ID A0A401UI55_9CLOT Unreviewed; 391 AA.
AC A0A401UI55;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:GCD09237.1};
GN ORFNames=Ctaglu_08600 {ECO:0000313|EMBL:GCD09237.1};
OS Clostridium tagluense.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=360422 {ECO:0000313|EMBL:GCD09237.1, ECO:0000313|Proteomes:UP000287872};
RN [1] {ECO:0000313|EMBL:GCD09237.1, ECO:0000313|Proteomes:UP000287872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A121 {ECO:0000313|EMBL:GCD09237.1,
RC ECO:0000313|Proteomes:UP000287872};
RA Murakami T., Segawa T., Shcherbakova V.A., Mori H., Yoshimura Y.;
RT "Genome sequencing and assembly of Clostridium tagluense strain A121.";
RL Submitted (NOV-2018) 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}.
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:GCD09237.1}.
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DR EMBL; BHYK01000004; GCD09237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401UI55; -.
DR OrthoDB; 9805492at2; -.
DR Proteomes; UP000287872; 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:GCD09237.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000287872};
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:GCD09237.1}.
FT DOMAIN 3..88
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 391 AA; 44867 MW; 7C28F0901C927D71 CRC64;
MSCKFYLYRG KGRNAENGHL WIYANEIENV DGEYENGDIV EAYNFRGEFI GKGFINDVSK
IAIRIMTRDI NEQINEEFFR KRLRAAWTYR KTVIDTSSCR FLFGEADFVP GMIIDKYEDY
YVIQSLALGI DKYKDIIVKL LTDEYNAKGV YERSDARVRE LEGMDQTKGF LTEPFDTNLE
IIENGVKYHV DIENGQKTGF FLDQKENRAA IQRLCKDADV LDCFTHTGSF ALNAGIAGAK
SVLGVDISDY AVECSRKNAE LNGLSDIVKF ESHNAFDVLR EWSREGRQYD VVILDPPAFT
KSRSTIDGAT RGYKEINLRG IKLVKTGGYF VTCSCSHFMY PDLFRDTIAE AALDANRTLR
QVEFRTQAAD HPILWNSDES YYLKFYIFQV V
//
