ID A0A1I8NLW0_STOCA Unreviewed; 780 AA.
AC A0A1I8NLW0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 28-JUN-2023, entry version 23.
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=106093069 {ECO:0000313|EnsemblMetazoa:SCAU000160-PA};
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU000160-PA, ECO:0000313|Proteomes:UP000095300};
RN [1] {ECO:0000313|EnsemblMetazoa:SCAU000160-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU000160-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 -!- 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}.
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DR RefSeq; XP_013115503.1; XM_013260049.1.
DR AlphaFoldDB; A0A1I8NLW0; -.
DR STRING; 35570.A0A1I8NLW0; -.
DR EnsemblMetazoa; SCAU000160-RA; SCAU000160-PA; SCAU000160.
DR GeneID; 106093069; -.
DR KEGG; scac:106093069; -.
DR VEuPathDB; VectorBase:SCAU000160; -.
DR OrthoDB; 205623at2759; -.
DR Proteomes; UP000095300; 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 Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 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 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 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|RuleBase:RU368012};
KW mRNA capping {ECO:0000256|RuleBase:RU368012};
KW mRNA processing {ECO:0000256|RuleBase:RU368012};
KW Nucleus {ECO:0000256|RuleBase:RU368012};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU368012};
KW Transferase {ECO:0000256|RuleBase:RU368012}.
FT DOMAIN 26..72
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT DOMAIN 169..382
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51613"
SQ SEQUENCE 780 AA; 90523 MW; E4F17BA1C5DD4A13 CRC64;
MEEENSETEL YESAPKKMKT EWSRSYSKKA MQMMRKMGYE ADKGLGKQNQ GRLEPVVAFQ
QDGRKGLGLK QGTFQIGDQW DITTEEIFIP ESVSWISNQE CFTYDLKDMK DFIKLGRRKT
TLNDETLFVD SNILEGILSA KTVFDNLNEN DLRRARSRSN PFETLRSSIF QNRAAVKMAN
IDSMLDFMFT NPKDKYGNSI VHGNELLYFA DICAGPGGFS EYILYRKAWE AKGFGFTLKG
PNDFKLDKFF AGSPESFDPY YGVNNDGDIY VEANQDTLNE YVRKHTAAGV HFVMADGGFS
VEGEENIQEI LSKQLYLCQC LTALKLLRTN GSFVVKLFDI FTTFSVGLVY LMYKCFDQIA
IIKPNSSRPA NSERYLVCKW KKEDTHDICT YLNLINNILN EENEEDVLDI VDLELILQDK
PFFDYIKESN DSIGQNQIIG LKKITAFCNN PQLKEIRQSE CRRKCLDLWN LPDKLRQAPE
NKSIEQFLEE FLSTWFEHKD FFNSAASDLL SSEDLNKKIE SVYDWYFVPV GRRETNANAC
SFFICTTRGK LFRYTDMRKW EPVDYMFEIS PKSLFYGELV FEYSGEGRTQ TRVCGLHIID
AIILGGRDIR RSPLVERLHM CAKFANSVNK PFKEGNTLTI RSKQLYRLED VKNFFSEMRP
YILKDNSSRL GISLNNSEGK FFVPGGILLL CEICHNFVSL MSKSQNMLYY YDKGKKLSFF
KDRMPVDIQN IYASFRNSFA RRLIWRWTNT CQVEENSNRV DPNVLYRDDL TSFIIYKLNM
//
