ID H2XRH2_CIOIN Unreviewed; 790 AA.
AC H2XRH2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 {ECO:0000256|ARBA:ARBA00021136, ECO:0000256|RuleBase:RU368012};
DE EC=2.1.1.57 {ECO:0000256|ARBA:ARBA00011923, ECO:0000256|RuleBase:RU368012};
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1 {ECO:0000256|RuleBase:RU368012};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000032256.1, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000032256.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure of
CC mRNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-
CC capped mRNA and small nuclear RNA (snRNA) to produce m(7)GpppRm (cap1).
CC Displays a preference for cap0 transcripts. Cap1 modification is linked
CC to higher levels of translation. May be involved in the interferon
CC response pathway. {ECO:0000256|ARBA:ARBA00002664}.
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|ARBA:ARBA00024256,
CC ECO:0000256|RuleBase:RU368012};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368012}.
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DR EMBL; EAAA01002798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2XRH2; -.
DR STRING; 7719.ENSCINP00000032256; -.
DR Ensembl; ENSCINT00000031688.1; ENSCINP00000032256.1; ENSCING00000024328.1.
DR GeneTree; ENSGT00940000157172; -.
DR HOGENOM; CLU_011097_0_0_1; -.
DR InParanoid; H2XRH2; -.
DR OMA; IDSMCDF; -.
DR TreeFam; TF314897; -.
DR Proteomes; UP000008144; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IBA:GO_Central.
DR GO; GO:0097309; P:cap1 mRNA methylation; IBA:GO_Central.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.40.50.12760; -; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR025816; RrmJ-type_MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001202; WW_dom.
DR PANTHER; PTHR16121:SF0; CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 1; 1.
DR PANTHER; PTHR16121; UNCHARACTERIZED; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS51613; SAM_MT_RRMJ; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU368012};
KW mRNA capping {ECO:0000256|ARBA:ARBA00023042,
KW ECO:0000256|RuleBase:RU368012};
KW mRNA processing {ECO:0000256|RuleBase:RU368012};
KW Nucleus {ECO:0000256|RuleBase:RU368012};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU368012};
KW Transferase {ECO:0000256|RuleBase:RU368012}.
FT DOMAIN 47..93
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT DOMAIN 191..402
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51613"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 89490 MW; C4209648B1F58260 CRC64;
NNPSTSTSSS SSSGEDSPST EDSPGCSGLG KAVKRKMDEV VQPLDMYSSV ANKMMRKMGY
QPGTGLGREK QGRVDIVPAS EQRGRRGLGL KIKALNKDVV IDWEDEKPPS AEEVVDWFPP
YDGGMPEKGE MEAWADVGKK KLVIDDETLF CDNGVLKTVL ECKSIFDDLE GQEMRKARMR
SNPYETIRGG IFLNRAAMKM ANMDSILDFM FTQPKCLGNN EILYFADVCA GPGGFSEYIL
WKKKWRAKGF GFTLKGPNDF KLGDFFAANS EFFEPHYGVN GIDGNGDIMN TSNLEEFQDF
VLTNTNEKGV HFVMADGGFS VEGQENIQEI LTKQLLMCQI VCALSILRVG GNFVLKTFDL
FTPFSNGLIY LLRIAFENVA IYKPVTSRPA NSERYAVCQG YRDEDRQLFN YLIEINDQMN
EFKKSSVNQD VKAVVPLEIL TGDQEFFNYM KTSNESIAKE QCKGLAKIHA FTKDRSLRET
KQAQVRLECL KKWQVPDRVR SAPQKTDVSS LFYKLTGLKE PHANSESKML TSDNLLSSIR
GVFNYKCYVS SVNSSILVSM GGSYIFLWNK NNRRWLNLTQ LKCLIPRDTI LEVEIAQELK
GESKGQHRVT TIHIVDALFL AGDDMRALNY AERMQSAAIF AEAIRKPSCK HLNLVRTKEI
FRLEDAGKIF TQLKLKTVKG GGSIPRPCYE ITNSDLCFVP RGIVFVRTSQ DPWSMEYSRS
QNRKYFFNMR TNESVFECPP DFNAPYDICS TSRLIWEWRD GVKVHPDQQH HRVNNISTDQ
LLNFVRSKLP
//
