ID A0A1D1VE83_RAMVA Unreviewed; 460 AA.
AC A0A1D1VE83;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=RvY_09537-1 {ECO:0000313|EMBL:GAU98382.1};
GN Synonyms=RvY_09537.1 {ECO:0000313|EMBL:GAU98382.1};
GN ORFNames=RvY_09537 {ECO:0000313|EMBL:GAU98382.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAU98382.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAU98382.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAU98382.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
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:GAU98382.1}.
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DR EMBL; BDGG01000004; GAU98382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D1VE83; -.
DR STRING; 947166.A0A1D1VE83; -.
DR Proteomes; UP000186922; 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 InterPro; IPR025807; Adrift-typ_MeTrfase.
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 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:UP000186922};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00946};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00946}.
FT DOMAIN 160..372
FT /note="Adrift-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000259|PROSITE:PS51614"
FT REGION 13..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..45
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
FT BINDING 285
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00946"
SQ SEQUENCE 460 AA; 51332 MW; 12FD9B24A8F3062A CRC64;
MDIMEQELIS EKIADSAANA PGRRRKKAHQ RGRHGSPRKR HGTPDRIRHP LCPQFWSGES
KSKLVTAALN KQIEDLDGRL YTLSDASHSF VSDISSANID VSSGCREPYA SSEMELVETE
LNAVKARVGG MPPEDWYRLT NYTDLASALR YSTKNDPNVE LGTNAWLKFW SILHDFSQLA
DVPHGGSTSV HLCEAPGAFV SALNHFLAVR KPTVHQEWSW LGSSLNPYAS DSKEAIADDR
LIKHTLKNWH FGADNIGDLR LPENQLSLVK AARSHGKKVL LVTADGGIDC SDNPADQELS
LSELKLAEVR TTLSLLDLGG NFVIKMFTFF RKKTCQLVQV LRICFSKVVF YKPSTSKPGN
SEIYVICLGF KGLPAGTTFE FLIKKELEPA LASELTSLAH KCADHQSVAI RMNLAVFTVD
STQRPRRSFH QAKQRFSHRF LTYRPIFALP NSARLIPMTE
//
