ID A0AAD3AVK4_9RHAB Unreviewed; 2124 AA.
AC A0AAD3AVK4;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 10-JUN-2026, entry version 10.
DE RecName: Full=Replicase {ECO:0000256|ARBA:ARBA00031012};
DE EC=2.7.7.48 {ECO:0000256|ARBA:ARBA00012494};
DE EC=2.7.7.88 {ECO:0000256|ARBA:ARBA00012582};
DE AltName: Full=Transcriptase {ECO:0000256|ARBA:ARBA00030436};
GN Name=L {ECO:0000313|EMBL:FAA01392.1};
OS Anole lyssa-like virus 1.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Replylivirus; Replylivirus allogus.
OX NCBI_TaxID=2772344 {ECO:0000313|EMBL:FAA01392.1, ECO:0000313|Proteomes:UP000831573};
RN [1] {ECO:0000313|EMBL:FAA01392.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A.allogus/Cuba/2011 {ECO:0000313|EMBL:FAA01392.1};
RX DOI=10.1007/s11262-020-01803-y;
RA Horie M., Akashi H., Kawata M., Tomonaga K.;
RT "Identification of a reptile lyssavirus in Anolis allogus provided novel
RT insights into lyssavirus evolution.";
RL Virus Genes:0-0(2021).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + phosphate + H(+); 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:ARBA00048548};
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 -!- 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 + S-adenosyl-L-homocysteine + H(+);
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:ARBA00047332};
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 -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}.
CC Virion {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; BR001666; FAA01392.1; -; Viral_cRNA.
DR RefSeq; YP_010798905.1; NC_076534.1.
DR GeneID; 80537177; -.
DR KEGG; vg:80537177; -.
DR Proteomes; UP000831573; Segment.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR InterPro; IPR039530; L_methyltransferase_rhabdo.
DR InterPro; IPR039736; L_poly_C.
DR InterPro; IPR048398; Methyltrans_Mon_C.
DR InterPro; IPR048397; Methyltrans_Mon_CD.
DR InterPro; IPR026890; Mononeg_mRNAcap.
DR InterPro; IPR014023; Mononeg_RNA_pol_cat.
DR InterPro; IPR025786; Mononega_L_MeTrfase.
DR NCBIfam; TIGR04198; paramyx_RNAcap; 1.
DR Pfam; PF21080; Methyltrans_Mon_1st; 1.
DR Pfam; PF14314; Methyltrans_Mon_2nd; 1.
DR Pfam; PF21081; Methyltrans_Mon_3rd; 1.
DR Pfam; PF14318; Mononeg_mRNAcap; 1.
DR Pfam; PF00946; Mononeg_RNA_pol; 1.
DR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 1.
DR PROSITE; PS51590; SAM_MT_MNV_L; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW mRNA capping {ECO:0000256|ARBA:ARBA00023042};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000831573};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484,
KW ECO:0000313|EMBL:FAA01392.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844}.
