ID L1LB52_THEEQ Unreviewed; 979 AA.
AC L1LB52;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 03-MAY-2023, entry version 31.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 {ECO:0000256|RuleBase:RU368012};
DE EC=2.1.1.57 {ECO:0000256|RuleBase:RU368012};
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1 {ECO:0000256|RuleBase:RU368012};
GN ORFNames=BEWA_049660 {ECO:0000313|EMBL:EKX72499.1};
OS Theileria equi strain WA.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=1537102 {ECO:0000313|EMBL:EKX72499.1, ECO:0000313|Proteomes:UP000031512};
RN [1] {ECO:0000313|EMBL:EKX72499.1, ECO:0000313|Proteomes:UP000031512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA {ECO:0000313|EMBL:EKX72499.1,
RC ECO:0000313|Proteomes:UP000031512};
RX PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT "Comparative genomic analysis and phylogenetic position of Theileria
RT equi.";
RL BMC Genomics 13:603-603(2012).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of
CC RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-
CC capped mRNA to produce m(7)GpppNmp (cap1).
CC {ECO:0000256|RuleBase:RU368012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC ribonucleoside)-(ribonucleotide) in mRNA + S-adenosyl-L-methionine =
CC a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-
CC ribonucleoside)-(2'-O-methyl-ribonucleotide) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67024, Rhea:RHEA-COMP:17169,
CC Rhea:RHEA-COMP:17170, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:167612, ChEBI:CHEBI:167614;
CC EC=2.1.1.296; Evidence={ECO:0000256|ARBA:ARBA00024560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC EC=2.1.1.57; Evidence={ECO:0000256|RuleBase:RU368012};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368012}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKX72499.1}.
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DR EMBL; ACOU01000007; EKX72499.1; -; Genomic_DNA.
DR AlphaFoldDB; L1LB52; -.
DR STRING; 1537102.L1LB52; -.
DR EnsemblProtists; EKX72499; EKX72499; BEWA_049660.
DR VEuPathDB; PiroplasmaDB:BEWA_049660; -.
DR eggNOG; KOG3674; Eukaryota.
DR OrthoDB; 5488054at2759; -.
DR Proteomes; UP000031512; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-UniRule.
DR GO; GO:0097309; P:cap1 mRNA methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.12760; -; 2.
DR InterPro; IPR025807; Adrift-typ_MeTrfase.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR16121:SF0; CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 1; 1.
DR PANTHER; PTHR16121; UNCHARACTERIZED; 1.
DR Pfam; PF01728; FtsJ; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51614; SAM_MT_ADRIFT; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|RuleBase:RU368012};
KW mRNA capping {ECO:0000256|RuleBase:RU368012};
KW mRNA processing {ECO:0000256|RuleBase:RU368012};
KW Nucleus {ECO:0000256|RuleBase:RU368012};
KW Reference proteome {ECO:0000313|Proteomes:UP000031512};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU368012};
KW Transferase {ECO:0000256|RuleBase:RU368012}.
FT DOMAIN 118..344
FT /note="Adrift-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51614"
FT REGION 934..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 111707 MW; 093B7043EF6BAEA2 CRC64;
MTSLTHNRRF VFQGNLNRLL SDAKRFPPSS NPCQKCAQRK RACICSQITK GVGRTQVYEI
EELSETKSIL NELRDSLDDV DMEKWSVHTK LLDVTSLTGK HISEITVNVN GRNEAGVEFV
TNAWIKMYEI LEFYKILDLI APNLKTSGGK ISSFHISECP GAFIAALNHN IKVKNERAEL
HWLATSLNPY YEGNNHNEVL AEDILFRETY PNWIVGFDGS GNITKSGNIE YIWDHISRPS
RHNKGKTPTL VDIVTADGSF NCQHDPNNQE NLTASLKFSE TICALGLLRV GGCFILKMFT
MFEESSLSIM ALLSLCFKRL EVYKPTFSKC SSSEVYVVCM EFNGITSILL STLCKFVDLY
ARQSDSRSQK EKTAIIPKEW ITSAFRAEFV ECSKMFTQAQ CRFLRTSMQQ YGANLDENPL
YKQKREFAKE FIKKYEIQGI KPESRLVKYM AYTNQVLTGK DTSSLFHVQK RAILDLKNRK
EYKSDYDELQ KERKRPRDAL YITANETEAN THTESVNKII DFAKRYKIEL SKSDKKDIRI
SFLPSIVEDL LSDLRSQKYL RENWFSVGRI SPSDFKMSFF VSNDILYDVT ALRTYLNSAL
PLCTESDALL VGSSSGEALS DISLPPSAVA VELAMVIKKY SDIGKYKYYL EISGSQQFPA
ICIFKRHNVH GSLIHVQSKH TDSATTSIEY SGTYELQIIL GGFVGDGTID LCFEYNYDEM
LKQSQPYKSL ITELGDSPLK RSCDFIFCDV ENFGSHHREV VHGEISTKHV LVAQLVQAMT
CIADGGDLII RMSTVYTRFT VGIIVVLSSV FQSVHLYQPE AVSPWTQKVY IVCQGYKEDT
VCRHFTQCLW DALCLHKKSN VDVLQTLRPL YFTQIARELW NFNTTLLYNH FEDLVLHTKP
PNVSNVQTIC KRFLQDHNLL EIFYPQPLLD ASNMQMPSVS KEEEEIKTLK RPLEEPDSPA
LTLSPVDENH SPIWSSDEE
//
