ID A0A1Q7W2N4_9ACTN Unreviewed; 281 AA.
AC A0A1Q7W2N4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=16S/23S rRNA (Cytidine-2'-O)-methyltransferase {ECO:0000313|EMBL:OLE25023.1};
GN ORFNames=AUG49_11920 {ECO:0000313|EMBL:OLE25023.1};
OS Catenulispora sp. 13_1_20CM_3_70_7.
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=1805055 {ECO:0000313|EMBL:OLE25023.1, ECO:0000313|Proteomes:UP000186605};
RN [1] {ECO:0000313|EMBL:OLE25023.1, ECO:0000313|Proteomes:UP000186605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- SIMILARITY: Belongs to the TlyA family.
CC {ECO:0000256|ARBA:ARBA00029460}.
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:OLE25023.1}.
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DR EMBL; MNJN01000188; OLE25023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7W2N4; -.
DR Proteomes; UP000186605; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 Methyltransferase {ECO:0000313|EMBL:OLE25023.1};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000313|EMBL:OLE25023.1}.
FT DOMAIN 5..72
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
FT REGION 260..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 29421 MW; 8AE59F600F3221DA CRC64;
MTARRRLDAE LVRRNLARSR EQARELIEAG RVSVNGQTAS KAATQVETSA PVVVTEAKNG
EEYVSRGGHK LAGALAAFAP HGLSFEGRRA LDAGASTGGF TDVLLRNGAA HVVAVDVGYG
QLAWSLRTDD RVTVLDRTNV RDLTPDMIGG RVELVVGDLS FISLRLVLPA LASCAVPDAD
LALMVKPQFE VGKERLGSGG VVRDVALHAE AVRDVAAAAA KLGLGVRGVA ASPLPGPAGN
VEYFLWLRAD APPLREEDLA RAIQEGPAGP GETNHDEGSG D
//
