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Database: UniProt
Entry: B8HSY6_CYAP4
LinkDB: B8HSY6_CYAP4
Original site: B8HSY6_CYAP4 
ID   B8HSY6_CYAP4            Unreviewed;       457 AA.
AC   B8HSY6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:ACL42783.1};
GN   OrderedLocusNames=Cyan7425_0391 {ECO:0000313|EMBL:ACL42783.1};
OS   Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC   Cyanothece.
OX   NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL42783.1};
RN   [1] {ECO:0000313|EMBL:ACL42783.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL42783.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L.,
RA   Sato H., Zhao L., Sherman L., Pakrasi H., Richardson P.;
RT   "Complete sequence of chromosome Cyanothece sp. PCC 7425.";
RL   Submitted (JAN-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; CP001344; ACL42783.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8HSY6; -.
DR   STRING; 395961.Cyan7425_0391; -.
DR   KEGG; cyn:Cyan7425_0391; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_3; -.
DR   OMA; FYAGDMK; -.
DR   OrthoDB; 9804590at2; -.
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:0001510; P:RNA methylation; IEA:GOC.
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: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.
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          8..66
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        412
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        412
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         290
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         319
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         340
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         385
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   457 AA;  51085 MW;  069636E7A81E8B88 CRC64;
     MIASDRQGLV QGQVIEITIA SLSATGDGVG RYGEQVIFVP DTVPGDRVAV RLLQVKPRYA
     HAQIETLLIP SPDRVRPPCI VADKCGGCQW QPVSYAQQLA AKQAQVSEAL ERIGKFKHPP
     VAPILAAPSP LAYRNKVTYP LRQVNHRVQA GYYRKGSHRL VNLNQCPVQD DRLNPLLADV
     KQDLQQRGWP IYDEHTHRGL LRHLSLRVGR RTGEILLTLV TTDWQLPDFK AQAEEWLQRY
     PALVGVCLNR NPDRTNAIFG CETRCIAGRP VLTEQFAGLE FEIGSETFFQ VYTEQAERLV
     QILLERLQLQ GTERIVDAYC GIGTLSLPIA RQAQQVIGLE IHPATVAQAK QNAIRNGLTN
     VSFYAGPVEQ QLPQLDLLPD IVVLDPPRKG CDRSVVEHLS QLRPPRIVYM SCNPATLARD
     LHLLCQANPY ELEQIQPADF FPQTAHVETL AFLRLAT
//
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