ID MRAW_PROMA Reviewed; 305 AA. AC Q7VE18; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 10-JUN-2008, entry version 31. DE S-adenosyl-L-methionine-dependent methyltransferase mraW (EC 2.1.1.-). GN Name=mraW; OrderedLocusNames=Pro_0196; OS Prochlorococcus marinus. OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=1219; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SARG / CCMP 1375 / SS120; RX MEDLINE=22810154; PubMed=12917486; DOI=10.1073/pnas.1733211100; RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., RA Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., RA Scanlan D.J., Tandeau de Marsac N., Weissenbach J., Wincker P., RA Wolf Y.I., Hess W.R.; RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, RT a nearly minimal oxyphototrophic genome."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003). CC -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent CC methyltransferase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. MraW CC family. 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; AE017126; AAP99242.1; -; Genomic_DNA. DR RefSeq; NP_874590.1; -. DR GeneID; 1461575; -. DR GenomeReviews; AE017126_GR; Pro_0196. DR KEGG; pma:Pro0196; -. DR HOGENOM; Q7VE18; -. DR BioCyc; PMAR167539:PRO_0196-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0008168; F:methyltransferase activity; IEA:HAMAP. DR HAMAP; MF_01007; -; 1. DR InterPro; IPR002903; Bact_MeTrfase. DR PANTHER; PTHR11265; Bact_methyltrans; 1. DR Pfam; PF01795; Methyltransf_5; 1. DR PIRSF; PIRSF004486; MraW; 1. DR ProDom; PD004685; Bact_methyltrans; 1. DR TIGRFAMs; TIGR00006; Bact_methyltrans; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 305 S-adenosyl-L-methionine-dependent FT methyltransferase mraW. FT /FTId=PRO_0000108682. FT REGION 47 49 S-adenosyl-L-methionine binding (By FT similarity). FT BINDING 66 66 S-adenosyl-L-methionine (By similarity). FT BINDING 93 93 S-adenosyl-L-methionine; via amide FT nitrogen (By similarity). FT BINDING 108 108 S-adenosyl-L-methionine (By similarity). FT BINDING 115 115 S-adenosyl-L-methionine (By similarity). SQ SEQUENCE 305 AA; 33870 MW; ECC8EEF9228D763A CRC64; MKEESKIVTS KFKHTPVLVN QVLEAIAKLP SELLIKGKLI DATIGGGGHS ALILKGFPSL HITGLDQDPS AIDAASKQLL HFGSRAEIIS SNFADFVPQE EVAFVLADLG VSSPQIDEAK RGFSFRLNGP LDMRMNPKKG LKADELLEKT EEKALADLIY KYGEEKFSRR IARRIKQDLS ANGPYEGTSA LAYAIAGCYP PKMRNGRIHP ATRTFQALRI AINNELDALQ HLLQKAPNWL LPGGVFAVIS FHSLEDRLVK KSFLTDERLE RITRKPIQAD SNEKLNNPRS RSAKLRLAKK RNPNE //