GenomeNet

Database: UniProt
Entry: K9XRS8_STAC7
LinkDB: K9XRS8_STAC7
Original site: K9XRS8_STAC7 
ID   K9XRS8_STAC7            Unreviewed;       455 AA.
AC   K9XRS8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:AFZ35315.1};
DE            EC=2.1.1.190 {ECO:0000313|EMBL:AFZ35315.1};
GN   OrderedLocusNames=Sta7437_1757 {ECO:0000313|EMBL:AFZ35315.1};
OS   Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC   Stanieria.
OX   NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ35315.1, ECO:0000313|Proteomes:UP000010473};
RN   [1] {ECO:0000313|Proteomes:UP000010473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA   Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA   Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA   Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT   genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
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; CP003653; AFZ35315.1; -; Genomic_DNA.
DR   RefSeq; WP_015192986.1; NC_019748.1.
DR   AlphaFoldDB; K9XRS8; -.
DR   STRING; 111780.Sta7437_1757; -.
DR   KEGG; scs:Sta7437_1757; -.
DR   PATRIC; fig|111780.3.peg.1833; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_3; -.
DR   OMA; FYAGDMK; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000010473; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000010473};
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          4..62
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        410
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        410
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         287
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         316
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         337
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         382
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   455 AA;  51067 MW;  ED9F048DDF32AD77 CRC64;
     MTKKWQQGEL VELEIVDLNS SGEGVGKING KVVFIPDTVT GDRALVRLTK VKNKYSYGKI
     EQLLIASPYR IRPRCIVADK CGGCQWQHID WEYQLDSKRQ QVLQALQRIG GFSQVQVKPT
     LHTPYSLNYR NKSTYPLGIS ASGQVQAGYY RQGSHQLINL NQCPVQDARL HPLLAEVKQD
     LQKQGWTIYN EKTHQGQLRH LSLRIGNRTG EILLTLVTTD KNLTEIEAQA QTWLTRYPQL
     VGVCLNYNPE RTNVIFGQET ITVAGSSYLR EIFAGVELNI LSDTFFQVNT EAAELLLSDI
     TKQLNLEGDE TIVDAYCGIG TFTLPLAKQA KSIVGIELHP TSVEQAKQNA NINQITNVTF
     YAEAVETLLP QLEFTPDLIL LDPPRKGCEP QVIETLINLS PSPRIIYVSC KPATLARDLN
     LLCQSGKYQL NFVQPVDFFP QTTHIESYAY LNATS
//
DBGET integrated database retrieval system