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Database: UniProt
Entry: C1MYL6_MICPC
LinkDB: C1MYL6_MICPC
Original site: C1MYL6_MICPC 
ID   C1MYL6_MICPC            Unreviewed;       463 AA.
AC   C1MYL6;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=rRNA methyltransferase 1, mitochondrial {ECO:0000256|ARBA:ARBA00034881};
GN   ORFNames=MICPUCDRAFT_59944 {ECO:0000313|EMBL:EEH55065.1};
OS   Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN   [1] {ECO:0000313|EMBL:EEH55065.1, ECO:0000313|Proteomes:UP000001876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH55065.1,
RC   ECO:0000313|Proteomes:UP000001876};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA   John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA   Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA   Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA   Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the marine
RT   picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase TrmH family.
CC       {ECO:0000256|ARBA:ARBA00007228}.
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DR   EMBL; GG663742; EEH55065.1; -; Genomic_DNA.
DR   RefSeq; XP_003060296.1; XM_003060250.1.
DR   AlphaFoldDB; C1MYL6; -.
DR   STRING; 564608.C1MYL6; -.
DR   GeneID; 9686027; -.
DR   KEGG; mpp:MICPUCDRAFT_59944; -.
DR   eggNOG; KOG0838; Eukaryota.
DR   OMA; EGANTHA; -.
DR   OrthoDB; 5404245at2759; -.
DR   Proteomes; UP000001876; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0031167; P:rRNA methylation; IEA:InterPro.
DR   CDD; cd18105; SpoU-like_MRM1; 1.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR047182; MRM1.
DR   InterPro; IPR047261; MRM1_MeTrfase_dom.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR013123; SpoU_subst-bd.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR46103; RRNA METHYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR46103:SF1; RRNA METHYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   Pfam; PF08032; SpoU_sub_bind; 1.
DR   SMART; SM00967; SpoU_sub_bind; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
DR   SUPFAM; SSF55315; L30e-like; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001876};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          188..276
FT                   /note="RNA 2-O ribose methyltransferase substrate binding"
FT                   /evidence="ECO:0000259|SMART:SM00967"
FT   REGION          20..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   463 AA;  48414 MW;  D48CA9385BABB482 CRC64;
     MTRVATLPGA LLRLNLRCLR PSGGGRVAAS RAPLAARRAP ATTTTSVSSW RMGGGGGEGR
     TTEEPPPRSS PPSSRDRYGY GDDDPSDFED DGPRPGRRGG GGGGGGGRGA GRRGGGFANN
     NSHADRRNPY YTAESSSSSA PRGGRRSRDR GATHDADAQP RTVWQERHDE KKRNRAEPTL
     AERMTGEALY GLNPARAALR DAARRARAGA AARRTIYRMF VQEGSDASGD AALLRAARDA
     RVEIETVSKH DLNVLTGSPP RPHNGVVLDA SALTPTPIDQ LPRWVHGEGS STVKGPAPVW
     LALDEVVDPQ NLGAVLRSAK FLGVAGVVVC AKNSAPLSPV VSKASAGALE SMDVRSVGVM
     HRFLMRCVED GWDVYGTAAE EGAADVADVD ARGRPSVLVM GNEGAGLRTN VRRACTSMLR
     IAGGGGEGDD DDGVDSLNVS VATGVILHAM LTSARRAPAV AEE
//
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