)-(2'-O-methyladenylyl)-adenylyl-cytidylyl-adenosine in mRNA + H+ + 2 S-adenosyl-L-homocysteineBy similarityEC:2.1.1.375By similarity
- a 5'-end triphospho-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + GDP + H+ = a 5'-end (5'-triphosphoguanosine)-adenylyl-adenylyl-cytidylyl-adenosine in mRNA + diphosphateBy similarityEC:2.7.7.88By similarity
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- GTPase activity Source: RHEA
- mRNA (guanine-N7-)-methyltransferase activity Source: InterPro
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase, Methyltransferase, Multifunctional enzyme, Nucleotidyltransferase, RNA-directed RNA polymerase, Transferase |
Biological process | mRNA capping, mRNA processing, Viral RNA replication |
Ligand | ATP-binding, Nucleotide-binding, S-adenosyl-L-methionine |
Names & Taxonomyi
Protein namesi | Recommended name: RNA-directed RNA polymerase LShort name: Protein L Alternative name(s): Large structural protein Replicase Transcriptase Including the following 4 domains: RNA-directed RNA polymerase (EC:2.7.7.48By similarity) Alternative name(s): PRNTaseCurated Alternative name(s): mRNA (guanine-N(7)-)-methyltransferaseBy similarity Short name: G-N7-MTaseBy similarity mRNA (nucleoside-2'-O-)-methyltransferaseBy similarity Short name: N1-2'-O-MTaseBy similarity |
Gene namesi | Name:L |
Organismi | Hirame rhabdovirus (strain Korea/CA 9703/1997) (HIRRV) |
Taxonomic identifieri | 453457 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Negarnaviricota › Haploviricotina › Monjiviricetes › Mononegavirales › Rhabdoviridae › Gammarhabdovirinae › Novirhabdovirus › |
Virus hosti | Acanthopagrus schlegelii (Black porgy) [TaxID: 72011] Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus) [TaxID: 8255] Plecoglossus altivelis (Ayu) [TaxID: 61084] Sebastes inermis (Dark-banded rockfish) [TaxID: 160818] |
Proteomesi |
|
Subcellular locationi
- Virion By similarity
- Host cytoplasm By similarity Note: L and P are packaged asymmetrically towards the blunt end of the virus.By similarity
Keywords - Cellular componenti
Host cytoplasm, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000297836 | 1 – 1986 | RNA-directed RNA polymerase LAdd BLAST | 1986 |
Interactioni
Subunit structurei
May form homodimer.
Interacts with the P protein.
By similarityFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 560 – 757 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 198 | |
Domaini | 1592 – 1788 | Mononegavirus-type SAM-dependent 2'-O-MTasePROSITE-ProRule annotationAdd BLAST | 197 |
Sequence similaritiesi
Family and domain databases
InterProi | View protein in InterPro IPR026890, Mononeg_mRNAcap IPR014023, Mononeg_RNA_pol_cat IPR025786, Mononega_L_MeTrfase |
Pfami | View protein in Pfam PF14318, Mononeg_mRNAcap, 1 hit PF00946, Mononeg_RNA_pol, 1 hit |
PROSITEi | View protein in PROSITE PS50526, RDRP_SSRNA_NEG_NONSEG, 1 hit PS51590, SAM_MT_MNV_L, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MDFFDLDIEI KQERLPAECS LNSPLNISLS SQLTDRMTPQ NENIRRQRER
60 70 80 90 100
IRTHTKTHSR IKHLSKLDND STRLHARLTE DLIKLQHLEV DSPVFDNWAL
110 120 130 140 150
LTSYYAALDY TLPERASFDW GQAAPYWNLY TQLRTILLQS QKIRKKDRGV
160 170 180 190 200
REIYSCGPLR LEFVEGTVLY FTDKQSGGEF TKSGELPSIT PYADFLAWVK
210 220 230 240 250
IISQRAQAVL MAVILRVTDK GLSPLPESLL SVYQTVDDIL KRAGQPAIDL
260 270 280 290 300
LKLWEPLVIT KLGELLGDRF GLEEDFRLTI RGEATRLAKK LAITNGLNRL
310 320 330 340 350
MTVLDSQTEA QPLFQFFGLF KHFAYPRVFS RDTIQAIQEV SDRPSSISAA
360 370 380 390 400
