ID F4L6S0_HALH1 Unreviewed; 470 AA.
AC F4L6S0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:AEE50901.1};
GN OrderedLocusNames=Halhy_3038 {ECO:0000313|EMBL:AEE50901.1};
OS Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 / O).
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC Haliscomenobacter.
OX NCBI_TaxID=760192 {ECO:0000313|EMBL:AEE50901.1, ECO:0000313|Proteomes:UP000008461};
RN [1] {ECO:0000313|EMBL:AEE50901.1, ECO:0000313|Proteomes:UP000008461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O
RC {ECO:0000313|Proteomes:UP000008461};
RX PubMed=21886862; DOI=10.4056/sigs.1964579;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Daligault H., Lapidus A., Zeytun A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA Verbarg S., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of Haliscomenobacter hydrossis type strain (O).";
RL Stand. Genomic Sci. 4:352-360(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 1100;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I.,
RA Daligault H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Verbarg S., Frueling A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Haliscomenobacter hydrossis DSM 1100.";
RL Submitted (APR-2011) 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; CP002691; AEE50901.1; -; Genomic_DNA.
DR RefSeq; WP_013765444.1; NC_015510.1.
DR AlphaFoldDB; F4L6S0; -.
DR STRING; 760192.Halhy_3038; -.
DR GeneID; 78192856; -.
DR KEGG; hhy:Halhy_3038; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_7_2_10; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000008461; 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; 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:UP000008461};
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 3..63
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 426
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 426
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 399
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 470 AA; 52639 MW; 1409702F197CBD6F CRC64;
MARRKKNVIL SNVQFFGIAD EGKAVGKTED GQVVFAKGVV PGDSADVLVL KKRKGHIQGV
VRQINTFSSE RVEPVCSHFG TCGGCKWQNL DYAAQLRHKA VVVENALIRL GKISVGEWLP
ILAAESPYYY RNKMEFAFSC KQWLTHEEIN SEKSNAADVL GFHPAGGFDK VIDIQHCWLQ
PDPSNEVRNT VRTIAIAQGL SFYDVKKHEG FLRNLMLRIT TTGETMALIA FGEDNPDLRR
PFLEEVERRL PQITTLVYCI NTKMNDTIWD LPVHTWSGKG YAEEQLGHVR FRIGPKSFFQ
TNTRQGENLY DVVTRFANLQ GHENVYDLYT GIGSIGLYVA KDCKQVVGIE EVAAAIDDAK
INAEVNGVEN VKFYVGDVRA ILTTEFAAQH GKPDLLITDP PRAGMHEDVI NMLLELEAPR
IVYVSCNPGT QARDLGRLST KYQVLKVQPV DMFPHTHHIE SVALLELNKS
//
