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Database: UniProt
Entry: K9XBB4_9CHRO
LinkDB: K9XBB4_9CHRO
Original site: K9XBB4_9CHRO 
ID   K9XBB4_9CHRO            Unreviewed;       466 AA.
AC   K9XBB4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:AFZ29793.1};
DE            EC=2.1.1.190 {ECO:0000313|EMBL:AFZ29793.1};
GN   ORFNames=Glo7428_1221 {ECO:0000313|EMBL:AFZ29793.1};
OS   Gloeocapsa sp. PCC 7428.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ29793.1, ECO:0000313|Proteomes:UP000010476};
RN   [1] {ECO:0000313|EMBL:AFZ29793.1, ECO:0000313|Proteomes:UP000010476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ29793.1,
RC   ECO:0000313|Proteomes:UP000010476};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
RL   Submitted (JUN-2012) 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; CP003646; AFZ29793.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9XBB4; -.
DR   STRING; 1173026.Glo7428_1221; -.
DR   KEGG; glp:Glo7428_1221; -.
DR   PATRIC; fig|1173026.3.peg.1289; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_3; -.
DR   Proteomes; UP000010476; 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; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
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; 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.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000010476};
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          18..76
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        422
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         300
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"
FT   BINDING         350
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         395
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   466 AA;  52448 MW;  EF42AF1F09F9AC76 CRC64;
     MSITELSNID AQNQSKNLWR QGNLVEVVIH DLSDTGDGVG KFGDRVVFVP DTTPGDRALV
     RLTYTKPEFA RAKLYELLES SPHRIRPSCI VADKCGGCQW QHISYKYQLE AKRNLVVQAL
     QRIGGFEHPP VDSVLAAPSP LSYRNKATYP LGISATGQVQ AGYFQKNSHQ LINLNQCPIQ
     DSRLNPLLRE VKQDIQHQNW QIYDEKRHQG QIRHLALRIG RRTGEMLLTL VVKDWIPEMT
     TQAQKWLQRY PQLVGVAVNR NSDRTNAIFG QETRCIAGKD YLIEEFAGLQ FQIRPETFFQ
     VNTEVAEALL QQIAQQLNLQ GHEVLLDAYC GIGTLTLPLA QQARQVIGLE LQPTSVQQAQ
     RNADLNHINN VTFQAGRVEK LLPQLEIVPD VVLLDPPRKG CDRTVIETLL QVQPSQIVYV
     SCKAATLARD LKLLCQTGIY HLVRVQPADF FPQTSHVECA AFLVSG
//
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