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Database: UniProt
Entry: F2U529_SALR5
LinkDB: F2U529_SALR5
Original site: F2U529_SALR5 
ID   F2U529_SALR5            Unreviewed;       797 AA.
AC   F2U529;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=mRNA m(6)A methyltransferase {ECO:0000256|ARBA:ARBA00012160};
DE            EC=2.1.1.348 {ECO:0000256|ARBA:ARBA00012160};
GN   ORFNames=PTSG_03395 {ECO:0000313|EMBL:EGD82745.1};
OS   Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX   NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN   [1] {ECO:0000313|Proteomes:UP000007799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Salpingoeca rosetta.";
RL   Submitted (AUG-2009) 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; GL832961; EGD82745.1; -; Genomic_DNA.
DR   RefSeq; XP_004995981.1; XM_004995924.1.
DR   AlphaFoldDB; F2U529; -.
DR   STRING; 946362.F2U529; -.
DR   EnsemblProtists; EGD82745; EGD82745; PTSG_03395.
DR   GeneID; 16076568; -.
DR   KEGG; sre:PTSG_03395; -.
DR   eggNOG; KOG2098; Eukaryota.
DR   InParanoid; F2U529; -.
DR   OrthoDB; 179166at2759; -.
DR   Proteomes; UP000007799; Unassembled WGS sequence.
DR   GO; GO:0001734; F:mRNA (N6-adenosine)-methyltransferase activity; IEA:UniProt.
DR   InterPro; IPR007757; MT-A70-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12829; N6-ADENOSINE-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR12829:SF2; N6-ADENOSINE-METHYLTRANSFERASE CATALYTIC SUBUNIT; 1.
DR   Pfam; PF05063; MT-A70; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51143; MT_A70; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:EGD82745.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007799};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGD82745.1}.
FT   REGION          24..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          415..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..455
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..481
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..530
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..783
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   797 AA;  88790 MW;  BD49D67F3C6FEDBC CRC64;
     MDATELEDAP VDDVLDAIFG VLPGSHASFG SKDRQAGNDG QGDRSDADGD SEDADDLGQT
     HQEKETREVL KELDTLLNTP TVMERAIEEE FRLNGKDVFL FCDHDTAEEC AQQSVSGMPC
     DRLHFRRVIQ PHTTHRYGNC RYLDRCFDMR TCKAVHYDVD ESDVECIRRR LKHKRELARQ
     RPDLEAHIDL NVFRTFPAQW IQCDVRYIDF SVLGKFSVIM ADPPWRINME LPYGTMSDEE
     MRQLPVQDLQ DNGVIFLWVT ARCVDLGREL LKRWGYNYAN DLIWIKINQL QNLVRTGRTG
     HWMNHAKEHC MIGVKGNLDG IYPGIDCDVL VSEVRDTSRK PDEIYGLIER LSPGTRKIEL
     FGRPHNVQSN WLTLGDQLQG VQLEDDALVQ RFTERYPYSP ADTLSLLLQN KLPSSSTAHK
     ARGEEHSDVD TSAGPRARQQ SHRHQHNHRH QHHLDDSHNR HSQAHHHQER PSSRHRPSHQ
     HRHHDDGGGD DSAERASRSG RARTPLRTVH TQRRRDSSEG RDEPVAVRGR SRSVGRDALQ
     AYGGGRSASV SGGHSKADEL MHTYGHHGPR RHDRQHQHQF RSSPRQQQLQ HVYYQQRKPG
     SIPESRSMSV DRTTSHGSSR GSGDGNDTGH NASAGNRPVF VPRSNAVEGE VVLNLRGHSG
     YWKRDRHGSK IFIRVLPKRK DDDDDDGGDD GGAGDDGGDD VDGGGGGVDG GDGDTPLVPP
     AQQSPLAASV APHTGSVTPP TPQTRQTVSP TPPQTGVHAD ATTTAPSAAP TAANTTATPA
     TLPASWSAAD LWGDKVE
//
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