ID   Q47NA2_THEFY            Unreviewed;       266 AA.
AC   Q47NA2;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   SubName: Full=Hemolysin A {ECO:0000313|EMBL:AAZ56067.1};
GN   OrderedLocusNames=Tfu_2034 {ECO:0000313|EMBL:AAZ56067.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ56067.1};
RN   [1] {ECO:0000313|EMBL:AAZ56067.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ56067.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Thermobifida fusca YX.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TlyA family.
CC       {ECO:0000256|ARBA:ARBA00029460}.
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DR   EMBL; CP000088; AAZ56067.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47NA2; -.
DR   STRING; 269800.Tfu_2034; -.
DR   KEGG; tfu:Tfu_2034; -.
DR   eggNOG; COG1189; Bacteria.
DR   HOGENOM; CLU_058015_1_0_11; -.
DR   OrthoDB; 9784736at2; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd00165; S4; 1.
DR   Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR004538; Hemolysin_A/TlyA.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR002942; S4_RNA-bd.
DR   InterPro; IPR036986; S4_RNA-bd_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR047048; TlyA.
DR   NCBIfam; TIGR00478; tly; 1.
DR   PANTHER; PTHR32319; BACTERIAL HEMOLYSIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR32319:SF0; BACTERIAL HEMOLYSIN-LIKE PROTEIN; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF01479; S4; 1.
DR   PIRSF; PIRSF005578; TlyA; 1.
DR   SMART; SM00363; S4; 1.
DR   SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS50889; S4; 1.
PE   3: Inferred from homology;
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT   DOMAIN          5..72
FT                   /note="RNA-binding S4"
FT                   /evidence="ECO:0000259|SMART:SM00363"
SQ   SEQUENCE   266 AA;  28212 MW;  C436D717A5CA45F1 CRC64;
     MARRSRLDAE LVRRGHARSR AHAAELIAAG RVRVAGTLAT KAATQVGVDQ AIVVEQADDE
     PVYVSRGAYK LIGALDAFAV DVTGRRCLDA GASTGGFTDV LLRRGAAHVV AVDVGYGQLA
     WSLRSDPRVT VLERQNVREL TPDQVGEPRP DLVVADLSFI SLRLVLAPLL ACAASDADFV
     LLVKPQFEVG RERVGAKGVV RDPEARASAV RDVAAHAWTL GLGVCGVTAS PLPGPSGNVE
     YFLWLRSGAA PLDERQLERA VAEGPQ
//