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Database: UniProt
Entry: C7NI84_KYTSD
LinkDB: C7NI84_KYTSD
Original site: C7NI84_KYTSD 
ID   C7NI84_KYTSD            Unreviewed;       401 AA.
AC   C7NI84;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=SAM-dependent methyltransferase, tRNA(Uracil-5)-methyltransferase {ECO:0000313|EMBL:ACV06591.1};
GN   OrderedLocusNames=Ksed_15760 {ECO:0000313|EMBL:ACV06591.1};
OS   Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541)
OS   (Micrococcus sedentarius).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC   Kytococcus.
OX   NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV06591.1};
RN   [1] {ECO:0000313|EMBL:ACV06591.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20547 {ECO:0000313|EMBL:ACV06591.1};
RX   PubMed=21304632; DOI=10.4056/sigs.761;
RA   Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA   Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA   Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S.,
RA   Goker M., Pukall R., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Kytococcus sedentarius type strain (541).";
RL   Stand. Genomic Sci. 1:12-20(2009).
RN   [2] {ECO:0000313|EMBL:ACV06591.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 20547;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Sims D., Brettin T., Detter J.C., Han C., Kuske C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Kytococcus sedentarius DSM 20547.";
RL   Submitted (AUG-2009) 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}.
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DR   EMBL; CP001686; ACV06591.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7NI84; -.
DR   STRING; 478801.Ksed_15760; -.
DR   KEGG; kse:Ksed_15760; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_11; -.
DR   Proteomes; UP000006666; Chromosome.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
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; 2.
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   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-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.
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..54
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        356
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         230
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         259
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
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         329
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   401 AA;  41792 MW;  07245312A294CFD3 CRC64;
     MVEVGEVAHG GHCVARMPDG RVVFVRHALP GEQVELLVTE GGSDSRFLRA DAVRVLRAAP
     GRREAPCRFS GPGGCGGCDF QHATPEAQLE LKQQVLTDQL RRLAGYEGPV EMRALETQGP
     AGLRWRTRVE FTLGADGVPG LRRHRSHELV PVDDCLIATE AVVGAAGLGR PRGAGVTGID
     VVAPAVGDAV VVELGHRGRV LGSEPVVQEQ TVSPEGEPLA VHLGARGFWQ AHPAAVPTYV
     QHVLAELDPR PGERVWDLFS GSGAFTVPLA LAVGATGEVL AVEGSEPAVD ACAAALEEHA
     PHTVADLVVG DVAETLARWE GGTDLVVLDP PRTGAGPAVV EAVAASGASR IAYVACDPAA
     LGRDLGHARQ AGLEVERVVG FDAFGTTHHL EAIATLRRAR G
//
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