ID A0A0V0WZF2_9BILA Unreviewed; 835 AA.
AC A0A0V0WZF2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 17.
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 Name=cmtr1 {ECO:0000313|EMBL:KRX81069.1};
GN ORFNames=T06_6462 {ECO:0000313|EMBL:KRX81069.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX81069.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX81069.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX81069.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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)-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:KRX81069.1}.
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DR EMBL; JYDK01000035; KRX81069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WZF2; -.
DR STRING; 92179.A0A0V0WZF2; -.
DR Proteomes; UP000054673; 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; -; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR025816; RrmJ-type_MeTrfase.
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; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51613; SAM_MT_RRMJ; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|RuleBase:RU368012,
KW ECO:0000313|EMBL:KRX81069.1}; 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:UP000054673};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU368012};
KW Transferase {ECO:0000256|RuleBase:RU368012, ECO:0000313|EMBL:KRX81069.1}.
FT DOMAIN 238..459
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51613"
SQ SEQUENCE 835 AA; 95764 MW; 1B634B9F1C935210 CRC64;
MKPTKFIREC EIRLDGCVSI YTCLTAVLNV HKFFINLNVE WRKNVHNMDE LAEICEFENV
SFENVHSDNL AEVCCSAASS GSNLLKRKLS GDQCVQPVLE NTEPYEKRCS SGKMINETMK
EMEFKEGPEF GIQDQGMAVP HSDHHTLPDW EMKKMEIIEE VKWFPPSPSP LALDLKLDEK
CIKIGRRVKD SRQEDSYFKK NILNDLLLAK SELHNIKDWR LRSARSRANP FELIKSAIFQ
NRAAIKLANL DALVDFQLTD PKDADGNSIV PNVAEYPELF YFADVCSGPG GFTEYVLWKR
GWNAHGFGMT LRNDCDFRLD KFTASSPVMF EAFYGEDGID GDGDITKGSN LESFSNFVLK
NTDQKGVHLF MADGGFSVVG EEILQEVLSK RIYLCQSLCG LLVLRKGGTF LCKFFDTFTP
FTVDLICLLW HCFDKLTLHK PHSSRPGNSE KYVIGIGFRG NCKQISDYLI KANLMFDTFK
ADEDIRQLLP SNFVQEANEF MSHFMEINEQ LSARQISFLK KYKTFSENRT LRDNRQQLIR
EYCLNLWKIP DESAKNFTQS AEMIFKLLSP RNASWLLEKR IKVDASWLQR LNIVQHLVVA
SFGEATVLIA GGNNLYYFHE KEWKEFDCVE AYLPNNTVIF GSFTRCYSTA ASSSSCSIES
NNIKLTEKVS LFRIIDAAWL GDVNVENFPY QQRLQLVAKF CKAIDKRYSI PKALHFEAAP
LLTPLDVVHL LQHQVKLMLS ENGHWILAKQ STVFPDYFIP VQTLMFVSKM KFENPFDDSS
KEKNYSNFQN FREMFVDRIA VQFYENDGDS CLNGDILENG RISCLQTFQN AVQKA
//
