ID   A0A2H4UVI3_9VIRU        Unreviewed;      1217 AA.
AC   A0A2H4UVI3;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=mRNA capping enzyme {ECO:0000313|EMBL:ATZ80933.1};
GN   ORFNames=BMW23_0888 {ECO:0000313|EMBL:ATZ80933.1};
OS   Bodo saltans virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Klosneuvirinae; Theiavirus;
OC   Theiavirus salishense.
OX   NCBI_TaxID=2024608 {ECO:0000313|EMBL:ATZ80933.1};
RN   [1] {ECO:0000313|EMBL:ATZ80933.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG1 {ECO:0000313|EMBL:ATZ80933.1};
RA   Deeg C.M., Chow C.-E.T., Suttle C.A.;
RT   "The kinetoplastid-1 infecting Bodo saltans virus (BsV), a window 2 into
RT   the most abundant giant viruses in the sea.";
RL   J. Anim. Genet. 0:0-0(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC         end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC         Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC         Evidence={ECO:0000256|ARBA:ARBA00024268};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus mRNA
CC       guanylyltransferase family. {ECO:0000256|ARBA:ARBA00008556}.
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DR   EMBL; MF782455; ATZ80933.1; -; Genomic_DNA.
DR   Proteomes; UP000240325; Genome.
DR   GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 3.20.100.10; mRNA triphosphatase Cet1-like; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR   InterPro; IPR037009; mRNA_triPase_Cet1_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR039753; RG7MT1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12189:SF2; MRNA CAP GUANINE-N7 METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR12189; MRNA GUANINE-7- METHYLTRANSFERASE; 1.
DR   Pfam; PF03291; mRNA_G-N7_MeTrfase; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51562; RNA_CAP0_MT; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240325};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          687..1055
FT                   /note="MRNA cap 0 methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51562"
FT   COILED          200..227
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1217 AA;  143292 MW;  197D67F9D537C77A CRC64;
     MQKSNIQSKI GNDNVKQIED LFKKINKDSE FEFIFFSKKD KHLTFEKYRT LVKFISKRAS
     SDSKIKLVKN EQTLDISFSP EIEKVYRCTL IGKDAINTYM KKLSIANNHV IFRNLIKLSK
     KDDKIEILKK EKKSDQTIDI DDLYMRARLS SETKISDEEY KKLIAIDETQ MDNIIFRYKE
     RTSLYVYQND KDYIRIDLTI TKMDKKYNKL NNAISNYELE LETMCEKPKN EILEKMYNEI
     EVIFKVVQQS NFIITKSEAN SVIENYKNLL AVPKQNERSL YGRQPISLEI QYVESLANKY
     AVTDKADGER HFLVIFNNHV YLMNKNLDVK NTGIILKKEQ ERYNNSVIDG ELIFLKNRHV
     FLTFDCLFNG GNDIRKEAKL EERLKNADII INDCFVFNGQ KGCKYLETEH HKEFNLNKTV
     EFHRKQIKMT LDNLNHDIEI EKQFLLVRRK YFIHSIGAKP WEIARYTALI WESYTGDPEI
     KCPYTLDGLI FQPNEQKYAV NKKDSRYDDY KWKPREKNSI DFYVEFLKDD DGNILTVYDN
     SYSKISDDPN AVDNAQERNA NQTYRICRLH VGQIVGQLQA PVLFRENDNL YEAYIPLQNG
     EIRDIEGNIL ADKTVVEFYY NSMSNLPNKF KWIPMRTRYD KTEMVMKYKQ NYGNFVSVAD
     KVWQSIVNPV LMTDFEDLAK GNNPDKNQYF YDKKLDELRK RIGHDMIVSA AKEDKYFQLI
     TKLGIPMRNF HNFIKSNIIF TFCHSMYQDN KQKSVLDLGC GRGGDQNRFY YAKVAFYVGV
     DYDRDALFNP LDSSTSRYNQ QKRKPGFTKM FFIHGDQSNE LDYESQFASL GGMDFQNKQL
     IERFFSKDPA KRTTFDVINC QFAIHYSFKN DDSLSNFKKN INNYLRNDGY VLITTFDGNA
     IRKLLKNKER FTQEYVNEEG EVKILFDIVK KYDDVNDDVI MGTGNAIDVH MAWLFNEGVY
     QTEYLVDEKF IIEEFKRDCN LELVTMDSFE NQFNILKEYL TEYVQYEADD RTREGILKRA
     GEFYKSNSVN DGCKKYTDLE KYYVFRKNIP KAKKQKGGNN DLTNTHKYSI SPLPGYDNNY
     SFINSIHHIL KNHEIIPKTL SPKTFCSDMG IDYENDINID SNFKKIAKNI VIYHANNDGK
     HEKILNGLNI LLAERNKDDE YTFKIIEKGK KITQNDNVIM LAKEGVMYAP IYQIDSDLRN
     GIFHMDDENI KQLLELQ
//