ID A0A0C9MGT6_9FUNG Unreviewed; 934 AA.
AC A0A0C9MGT6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=mRNA m(6)A methyltransferase {ECO:0000256|ARBA:ARBA00012160};
DE EC=2.1.1.348 {ECO:0000256|ARBA:ARBA00012160};
GN ORFNames=MAM1_0127d06013 {ECO:0000313|EMBL:GAN06529.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN06529.1};
RN [1] {ECO:0000313|EMBL:GAN06529.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN06529.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(6)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55584, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.348;
CC Evidence={ECO:0000256|ARBA:ARBA00036277};
CC -!- SIMILARITY: Belongs to the MT-A70-like family. {ECO:0000256|PROSITE-
CC ProRule:PRU00489}.
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DR EMBL; DF836416; GAN06529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MGT6; -.
DR STRING; 91626.A0A0C9MGT6; -.
DR OrthoDB; 1357820at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR006342; FkbM_mtfrase.
DR InterPro; IPR007757; MT-A70-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR01444; fkbM_fam; 1.
DR PANTHER; PTHR12829; N6-ADENOSINE-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR12829:SF2; N6-ADENOSINE-METHYLTRANSFERASE CATALYTIC SUBUNIT; 1.
DR Pfam; PF05050; Methyltransf_21; 1.
DR Pfam; PF05063; MT-A70; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 3.
DR PROSITE; PS51143; MT_A70; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 610..789
FT /note="Methyltransferase FkbM"
FT /evidence="ECO:0000259|Pfam:PF05050"
FT REGION 439..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 106440 MW; D5ADC6D97AB92F10 CRC64;
MSERPKRKRR QATALAASTH ARVSNAHYVG YVEDNESVEA IMKKFEELER IQQEFTSSPQ
LVSNTPPAKP EQDGCVQDTL IEDPLTQEQL EEVFRRTSAF TVKSASLDPN FVVDMDALDL
LQAEYRNNDT NEFVEEDDYY YVGDDFDLNE QVDDKDGQYR DRDYRRSTPS KKKRLDRQSV
LNKHKILAAQ AKDETGRIVT AKKQVCSIDP SLPTYVKIPP RPIKASWAHF IKPLSEIIPP
THYTYHEVKN LVDQDLTQYG SQFQAIYMDP PLLMAGEAPT PGKINIDDLA KLNVPDVIET
GFLFIWSEKE WLHRIVKIAT QWGFRYVENY CWVKKNINNT IYKGESNYFC KSKLNLLIFK
KEKSKIEIRH QRNADCLFDF VKPMVAGQFT EPKPSYVYHV IETLLPKSVQ ESRLLKLWST
RNYRRLGWTT VAEVTKDNVG AFEPPPFNPN TGADSHPPPP PPPPPPAQPN IGISPIAEAK
LAEHVGINPQ PLDEPDTHYP DTHAKSSQDL DTIAPTADKT TYRLAPEGLK YAQSGDLWQF
GVINTKPDVF IVSNTNYPDV NNHYHREFRI YTLMKWILRV HRRDPERTAP LVMVDAGSNH
GLFSLVAGAS GAHTIAFEPQ THLRSVINMA GRLNQLSQRL RVLPFAVLDQ FKKLAMEKVE
INDGGIGGLS YDNPNALITT QTIRLDTLPA YNRLFPQSTA MEKQLKINTD RKDDKSILEP
EDLGAEYAKE IEAASDNASA EIPESLLFRQ PIHFLKIDVE GFELPALRSA AKLFENQLVE
NTVLEFGPPS RWDVTVPDAN HMDLKDVRAK TMKEAKEVLH RAVDEWGLDI NLLPAEGWEK
TVKFMIDHGI DLSGGNPSKN KVVQRVNAWK FDDLPLDHDE FEKELEIKEN VVTEFIRLPA
RLIDDYLEAS QAIGEMYLWF TKKDTQSPVL QKIT
//