ID   RAMAC_XENTR             Reviewed;         116 AA.
AC   Q28HC9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 64.
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 methyltransferase subunit {ECO:0000250|UniProtKB:Q9BTL3};
DE   AltName: Full=RNMT-activating mini protein {ECO:0000250|UniProtKB:Q9BTL3};
DE            Short=RAM {ECO:0000250|UniProtKB:Q9BTL3};
GN   Name=ramac; Synonyms=fam103a1, rammet; ORFNames=TEgg087e08.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BTL3}.
CC   -!- SIMILARITY: Belongs to the RAM family. {ECO:0000305}.
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DR   EMBL; CR760936; CAJ82021.1; -; mRNA.
DR   RefSeq; NP_001037960.1; NM_001044495.1.
DR   RefSeq; XP_012814615.1; XM_012959161.2.
DR   AlphaFoldDB; Q28HC9; -.
DR   SMR; Q28HC9; -.
DR   STRING; 8364.ENSXETP00000061426; -.
DR   PaxDb; Q28HC9; -.
DR   DNASU; 733725; -.
DR   Ensembl; ENSXETT00000060801; ENSXETP00000061426; ENSXETG00000030369.
DR   GeneID; 733725; -.
DR   KEGG; xtr:733725; -.
DR   CTD; 83640; -.
DR   Xenbase; XB-GENE-969014; ramac.
DR   eggNOG; ENOG502S60Q; Eukaryota.
DR   HOGENOM; CLU_144253_0_0_1; -.
DR   InParanoid; Q28HC9; -.
DR   OMA; PPIIEEW; -.
DR   OrthoDB; 1548572at2759; -.
DR   PhylomeDB; Q28HC9; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000030369; Expressed in ovary and 13 other tissues.
DR   ExpressionAtlas; Q28HC9; differential.
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   mRNA capping; mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT   CHAIN           1..116
FT                   /note="RNA guanine-N7 methyltransferase activating subunit"
FT                   /id="PRO_0000295548"
FT   REGION          1..55
FT                   /note="Interaction with RNMT"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BTL3"
FT   REGION          31..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..116
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        46..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   116 AA;  14301 MW;  34FFBEB4E1579C64 CRC64;
     MAEALGAQEL YEKMFEQRFT ANDKEYQEYL KREQDQPPIV EDWKMGNQRN TDRYRDNRHH
     RGWDGRQNWS SNSYNQSYGR GGWGNSYNQY RQDRHNYQQG HYTHNPSNQR FHSDRY