ID A0A0J7L5F3_LASNI Unreviewed; 909 AA.
AC A0A0J7L5F3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 2 {ECO:0000256|ARBA:ARBA00021134};
DE EC=2.1.1.296 {ECO:0000256|ARBA:ARBA00012770};
GN ORFNames=RF55_1455 {ECO:0000313|EMBL:KMQ98182.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ98182.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ98182.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ98182.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KMQ98182.1}.
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DR EMBL; LBMM01000509; KMQ98182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7L5F3; -.
DR STRING; 67767.A0A0J7L5F3; -.
DR PaxDb; 67767-A0A0J7L5F3; -.
DR OrthoDB; 5764at2759; -.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProt.
DR Gene3D; 3.40.50.12760; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR025807; Adrift-typ_MeTrfase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR16121:SF2; CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 2; 1.
DR PANTHER; PTHR16121; UNCHARACTERIZED; 1.
DR Pfam; PF01728; FtsJ; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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|PROSITE-ProRule:PRU00946};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00946};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00946}.
FT DOMAIN 116..334
FT /note="Adrift-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51614"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 159
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 178
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
SQ SEQUENCE 909 AA; 103306 MW; 255AB5287ED3E606 CRC64;
MMEEKGNSFA VKQQWNKKVD KSRHAELTYN IETLFEKHFI ISDSQGQAET YTLPESESIF
KEPPWRLDNL QILKDSLNEM KSRLNNFNLC EWQQHTNQMN KAGDIVNVVK KTIQAELVTQ
AWCKFYEIAS NFFLVPLNEI RREENGKNFT SVHLCEAPGA FVAALNHWLK TNAPDVRWNW
LATTLNPYCE ENSYDRMVAD DRFIRHTLKR WCFGADNTGD IMDLRNLDVL VERCKLLDGG
VLLVTADGSV DCTDVPGEQE NAVAQLHLCE TMTCMHLLRK GGNFLLKLFT LFEHQSVCLM
YLLSCAFHQV VVTKPASSKA GNSEMYVVCM NFRGRDYVAP YLNILRQHCG NVSPTKAMFN
PRDIPGSFLR RLEECSEFFK HHQYQVIRDN ISTFHAERYD SILFELKHVK RIVANKYLKE
CRLSRIDSAN EIVGREILEK SNNSFINKKW RADSYNERCK RQDLKPQEHL LQICNKAKEI
ESPAEKSYTS SGDVRVDILE KLPVPFGLVR FGVAPDHPEV KNVINTFHKT ANNPRVQFLG
NVNVGTDVTV DQLRDFYHAV LLTYGAQKDR LLDIPGEHLS NVISGRRFVG WYNGMPADKD
LNINLDVEEV VVLGQGNVAI DITRILLTPI DKLKNTDITS FALERLSHSR VRKVSMVGRR
GPLQAAFTIA ELRELLKLEN CKKLWRAQDF AGVRDIVPTL ARPRKRLTEL MLKSLEESVS
DSTYAKELNP IFLRSPVEFY GGDELRSVRF AVSRLRGDTI QNQIAEATDE FETIPCDLAL
RSIGYKSAQI DSSIPFDARK GRVVNVSGKV DSNLYSAGWA ATGPVGVILS TMTNAFQVGN
LVCKELASSS ENKAGSNGVR DILNSKGIQI VSYGDWQKID RIEQERGKQL GKTREKIVDV
TEMLDIAAK
//
