MTR1_DICDI
ID MTR1_DICDI Reviewed; 757 AA.
AC Q54WR1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1;
DE EC=2.1.1.57;
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1;
DE Short=MTr1;
GN ORFNames=DDB_G0279593;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 to produce m(7)GpppNmp (cap1). Cap1 modification is linked
CC to higher levels of translation. {ECO:0000250}.
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;
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DR EMBL; AAFI02000031; EAL67735.1; -; Genomic_DNA.
DR RefSeq; XP_641656.1; XM_636564.1.
DR AlphaFoldDB; Q54WR1; -.
DR SMR; Q54WR1; -.
DR STRING; 44689.DDB0234233; -.
DR PaxDb; Q54WR1; -.
DR EnsemblProtists; EAL67735; EAL67735; DDB_G0279593.
DR GeneID; 8622063; -.
DR KEGG; ddi:DDB_G0279593; -.
DR dictyBase; DDB_G0279593; -.
DR eggNOG; KOG3673; Eukaryota.
DR HOGENOM; CLU_368210_0_0_1; -.
DR InParanoid; Q54WR1; -.
DR OMA; SKQIPIH; -.
DR PhylomeDB; Q54WR1; -.
DR PRO; PR:Q54WR1; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB.
DR GO; GO:0097309; P:cap1 mRNA methylation; ISS:UniProtKB.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR InterPro; IPR030376; Cap_mRNA_MeTrfase_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; PTHR16121:SF0; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS51613; SAM_MT_RRMJ; 1.
PE 3: Inferred from homology;
KW Methyltransferase; mRNA capping; mRNA processing; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..757
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 1"
FT /id="PRO_0000399806"
FT DOMAIN 62..108
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 214..438
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 257
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 301
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 352
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
SQ SEQUENCE 757 AA; 87953 MW; C18AF00EEA2864F1 CRC64;
MFQSNQYDEY NKTNKSDEEN ESNENENENE NENENRSEDG DQDSEDSFIY EEDDEEEEDT
PKLSFGAKFL AKHGHIEGQG LGKEKDGRID LIEVDRFQST KGLGFAENDL PEFYRVTKHI
LEDEDVDFPS KQRFEWISCN SEGYNFWEGF PVDHTLVKFV ANDSITDKPR RGHCSVELLM
ELDQHKNALD TLDPNRFYVA RKKSNPYESI KGSIFINRAA VKMANIDKLA DLLTPIIPVP
GKPRDFIYFG DVCAGPGGFT EYVYWKKTRG GKIKGEEGLD LDDVVKGFGF TIKGQCDWNV
EKFSKQIPIH NFVKEYGLDD TGNILKSENI RDFSSKVFYN TNGFGLQLFL ADGGINTDGK
ESLQELMLQQ LILCQILTMF ETIGRGGNFV CKIFDTFTPF TIGLLYLVYQ HFQSFSIVKP
FTSRPLNSER YIICKNFLSY RPMNIIDFLH YINSLLNNNQ TILELIEINS MDPNFLRYIL
ESNELICLRQ IKAFSLFKKY VEDIELPPID QKEIRAKCLE EWGLPKETKY DIENYQKHKN
RQKHHHNNHS NNNNNNNNSN NNNNNNNQHQ HQHHQHQHHQ NQHQNQYQHQ NQHKKYNNNI
NNNSNNSSPN SSPNLTSSPN LNSPPNINNG NNHQNNNNNN SNNNNNNNNN NNNNNNNNNN
NNNNNNNNKN RRFISTKLVK NNSQFQQKPP PPHRHMSPLQ IQQQFLLQQQ KEQQLLQQPQ
KDQLHQLHQQ QSQSALPDFS AANFMEALLK RKNDSQQ
