ID A0A1I0STG3_9SPHI Unreviewed; 394 AA.
AC A0A1I0STG3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=23S rRNA (Cytosine1962-C5)-methyltransferase {ECO:0000313|EMBL:SFA42789.1};
GN ORFNames=SAMN04488511_103153 {ECO:0000313|EMBL:SFA42789.1};
OS Pedobacter suwonensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=332999 {ECO:0000313|EMBL:SFA42789.1, ECO:0000313|Proteomes:UP000198836};
RN [1] {ECO:0000313|Proteomes:UP000198836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18130 {ECO:0000313|Proteomes:UP000198836};
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; FOJM01000003; SFA42789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0STG3; -.
DR STRING; 332999.SAMN04488511_103153; -.
DR OrthoDB; 9805492at2; -.
DR Proteomes; UP000198836; 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:SFA42789.1}; 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:SFA42789.1}.
FT DOMAIN 2..87
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 394 AA; 43825 MW; 22810C364BDBB23A CRC64;
MVEIILKKGK EKAALQRHPW VFSGALEKVK GKPEDGDVVK VFAFDHEFLA YGYFNSNSRV
AVRLLEWDET QTIDHSWYQN RLKQAIASRQ FILNEQTDTC RLVFSEADFL PGLIVDQYAD
FLSLQILSSG IEKVKAEIVE ILKTELNPKG IFDKSDATAR NHEGLPVENG LLWGENPPEF
LAVKENGIIY HINIAEGQKS GFYCDQRDNR HILASYTKGK KVLDCFSYSG GFSLNSLANG
AAGVTSVDSS GLAIETLKQN VALNQFDGKT VTAIQSDVNK QLRAFKEAGK LFDVVVLDPP
KYAPSRSALD RAARAYKDLN RLGMLMLEKG GLLATFSCSG AVDIETFKQI IAWAALDAGK
EVQIIKQFCQ PEDHPVRISF PEGEYLKGLL LRVL
//
