ID C1MVK9_MICPC Unreviewed; 812 AA.
AC C1MVK9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EEH56008.1};
GN ORFNames=MICPUCDRAFT_59415 {ECO:0000313|EMBL:EEH56008.1};
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:EEH56008.1, ECO:0000313|Proteomes:UP000001876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH56008.1,
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 I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG663741; EEH56008.1; -; Genomic_DNA.
DR RefSeq; XP_003060056.1; XM_003060010.1.
DR AlphaFoldDB; C1MVK9; -.
DR STRING; 564608.C1MVK9; -.
DR GeneID; 9685494; -.
DR KEGG; mpp:MICPUCDRAFT_59415; -.
DR eggNOG; KOG2198; Eukaryota.
DR OrthoDB; 8499at2759; -.
DR Proteomes; UP000001876; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001876};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}.
FT DOMAIN 117..548
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 424
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 274
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 371
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 812 AA; 87039 MW; FCD45EFD38A66800 CRC64;
MGKRNRSRAM VLARKRRGGA PAKPAAGAKD GGDAGAIPNK ITFDDDDDDD DDDDDGDGDV
REVPPPPPPR APDEKIVLPR TSAPWFSRTL SARSTTHFEE YYRRQNILAD EREWSAFLAH
LRAPLPVTFR MSIMASHRAG VEEALREGKR LLTPGAENPR PRTDDGRVVP PPRRLDWCDG
WQLGVDKMTL KYSRDATLRE TQRWLVKHNS TGVLTRQAVD SMVPAAILGV EPHHAVLDLC
ASPGSKTTQC LEALHAGGET GGGGAPAGCV AANDIDPRRC YFLVRRCAAL GAATQALMVT
NHHAQWFPNG NVPLTTVAGG TTPGRGRDAI AKAIAKAKAN GAPGSAPLAP FATREDGGRY
PEGSFDRIIC DVPCSGDGTL RKNPQIWSEW RPEFAMGLHA LQLRIAQRGV ALLKVGGYMV
YSTCSFNPVE NEAVVAELLR RCGDAIELVD ASDRVKGLRR REGMTTWKVI TTVDDEILEH
ASYEDCQRDA SLGVGLRRAF RPSMWPPVAS GVTRLGVRVR GPPLRRCVRL VPQDGDMGGF
FAALIRKVKP LRGPSPTSEG VSTAMKAPGA SAIVPRAMAI GGLVGGVPRP PLEHRYVPAP
EEVLDALTRE WGGGGGGDAM REMCACLFTR STSCRRVTYL SPGIKKMCVD AIGAERLKCV
WSGVRVWEKR DDVRGGGGGG GGGGGGGAFP YRLTKEGAVV LARHAGDARR LLMPARDVKQ
LLRDLGADVP LKAFTPAVAN AARAMTPGSV LCELKKVGGG SDDACPPLAV ELTPEGTLRV
EWRYRKGLEG APKAAAAAIL RKLDANSRDG GY
//
