GenomeNet

Database: UniProt
Entry: F4KLW7_PORAD
LinkDB: F4KLW7_PORAD
Original site: F4KLW7_PORAD 
ID   F4KLW7_PORAD            Unreviewed;       493 AA.
AC   F4KLW7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:AEE12155.1};
GN   OrderedLocusNames=Poras_0201 {ECO:0000313|EMBL:AEE12155.1};
OS   Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC 10618 /
OS   JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides asaccharolyticus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE12155.1, ECO:0000313|Proteomes:UP000006545};
RN   [1] {ECO:0000313|Proteomes:UP000006545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC   {ECO:0000313|Proteomes:UP000006545};
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., Lu M.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002689; AEE12155.1; -; Genomic_DNA.
DR   RefSeq; WP_013759843.1; NC_015501.1.
DR   AlphaFoldDB; F4KLW7; -.
DR   STRING; 879243.Poras_0201; -.
DR   KEGG; pah:Poras_0201; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_2_10; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000006545; 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; 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.
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:UP000006545};
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          1..63
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        434
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         308
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         337
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         358
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         407
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   493 AA;  55856 MW;  5A18F37B45D11763 CRC64;
     MARGRKEPRY LDDVLIERMG AEGQCVAHVE DKVLFVPYAA PGDRCRIRVG RSKRSYMTGT
     IEELLEPSPL RVEPRCEVFG ACGGCKWQQL PYEEQLRGKA QQAADAMTRI GHIEIEETEP
     IVGCEDPWHY RNKVEFTFSK KRWLTEEELK SLPEEASEQE LCGVGFHKAG MFDKVLDLHG
     VTCQIADPIA SEIRDYLNDY CLARWEEYPY YDQRAHEGVM RTLLIRTTTL GGLMVLIAFA
     EGTEELRIQL LEALRMRFPQ ITSLYYMVNT KFNDSLADLP AQLYSGAPYI EEDMHGLRYR
     IGPKSFYQTN SRQAERLYEK VREYAQLTGD EVVYDLYTGA GTIANYLAQS CRSVIGIEYV
     PEAVEDAFVN RDQNGITNAT FYAGDMKAIL TDDFVAAHGR PDVLVTDPPR AGMDTPVVDV
     ILRAAPQRIV YVSCNPATQA RDLALLMAEG QYRAVRACAV DMFPHTHHVE TVALLSKLNT
     EHHLDIEIGE DED
//
DBGET integrated database retrieval system