EFLHDQCEIR KEFYIRYLKA YHRAPGLDLS ALSPSSFLRE SLEHGKIPNE
410 420 430 440 450
KSPHYSNKEW YFIKFTKSIE WPISDTLSTF LSDKAITRDR AAWIEEGHSG
460 470 480 490 500
RDMSEKRLLL KFIKENFSSV AEIVAAADAI YNNEGDRLIA LKVKEMELKI
510 520 530 540 550
KGRGFGLMTF MPRLLQVLRE SIAKKTSKLF PEITMTSSDL DMKKRKFMLS
560 570 580 590 600
KRSDDRRGFI HINKSLDINK FCTSQRQFNS SAVFSSLDEM MGTFPLFSRV
610 620 630 640 650
HEIFEKTWIV DGSASDPPDL SHFTRILEEC RLHGIEAPHV WADGVFSGLK
660 670 680 690 700
GGIEGLCQYV WTICLLLRVE RVMQKTKLTH YILAQGDNVI ITIIVPVEIH
710 720 730 740 750
RDGIISDQES RRLLTLSRNI DLSLESELEK SGLTLKIEET LTSENISIYG
760 770 780 790 800
KDLHCPQHLT LALKKAASAA IISSEQYQDI PTFLSGLGTS LESLSECVNS
810 820 830 840 850
KTGAHLFGVL MGVAGWKDLA THQTWRGWRY PYHKAPLSGR VRASDMKIGK
860 870 880 890 900
GEAVELTIPV MSPRQQGKET LRELLANSLL GSALGMLAFP TPIDLEKRGV
910 920 930 940 950
GDYITHRLAI ARKALLSEKL DPHIEKRVRS ACNLPLSSRV DLSKLFDSPF
960 970 980 990 1000
SLNLATEEDA TAVIKRQAKK TLRLQEIGND KLRAQIGNMD KGIAALDADL
1010 1020 1030 1040 1050
AGAETINPRL NHMIRDITDE KESEMFVTKF ASARTMRTLA MGDSSEVPIV
1060 1070 1080 1090 1100
VLLEKKSQQK ELYTIWRARR PHATMWKCST VLAKGLRDIS WGKTIVGVTS
1110 1120 1130 1140 1150
PSPIEAMETT HIDPTDWEDS RSRETLSINY YLSRAGIDEQ TAKLTRGSLV
1160 1170 1180 1190 1200
PYYGTQTKPL IAKAYLELKG NPRTNKALLL LSVRESLVKT GSNLDELIMQ
1210 1220 1230 1240 1250
LCSHALDIDA ASLPALRAQE EATAGEGLRG GIKESMSPVG PDNFYTNITH
1260 1270 1280 1290 1300
KVFNRKWVTP YHVNIADFII QGLIETRKHL ILNEKMDGLL PLSSVKCTAC
1310 1320 1330 1340 1350
FRKKEREFFD IPEGPTWKND STTSDPAYTY FTTWCDLPRV STLPTMDQQS
1360 1370 1380 1390 1400
ATRLLGRGLS LNRPTAGEII TKFYSMSMES QRLLHPVDLL LGYGEGVVFG
1410 1420 1430 1440 1450
YIRSQHIHHG ALFQTKRETL TNKLRKFILD TKTQHAKQIG YLFQDEDSLH
1460 1470 1480 1490 1500
ELMAQGLCPY VPRSIPLTIT ELTNACAITT IRATEVILSA GSRVALMPVQ
1510 1520 1530 1540 1550
AIDETDVDNS RLAANTMQTI LGDSRPMNPV YLDCDLTTNM TAWESSIELD
1560 1570 1580 1590 1600
VLKSENFHID GLLMDLTARE LPISDTPWKQ RDWTCSNDPR IIAKGIKTKS
1610 1620 1630 1640 1650
LFIHQGVAEA LNMTPDLLVV IGGGLGGCAV PYLQEWADVP LIFATLFDER
1660 1670 1680 1690 1700
ERISEDGDLV VPPEILVRGM APRMIERELL EAELCDVTND GNRRLLTRLV
1710 1720 1730 1740 1750
KKNRGKGTVV LIDEIENRGA PESLLQSSLQ DLVRRLDKVC TLTSIHTVRE
1760 1770 1780 1790 1800
STVEQFAQRT NSIKRDRKTV TLHWNRYNRR DQFEALVIVK GEETRSDYHV
1810 1820 1830 1840 1850
STATAAQAFR KIDEQLEVEG RLSATRWSLP TLPAREKEIL FGYVSSVFLK
1860 1870 1880 1890 1900
TNLVLSADDM DRETLLETIE DTAPGLISWK EKLEHRDHAF RSDIDEKGIT
1910 1920 1930 1940 1950
QDKVFNLICL AWVITGLRYG IWETDAQSII TKTVYITRGP KLCPLGEKPK
1960 1970 1980
RVFASFKLQS DKRVEDAKGF LSALLHLEGF FPLGRQ
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF104985 Genomic RNA Translation: AAQ73462.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF104985 Genomic RNA Translation: AAQ73462.1 |
3D structure databases
SMRi | Q77SJ8 |
ModBasei | Search... |
Family and domain databases
InterProi | View protein in InterPro IPR026890, Mononeg_mRNAcap IPR014023, Mononeg_RNA_pol_cat IPR025786, Mononega_L_MeTrfase |
Pfami | View protein in Pfam PF14318, Mononeg_mRNAcap, 1 hit PF00946, Mononeg_RNA_pol, 1 hit |
PROSITEi | View protein in PROSITE PS50526, RDRP_SSRNA_NEG_NONSEG, 1 hit PS51590, SAM_MT_MNV_L, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | L_HIRRV | |
Accessioni | Q77SJ8Primary (citable) accession number: Q77SJ8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 21, 2007 |
Last sequence update: | July 5, 2004 | |
Last modified: | May 25, 2022 | |
This is version 84 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families