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Y3134_GLOVI
ID   Y3134_GLOVI             Reviewed;         457 AA.
AC   Q7NGN4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Uncharacterized RNA methyltransferase gll3134;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=gll3134;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01024}.
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DR   EMBL; BA000045; BAC91075.1; -; Genomic_DNA.
DR   RefSeq; NP_926080.1; NC_005125.1.
DR   RefSeq; WP_011143127.1; NC_005125.1.
DR   AlphaFoldDB; Q7NGN4; -.
DR   SMR; Q7NGN4; -.
DR   STRING; 251221.35213705; -.
DR   EnsemblBacteria; BAC91075; BAC91075; BAC91075.
DR   KEGG; gvi:gll3134; -.
DR   PATRIC; fig|251221.4.peg.3164; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_3; -.
DR   InParanoid; Q7NGN4; -.
DR   OMA; FYAGDMK; -.
DR   OrthoDB; 1421660at2; -.
DR   PhylomeDB; Q7NGN4; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.150; -; 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   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF01938; TRAM; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 2.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53335; SSF53335; 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   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..457
FT                   /note="Uncharacterized RNA methyltransferase gll3134"
FT                   /id="PRO_0000161983"
FT   DOMAIN          10..69
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00208"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         82
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         323
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         344
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT   BINDING         387
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   457 AA;  49842 MW;  FE93142A37715A3A CRC64;
     MVGRPVEPGA LLQGQTVTVP ITALAAGGDG IARLTDGRVL FVAGAVPGDT VEARLVHLKK
     DHGFGKILQI VQASPHRIEA PCPVAERCGS CQWQWIDYPF QLEAKQRQVR EALEHLGGFA
     EPPVEPVIAQ PRPFGYRNKS TFPIGRDARG EPVIGYYQKD SHRIVPLDAC PVQDSRLDPL
     LAAARELIRT QGWSIYDEKH HRGALRHLGL RIGERTGQRL LTFVVNGQTL SGIKPAAQAL
     MDRFADLVGV CLNTHTERGN TIFGPQTRCL AGQDFIEEVL DGFRFRIEPT TFFQICTSQA
     EILARLVARG ADATAEQTVV DAYCGIGTLS LPLARAARAV VGIESHVRSV EQARQNARIN
     GIENCRFLAG TVEALLPDLR ADIVVVDPPR KGCDPEVLEA ILHAVPMRVV YVSCNPATLA
     RDLKRLVAGG YCLVGVQPVD LFAQTHHVEC VATLERS
 
 
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