ID Q8DVL0_STRMU Unreviewed; 384 AA.
AC Q8DVL0;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=THUMP domain-containing protein {ECO:0000259|PROSITE:PS51165};
GN OrderedLocusNames=SMU_472 {ECO:0000313|EMBL:AAN58220.1};
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58220.1, ECO:0000313|Proteomes:UP000002512};
RN [1] {ECO:0000313|EMBL:AAN58220.1, ECO:0000313|Proteomes:UP000002512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2] {ECO:0007829|PDB:3LDG}
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RA Wang K.-T., Su X.-D.;
RT "Crystal structure of SMU.472 complexed with SAH.";
RL Submitted (JAN-2010) to the PDB data bank.
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DR EMBL; AE014133; AAN58220.1; -; Genomic_DNA.
DR RefSeq; NP_720914.1; NC_004350.2.
DR RefSeq; WP_002263884.1; NC_004350.2.
DR PDB; 3LDG; X-ray; 1.96 A; A=1-384.
DR PDBsum; 3LDG; -.
DR AlphaFoldDB; Q8DVL0; -.
DR SMR; Q8DVL0; -.
DR STRING; 210007.SMU_472; -.
DR KEGG; smu:SMU_472; -.
DR PATRIC; fig|210007.7.peg.414; -.
DR eggNOG; COG0116; Bacteria.
DR HOGENOM; CLU_032119_3_1_9; -.
DR OrthoDB; 9809404at2; -.
DR PhylomeDB; Q8DVL0; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR GO; GO:0009451; P:RNA modification; IEA:UniProt.
DR CDD; cd11715; THUMP_AdoMetMT; 1.
DR Gene3D; 3.30.2130.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR000241; RlmKL-like_Mtase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004114; THUMP_dom.
DR PANTHER; PTHR47313; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE K/L; 1.
DR PANTHER; PTHR47313:SF1; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE K_L; 1.
DR Pfam; PF02926; THUMP; 1.
DR Pfam; PF01170; UPF0020; 1.
DR SMART; SM00981; THUMP; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51165; THUMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3LDG};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000002512};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00529};
KW Transferase {ECO:0000256|ARBA:ARBA00022603}.
FT DOMAIN 45..159
FT /note="THUMP"
FT /evidence="ECO:0000259|PROSITE:PS51165"
FT BINDING 178
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0007829|PDB:3LDG"
FT BINDING 205
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0007829|PDB:3LDG"
FT BINDING 207
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0007829|PDB:3LDG"
FT BINDING 263
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0007829|PDB:3LDG"
FT BINDING 264
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0007829|PDB:3LDG"
FT BINDING 292
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0007829|PDB:3LDG"
FT BINDING 293
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0007829|PDB:3LDG"
SQ SEQUENCE 384 AA; 43586 MW; D03F7A95CBDA629D CRC64;
MKKTFNLVAT AAAGIEAVVG KELRNLGLDC QVENGRVLFK GNIETIAKSN LWLRSADRIK
IVVGEFPART FEELFQGVYA LDWENYLPLG CQFPVAKAKS VKSKLHNEPS IQGITKKAIV
KKLQHYFHRP DSVPLPENGP EFKIEISLLK DQARVMIDTT GPSLFKRGYR TEKGGAPIKE
NMAAAIILLS NWFPDKPFVD PTCGSGTFCI EAAMIGMNIA PGFNRDFAFE EWPWVDEALV
TRVRNEADEQ ADYDIQLDIS GFDFDGRMVE IARKNAREVG LEDVVKLKQM RLQDFKTNKI
NGVLISNPPY GERLLDDKAV DILYNEMGET FAPLKTWSQF ILTNDTDFEQ KFGRKADKKR
KLYNGSLKVD LYQFYGQRVK RVLR
//
