ID A0A1G5BF92_9FIRM Unreviewed; 431 AA.
AC A0A1G5BF92;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=23S rRNA (Cytosine1962-C5)-methyltransferase {ECO:0000313|EMBL:SCX88808.1};
GN ORFNames=SAMN02910371_00283 {ECO:0000313|EMBL:SCX88808.1};
OS Butyrivibrio sp. INlla14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520808 {ECO:0000313|EMBL:SCX88808.1, ECO:0000313|Proteomes:UP000199551};
RN [1] {ECO:0000313|Proteomes:UP000199551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INlla14 {ECO:0000313|Proteomes:UP000199551};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmI family.
CC {ECO:0000256|ARBA:ARBA00038091}.
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DR EMBL; FMVS01000003; SCX88808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5BF92; -.
DR OrthoDB; 9805492at2; -.
DR Proteomes; UP000199551; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd21153; PUA_RlmI; 1.
DR CDD; cd11572; RlmI_M_like; 1.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR Gene3D; 3.30.750.80; RNA methyltransferase domain (HRMD) like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR041532; RlmI-like_PUA.
DR InterPro; IPR019614; SAM-dep_methyl-trfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42873:SF1; METHYLTRANS_SAM DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42873; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE; 1.
DR Pfam; PF10672; Methyltrans_SAM; 1.
DR Pfam; PF17785; PUA_3; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:SCX88808.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199551};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SCX88808.1}.
FT DOMAIN 9..94
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 431 AA; 48225 MW; BCD79B617470E152 CRC64;
MGKIKTANAA AIIRKREGRE FKAGGAWIYD NEVDRVEGSF ENGDIIEVHD FDGYFLGYGF
INEKSKIRIR MMSRKKENPV DEALLEKRIK RAWEYRKAVM ASYIDEYLLD GDKEAAKDKE
KYAKALSKLS TRFIFGEADF IPGITIDKFS DVLVIESLAL GTDRMKGIIL DICKKVLAED
GVNIRGIYER SDAKVRELEG LERTKGFIGQ EFDTKVLIEE NGVKYYVDVE NGQKTGFFLD
QKFNRQSIRG LCKGKKVLDC FTHTGSFALN AAAGGASSVL GVDASDLGCK QAEENAALNG
LEKIASFQCA DVFELLPDLE KKGEKFDVVI LDPPAFTKSR ASIKKAATGY KEINMRGMKL
VKDGGYLATC SCSHFMDEEL FLKTIADAAR DAHKRLTQVE FRQQAADHPI LWGGAASYYL
KFVIFQVTDE I
//