FT DOMAIN 610..798
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50526"
FT DOMAIN 1673..1870
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51590"
FT REGION 1116..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1133
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2124 AA; 243952 MW; 0EC9861F5B187E1D CRC64;
MDDYEILDDE EDPVYVPDEV GPDSKCANIL RTSDYNLNSP LIEDPADMML TWLMSGERPK
RMNGSPGLDR SYHVLKNLSR KVDWGRTQYG SKGSQTFINR WAEVCSMNNR QAREHLRELA
GFCKKTSHVE KVFTEFLEVR GFHVSLGSIL ESYSKINYDQ EGGRYIGNLY HSYMIFHVIV
LYMNALDWEE EKMIISLWSK ISKYEAKYDR MWISDKIWGL LLITKEFVYH RDLDILVDKN
FILMMKDMFL SRFNSISVLL SPADDRYSKD IIYKMISLYK AGDTILSLKG NKGYEAIKML
EPIVTNLLVK EAESFRPLIH KLGEFPEYME EKSNQLIGLF GKPVKDFFDE LKSFNNIHDL
VFVFGCYRHW GHPYIDYRSG LSKLYDQVHM KKDIDSMYQN ALASDLTKKI LRWGFEKYSR
WFVDISQLPK DHLLKPYMLT QTWPPIHIID QMKETWHKLP VTKIFETPES MDPSETLDDK
SHSFDRRKFE TWLREHPGRP IPSEKVIITA LSKDPVNPLE FLQKVDKDGL DFNDLIIGLK
PKERELKIEG RFFALMSWNL RLYFVITEKL LADKIIPLFD SLTMTDNLNR VFKKLIDRVN
GQGLEDYQRV TYAFHLDYEK WNNHQRMEST KDVFQVLDRF FGFHNVFSRT HEFFQKSWIY
YTDRADLIGV WDNKIFCRDV SEGPVCWNGQ EGGLEGLRQK GWSLVSLLMI EREALVRNTR
TKILAQGDNQ VLCPTYHLSE GLNKTGLEYE LDNIARNASA IYRAIEEGAR KLGLIIKKEE
TMCSFDFMIY GKTPLFRGNI LVPESKRWAR VSCISNDQIV SLSNIMSTVS TNALTVAQHS
QSLVKPMRDY LLMSVQAVYH YLLFSPLLKN RVYSILILRG EKFIICMARI LFLDPSLGGV
SGTSLGRFHV RQFPDPVTEG LAFWKELGDF TKTEWIKKLS NEAGNPRLGQ RTLDSFSKLM
EDPTCLNIEG GSSPMLILRE AIRKALYDDV DKIKNAEFRE AILLSKNHRD NFLVFLRKIK
PLFPRFLSEL FSSSFLGIPE SIIGLIQNSR TVRRQFKKGF SQYLEDLFVR SESEGLSRVT
KDPSKSTQIW RCSAERADRL REISWGSPVV GTTIPHPSEM LRSTPTTSTS CSCKDSGGPN
PRISVSILSS FDNSFRRRGP LKGYLGSATS VSTQLFHSWE KVTNVHVVRK ALALKESINW
FVDRNSNLAE SLLANIKSLT GANFEIEEAP IFKRTGSALH RFKSSRCSEG GYSAVCPNLL
SYISVSTDTM SDLTQDGTNF DFMFQALMLY CQTWSSELAQ RDTQYQDITL HWHIDCRLCL
RVIDEVSLEA PEPFIFPDIS IRISKMTSGA VPQFRPIPEL KLPEGSFSTL PEVDKSFHMG
TAQGLLYSIL VGIHDQGFND PSIFPVNIYK NLAPQHYLLG LARGIMIGAS LCFLSRMTKI
NVNRPLDLFS GVISYIVLRL ENHPSLYMML KNPNLREEVF SIPQKVPAAY PTTMKEGNNA
VINYLQNVIR YQKDKTLGER RGELLWVFSD FRSRKMTYLT VVTFQTFIIL SKMGKSLSKQ
MRNDLTELNS LMRKVLGGCG EDVVPSRHDV CKILRESLAK TRWVDSEVRH ASKFLTTSLP
ETKPKKRTES PKEWICSYQK IMIETSSHPC PLPRLEAEKL SSHVSNPLMS GLRVVQYATG
AHYKIKPILN SMECPPQLCL VIGDGSGGIS RAILSFFPDS LLVFNSLLEI NDMMASGSCP
LPPSAIMRSG RQNTDRVIGL NQIWEMPSDL RLIHTWIYFD NVQKKLKKDY ELIVCDAEVT
DVESSNKISE NLIKMLKNVS GELTVIFKSY GSMLVDPKYS VLENLSSSFP KIEGYTTQVT
SSFSSEIYLV CRRSGIYHKE REHLSAATVR ELRLTCINCR DCRAEMGRAR SLKYSDLIMG
FPPDIISNPY TDLISTLIDS DVESFLVHRM VDDLELLRNR ESKLSNIFAI MVIYSNRVFN
VSKQMSGSHY QPPSDPKIVR HFNICLGTLL FLFTTTNNLT GFSKCHSLYN DKITYNFHKC
NIKGKTFLSW SWTKKSSVKK CISVNTELSM SSHWIRIIYK IVQTTSIKSE LSKILENGMK
TLANYNKWIS RSTLSLRTSL LENI
//
