GenomeNet

Database: UniProt
Entry: I0QHJ1_STRSL
LinkDB: I0QHJ1_STRSL
Original site: I0QHJ1_STRSL 
ID   I0QHJ1_STRSL            Unreviewed;       456 AA.
AC   I0QHJ1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Putative RNA methyltransferase {ECO:0000313|EMBL:EIC80751.1};
GN   ORFNames=PS4_26920 {ECO:0000313|EMBL:EIC80751.1};
OS   Streptococcus salivarius PS4.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1157946 {ECO:0000313|EMBL:EIC80751.1, ECO:0000313|Proteomes:UP000010314};
RN   [1] {ECO:0000313|EMBL:EIC80751.1, ECO:0000313|Proteomes:UP000010314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PS4 {ECO:0000313|EMBL:EIC80751.1,
RC   ECO:0000313|Proteomes:UP000010314};
RX   PubMed=22843595; DOI=10.1128/JB.00896-12;
RA   Martin V., Maldonado-Barragan A., Jimenez E., Ruas-Madiedo P.,
RA   Fernandez L., Rodriguez J.M.;
RT   "Complete Genome Sequence of Streptococcus salivarius PS4, a Strain
RT   Isolated from Human Milk.";
RL   J. Bacteriol. 194:4466-4467(2012).
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:EIC80751.1}.
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; AJFW01000046; EIC80751.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0QHJ1; -.
DR   PATRIC; fig|1157946.4.peg.1381; -.
DR   Proteomes; UP000010314; 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   456 AA;  51476 MW;  107C89BBF5364A93 CRC64;
     MLNKNAIVEV EIVDLTHEGA GVAKVDGFVF FVDNALPGEV IKMRVLKLKK NIGFGKVEEF
     VTLSPNRNQD IDATYLRSGI ADFGHMTYEE QLKFKRKQVV DNLYKTAGVS DVEVAETLGM
     ETPYAYRNKA QVPVRRVKGQ LETGFYRKNS HDLIPIEDFL IQDKEIDKLI VFVRDLLRRY
     DLKPYDEKEQ TGLIRHLVVR RGHYSGQMML VFVTTRPKVF RIDQIIAKIT EAFPSVVSII
     QNINDKNTNA IFGKEFRTLY GQDTITDSML GNDYEISAQS FYQVNTEMAE KLYQTAIDFS
     DLTSDSIVID AYSGIGTIGL SFAKQVKEVY GVEVIETAVE DAKKNAERNG ITNAHYVADS
     AENAMAKWSK DGIKPDVIIV DPPRKGLTES FIKASVAMQP EKITYVSCNP ATMARDIKRY
     QELGYELKKV QPVDLFPQTH HVEAVSLLVR AETSAK
//
DBGET integrated database retrieval system