ID W8QQQ8_9RHAB Unreviewed; 2131 AA.
AC W8QQQ8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 10-JUN-2026, entry version 75.
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};
OS Long Island tick rhabdovirus.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Sawgrhavirus; Sawgrhavirus longisland.
OX NCBI_TaxID=1459044 {ECO:0000313|EMBL:AHL66985.1, ECO:0000313|Proteomes:UP000148852};
RN [1] {ECO:0000313|EMBL:AHL66985.1, ECO:0000313|Proteomes:UP000148852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS1 {ECO:0000313|EMBL:AHL66985.1};
RX PubMed=24517260; DOI=10.1186/1743-422X-11-26;
RA Tokarz R., Sameroff S., Leon M.S., Jain K., Lipkin W.I.;
RT "Genome characterization of Long Island tick rhabdovirus, a new virus
RT identified in Amblyomma americanum ticks.";
RL Virol. J. 11:26-26(2014).
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; KJ396935; AHL66985.1; -; Viral_cRNA.
DR RefSeq; YP_009094017.1; NC_025340.1.
DR GeneID; 20964298; -.
DR KEGG; vg:20964298; -.
DR Proteomes; UP000148852; 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; 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; 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:UP000148852};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
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..797
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50526"
FT DOMAIN 1663..1860
FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51590"
SQ SEQUENCE 2131 AA; 242037 MW; 111B8FF91CF00D82 CRC64;
MDLQFPVCPD GEAHQEYDLV PDEDTPRPVR QRTVVGTDYN LNSPLLDWRV QSLITALVVG
QHASGNSSFA NELRALRSLM SEENVSPRKL LPSGDHHRRL PELIYSSRRW VKINLGPRIT
ELWEGSREVL LAMERSVLGQ VIHDPNRLVL DILCHQAQVD KKTRQEIKTF LNLHYLICMM
NARKPKFASQ LARHIFRECN LDLSGPTFKY AIKDKNGQTQ VVGTRHHVVF LQSGVLVDKN
FVLMLKDISL ARLMAMCSVV GRDPEKPGNY CANKLRLLYN EGDKLLANHG NLAYKAIKLL
ESECVNQWSR LGHEHRPLIP ESTGLADHLD STAEELRASY GIEVIPFCSV VRRERDPWVV
AQMYGAYRHW GHPYIDSLKG LKKLRERVFK ELEIDEEFAE QLGSEMAFLV LQDRFQKERR
WYCTADGLPP DSPLRRCIEE GVWPTSKVIN DFGDNWHKLN LLPCFEVPEE IDPADLFSDK
AHSLPRSKIL DHVATKPRIP IPGVRVIETL ITTDVPPVKT FLQNVNDHGL SPEDLVIGLK
PKERELKDEG RFFSLMGWNL RLYFVITEYL IKKLFVPLFK GLTMADDLNT VTKKMIAATE
GQGLCDYSRV YIANSLDYEK WNNNQRYESN QHVFRVMGKF LGLPEIFSLT HKFFQSSLVY
YCDRPDLMRV TENSLENVNE ETPVCWEGQA GGFEGLRQKG WSIVNYLILR REIMMRNTGT
LILAQGDNQI IIPKYKIVNK VNDEGLVTEL KNVWDNNSNL MDRIRRSTHA LGLTINKDEV
VTSAELLVYG KVPIYRGVVL PLETKRWARV SSVTNDQLPS LATAVSSTVT SALAVCLHSD
DPVQTMWHYG LIGCFVVALN TTFNPLIGVD PFKWESLPTR TKKEVGIRTL YKDPSVGGVC
GSNLFRFLLG RFPDPVCESL SWWRLIYYNT TDDCVQDIAL ECGHPQLGKV GPETWSRLLE
DPTSLNIPST LSSDTLIKEQ VYEGLCQKAN DGTIKNRRLR ESVLYNDAHK ATFVHWLFTI
TPTFPRFLSE FYTATYFRLT EGIISTFQNS RTIRSVFSTT FTEKVEKVIK KSEKSSIRLL
ITPKTSATHP KIWDCSASHA DNLRCSSWGR KVEGSTIPHP GEMLVEKACD GCTGPHVVAK
KTGMDFYGTW VRGPLMPYLG SKTSENTSVL QPWEKNIEIP LLRQACQLRR TIDWLMEPDD
KLATSIYNNI KSMTGLDLKD ETYQALRTGC GRHRLRSARV SNEGTPSCGY PPLMYVAVTT
DSLGDLNKDN HDFMYQSVIC WAGVLATLKG NKYLMRDTTH FHIKDPKCLR VISEEKLTVP
TEYKFPDVSE SVKRMLSVEL VVKTSTRHTD PLPVVWSDVP DTDKSWHLGR AQGFLWALSV
FDGSTDELKD VLFPISITSR VCVWDYMHGL HRGLMLGSVF PPLFARYGSL DTKAALRFQG
AYWNSINEAL EKSKLPELLW NKRFAQFSAH YGASVIKSYP ARRDELVSTL RQWLISRIQE
DFRDETVGVP HSVVVFAEMD SDYVINMFRV AEKTLGVFLK VRLGTKDLHD ISYARVLVQM
LMAQKHEKIT DSDNRKLQQE VRGKNLPSIS LVGSEARRAA ADIEIAVSGP EHTPLVLPLR
ECGISTDVVP VEYIPRDNDW AGYSFAETLP TERIRNPMAA GARLVQLSTG AHYKFRDLLC
HITLSGDGIF CGDGSGGMGA CYLRMFPHRR VIFNSLLSLE GDSLKGMAPP GPGAYSASGQ
DVVARCINYD TCYQEPSDLR DQTTWENIIT QVKRSKLRIG VVCCDADAWS PTSVRQIESG
FLYGCERLLR PGRGTAIFKT FWYHILNPES IIHRMGALFE HVWVCCPFTQ GSNTSEAYLV
GQKLKKTETT HKCLVTEQTL LRVYKTLKAS RTYEQEFRRA TMMSFELMTA GMESRAPFSD
SITIMEFFIS LGVKSGLALE MSNQVLDLAW DLVHPEAMLR LLSFLLTRDT VDIETRVEGH
LLIPSSTQLQ RSVAVIYGLW FGTSLVTRDE KWYSVPVRLY QNPTRVYFEG HQRGNFTYMR
WGFGHGKFTK VVDQGERVGV TQSLIRLMQA LYRGRWSGRD PSASDTKRVN AVMANYSRLM
TCKKVDAATP ITLRLARPDP LVNHILELPE E
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