ID   RAMAC_PONAB             Reviewed;         118 AA.
AC   Q5R9Q6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=RNA guanine-N7 methyltransferase activating subunit {ECO:0000250|UniProtKB:Q9BTL3};
DE   AltName: Full=Protein FAM103A1;
DE   AltName: Full=RNA guanine-7 methyltransferase activating subunit {ECO:0000250|UniProtKB:Q9BTL3};
DE   AltName: Full=RNMT-activating mRNA cap methylating subunit {ECO:0000250|UniProtKB:Q9BTL3};
DE   AltName: Full=RNMT-activating mRNA cap methyltransferase subunit;
DE   AltName: Full=RNMT-activating mini protein {ECO:0000250|UniProtKB:Q9BTL3};
DE            Short=RAM {ECO:0000250|UniProtKB:Q9BTL3};
GN   Name=RAMAC; Synonyms=FAM103A1, RAMMET;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory subunit of the mRNA-capping methyltransferase
CC       RNMT:RAMAC complex that methylates the N7 position of the added
CC       guanosine to the 5'-cap structure of mRNAs. Promotes the recruitment of
CC       the methyl donor, S-adenosyl-L-methionine, to RNMT. Regulates RNMT
CC       expression by a post-transcriptional stabilizing mechanism. Binds RNA.
CC       {ECO:0000250|UniProtKB:Q9BTL3}.
CC   -!- SUBUNIT: Interacts with RNMT; this interaction enhances mRNA binding
CC       and cap methyltransferase activity. {ECO:0000250|UniProtKB:Q9BTL3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BTL3}.
CC   -!- SIMILARITY: Belongs to the RAM family. {ECO:0000305}.
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DR   EMBL; CR859326; CAH91504.1; -; mRNA.
DR   RefSeq; NP_001125885.1; NM_001132413.1.
DR   AlphaFoldDB; Q5R9Q6; -.
DR   SMR; Q5R9Q6; -.
DR   STRING; 9601.ENSPPYP00000024226; -.
DR   Ensembl; ENSPPYT00000007954; ENSPPYP00000007643; ENSPPYG00000006736.
DR   GeneID; 100172817; -.
DR   KEGG; pon:100172817; -.
DR   CTD; 83640; -.
DR   eggNOG; ENOG502S60Q; Eukaryota.
DR   GeneTree; ENSGT00390000011190; -.
DR   HOGENOM; CLU_144253_0_0_1; -.
DR   InParanoid; Q5R9Q6; -.
DR   OMA; PPIIEEW; -.
DR   OrthoDB; 1548572at2759; -.
DR   TreeFam; TF335880; -.
DR   Proteomes; UP000001595; Chromosome 15.
DR   GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR   GO; GO:0031533; C:mRNA cap methyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008047; F:enzyme activator activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; ISS:UniProtKB.
DR   GO; GO:0032259; P:methylation; ISS:UniProtKB.
DR   GO; GO:0036031; P:recruitment of mRNA capping enzyme to RNA polymerase II holoenzyme complex; ISS:UniProtKB.
DR   GO; GO:0106005; P:RNA 5'-cap (guanine-N7)-methylation; IEA:InterPro.
DR   InterPro; IPR028271; RAMAC.
DR   Pfam; PF15320; RAM; 1.
PE   3: Inferred from homology;
KW   Acetylation; Methylation; mRNA capping; mRNA processing; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT   CHAIN           2..118
FT                   /note="RNA guanine-N7 methyltransferase activating subunit"
FT                   /id="PRO_0000089985"
FT   REGION          2..55
FT                   /note="Interaction with RNMT"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT   REGION          30..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..118
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT   MOTIF           36..42
FT                   /note="RNMT-activating domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT   COMPBIAS        58..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT   MOD_RES         85
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTL3"
SQ   SEQUENCE   118 AA;  14367 MW;  50B03D8BDE63E4BA CRC64;
     MTDTAEAVPN FEEMFASRFT ENDKEYQEYL KRPPESPPIV EEWNSRAGGN QRNRGNRLQD
     NRQFRGRDNR WGWPSDNRSN QWHGRSWGNN YPQHRQEPYY PQQYGHYGYN QRPPYGYY