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Database: UniProt
Entry: A5G5A6_GEOUR
LinkDB: A5G5A6_GEOUR
Original site: A5G5A6_GEOUR 
ID   A5G5A6_GEOUR            Unreviewed;       470 AA.
AC   A5G5A6;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:ABQ26974.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:ABQ26974.1};
GN   OrderedLocusNames=Gura_2801 {ECO:0000313|EMBL:ABQ26974.1};
OS   Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ26974.1, ECO:0000313|Proteomes:UP000006695};
RN   [1] {ECO:0000313|EMBL:ABQ26974.1, ECO:0000313|Proteomes:UP000006695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rf4 {ECO:0000313|EMBL:ABQ26974.1,
RC   ECO:0000313|Proteomes:UP000006695};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA   Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter uraniireducens Rf4.";
RL   Submitted (MAY-2007) 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; CP000698; ABQ26974.1; -; Genomic_DNA.
DR   RefSeq; WP_011939649.1; NC_009483.1.
DR   AlphaFoldDB; A5G5A6; -.
DR   STRING; 351605.Gura_2801; -.
DR   KEGG; gur:Gura_2801; -.
DR   HOGENOM; CLU_014689_7_0_7; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000006695; Chromosome.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
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; 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; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 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:UP000006695};
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          17..75
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        425
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         398
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   470 AA;  51956 MW;  561D19603D22D976 CRC64;
     MKNKSEKPKT LKSESDKLKI GQLLDLTINS LNEDGFGAAS YEGTPILVAG SLPGEIIRAK
     VTYVGRRETF ARMIKLVQRS PDRLPTAPCA KGLSCDGCPL IQMNYPAQLT WKKQLVGKFV
     RRYKTLEKAV LHDVIESPQQ LNYRNSAKLV ITGKFAEPII GIYRRNSHDV LDIGDCPLHH
     PLINKIITAV KAGIKKGKVP IYNPKSEMGL LRYLVIRVSE TANRAMVVFV TSERSYNEIH
     HLAKHLQAAV PEVTVIDQNI NGSSGNVIFG QKDHFVTKEH VLPAAIGGTR FHISPRSFFQ
     VNSGAARIIY EKVREWGALT GKERVLDLYC GIGGISLFLA GKAREVLGIE VVEAAVADAE
     MNAQLNNIRN CRFKAGDVAR LLGELREEGE KVDLVILNPP RKGCDEQVLR ETAAIGPQKI
     IYVSCSPQTL SHDLDILAAL GYRTTEIQPV DMFPQTPHVE DVALLVKMKS
//
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