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Database: UniProt
Entry: K1ZFZ9_9BACT
LinkDB: K1ZFZ9_9BACT
Original site: K1ZFZ9_9BACT 
ID   K1ZFZ9_9BACT            Unreviewed;       451 AA.
AC   K1ZFZ9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=TRAM domain-containing protein {ECO:0000259|PROSITE:PS50926};
GN   ORFNames=ACD_65C00196G0005 {ECO:0000313|EMBL:EKD47961.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD47961.1};
RN   [1] {ECO:0000313|EMBL:EKD47961.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKD47961.1}.
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DR   EMBL; AMFJ01027301; EKD47961.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1ZFZ9; -.
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:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0001510; P:RNA methylation; IEA:GOC.
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; IPR025714; Methyltranfer_dom.
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; PF13847; Methyltransf_31; 1.
DR   Pfam; PF01938; TRAM; 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};
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..59
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        407
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        407
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         285
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         314
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         335
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         380
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   451 AA;  50758 MW;  05ABF77759026D12 CRC64;
     MTKGQILRVK INKLAFGGSG IGILEDGKKV FVEGVIPGDV VSARVRRSKK NYVEADLIEV
     VEPSPSRIKP KCKHFPLCGG CFWQMLPYEE QLKFKQEQVK EALKFTGGFK DTDTLVRPII
     GCKDPWFYRN KMEFSFGNSS KDDPDLRLGL HPRGKHIDVF DIEECFLQSE KVAKILARVR
     DFAKKNNLSF DKLSSLYVRD SKNTGEIMIN LVTCVDFPLQ KEFVEIFADM PEVVSIYWSL
     VTKKRGIKTQ IQEFLLAGKP TIREELTTED GTVLKFKISP QAFFQPNTRQ AEILYSEAIK
     AAGLTGAEVV FDLYCGTGTI GLFCAHKAKK IYGLEINESA IKNAKQNAIL NGIENSWFKA
     GDVDKNILEI PDTPDVVIVD PPRAGLGEKV VLKIVDFKPK VVVYVSCDPA NLARDLKIFE
     TQGYKVEYVQ PVDMFPHTYH IENVARVAIS M
//
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