CMTR1_AILME
ID CMTR1_AILME Reviewed; 835 AA.
AC D2HRF1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1;
DE EC=2.1.1.57 {ECO:0000250|UniProtKB:Q8N1G2};
DE AltName: Full=Cap methyltransferase 1;
DE AltName: Full=Cap1 2'O-ribose methyltransferase 1;
DE Short=MTr1;
DE AltName: Full=FtsJ methyltransferase domain-containing protein 2;
GN Name=CMTR1; Synonyms=FTSJD2; ORFNames=PANDA_014567;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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:0000250|UniProtKB:Q8N1G2}.
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:0000250|UniProtKB:Q8N1G2};
CC -!- SUBUNIT: Interacts with POLR2A (via C-terminus).
CC {ECO:0000250|UniProtKB:Q8N1G2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N1G2}.
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DR EMBL; GL193218; EFB19601.1; -; Genomic_DNA.
DR RefSeq; XP_002925128.1; XM_002925082.3.
DR AlphaFoldDB; D2HRF1; -.
DR SMR; D2HRF1; -.
DR STRING; 9646.ENSAMEP00000016193; -.
DR Ensembl; ENSAMET00000016867; ENSAMEP00000016193; ENSAMEG00000015322.
DR GeneID; 100464010; -.
DR KEGG; aml:100464010; -.
DR CTD; 23070; -.
DR eggNOG; KOG3673; Eukaryota.
DR InParanoid; D2HRF1; -.
DR OrthoDB; 1336442at2759; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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 CDD; cd00201; WW; 1.
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 InterPro; IPR001202; WW_dom.
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 SMART; SM00456; WW; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS51613; SAM_MT_RRMJ; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
PE 3: Inferred from homology;
KW Acetylation; Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..835
FT /note="Cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase 1"
FT /id="PRO_0000399797"
FT DOMAIN 87..133
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 231..450
FT /note="RrmJ-type SAM-dependent 2'-O-MTase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT DOMAIN 752..786
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 24..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..835
FT /note="Interaction with POLR2A"
FT /evidence="ECO:0000250"
FT MOTIF 2..19
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 31..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT ACT_SITE 364
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT ACT_SITE 404
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00945"
FT BINDING 203..207
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 277..283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 335..336
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 374..376
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC3"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBC3"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1G2"
SQ SEQUENCE 835 AA; 94950 MW; 83A98A0FC16C1A5C CRC64;
MRRRNDPECT APIKKQKKRV AELALNLSAA SGDEPPSSVN HAAKASTTSL SGSDSETEGK
QHGSDSFDDA FKADSLVEGT SSRYSMYNSV SQKLMAKMGF REGEGLGKYS QGRKDIVEAS
NQKGRRGLGL TLQGFDQELN VDWRDEPEPS ACEQVSWFPE CTTEIPDTQE MSDWMVVGKR
KMVIEDETEF CGEELLHSVL QCKSVFDVLD GDEMRRARTR ANPYEMIRGV FFLNRAAMKM
ANMDFVFDRM FTNPRDSCGK PLVKDREAEL LYFADVCAGP GGFSEYVLWR KKWHAKGFGM
TLKGPNDFKL EDFYSASSEL FEPYYGEGGI DGDGDITRPE NITAFRNFVL DNTDRKGVHF
LMADGGFSVE GQENLQEILS KQLLLCQFLM ALSVVRTGGH FICKTFDLFT PFSAGLIYLL
YCCFERVCLF KPITSRPANS ERYVVCKGLK VGIDDVRDYL FAVNIKLNQL HNTDSDVSLV
VPLEVIKGDH EFTDYMIRSN ESHCSLQIKA LAKIHAFVQD TTLSEPRQAE IRKECLRLWG
IPDQARVAPS SSDPKSKFFE LIQGTEIDIF SYKPTLLTSK TLEKIRPVLD YRCMVSGSEQ
KFLIGLGKSQ IYTWDGRQSD RWVKLDLKTE LPRDTLLSVE IVHELKGEGK AQRKISAIHI
LDVLVLNGSD VREQHFNQRI QLAEKFVKAV SKPSRPDMNP IRVKEVYRLE EMEKIFVRLE
MKIIKGSSGT PKLSYTGRDD RHFVPTGLYI VRTVNEPWTM GFSKSFKRKF FYNKKTKIST
FDLPADSIAP FHICYYGRLF WEWGDGIRVH DSQKPQDPDK LSKEDVLSFI QTHSA
