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Database: UniProt
Entry: F9MKI2_STRMT
LinkDB: F9MKI2_STRMT
Original site: F9MKI2_STRMT 
ID   F9MKI2_STRMT            Unreviewed;       453 AA.
AC   F9MKI2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:EGU70325.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:EGU70325.1};
GN   Name=rumA_2 {ECO:0000313|EMBL:EGU70325.1};
GN   ORFNames=HMPREF9959_0801 {ECO:0000313|EMBL:EGU70325.1};
OS   Streptococcus mitis SK569.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1035187 {ECO:0000313|EMBL:EGU70325.1, ECO:0000313|Proteomes:UP000003550};
RN   [1] {ECO:0000313|EMBL:EGU70325.1, ECO:0000313|Proteomes:UP000003550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK569 {ECO:0000313|EMBL:EGU70325.1,
RC   ECO:0000313|Proteomes:UP000003550};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGU70325.1}.
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DR   EMBL; AFUF01000038; EGU70325.1; -; Genomic_DNA.
DR   RefSeq; WP_000914551.1; NZ_AFUF01000038.1.
DR   AlphaFoldDB; F9MKI2; -.
DR   PATRIC; fig|1035187.4.peg.1297; -.
DR   eggNOG; COG2265; Bacteria.
DR   Proteomes; UP000003550; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0001510; P:RNA methylation; IEA:GOC.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   NCBIfam; TIGR00479; rumA; 1.
DR   PANTHER; PTHR11061:SF48; 23S RRNA (URACIL(747)-C(5))-METHYLTRANSFERASE RLMC; 1.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   Pfam; PF01938; TRAM; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS50926; TRAM; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}.
FT   DOMAIN          1..59
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        408
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         283
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         312
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         333
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         381
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   453 AA;  51306 MW;  8927813D4A429BCC CRC64;
     MLKKNDIVEV EIVDLTHEGA GVAKVDGLVF FVENALPSEK ILMRVLKVNK KIGFGKVEEY
     LVQSPHRNQD LDLAYLRSGI ADLGHLAYPE QLKFKTKKVK DSLYKIAGIA DVEVAETLGM
     ENPVKYRNKA QVPVRRVNGV LETGFFRKNS HDLMPLEDFF IQDSVIDEVV VALRDLLRRY
     DLKPYDEKEQ AGLIRNLVVR RGHYSGQIMV ILVTTRPKVF RVEQLIDQLI KQFPEIVSVM
     QNINDQNTNA IFGKEWRTLY GQDYITDQML ENDYQIAGPA FYQVNTQMAE KLYQTAIDFA
     ELKADDVVID AYSGIGTIGL SVAKHVKEVY GVEVIPEAVE NSKKNAQLNN ISNAHYVCDT
     AENAMKTWLK EGIQPTVILV DPPRKGLTES FIKASSQTGA DRIAYISCNV TTMARDIKLY
     QELGYELKKV QPVDLFPQTH HVECVVLLQR KKG
//
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