ID D0SNG7_ACIJU Unreviewed; 272 AA.
AC D0SNG7;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Putative ribosomal RNA large subunit methyltransferase A {ECO:0000313|EMBL:EEY92481.1};
GN ORFNames=HMPREF0026_02027 {ECO:0000313|EMBL:EEY92481.1};
OS Acinetobacter junii SH205.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575587 {ECO:0000313|EMBL:EEY92481.1, ECO:0000313|Proteomes:UP000018442};
RN [1] {ECO:0000313|Proteomes:UP000018442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH205 {ECO:0000313|Proteomes:UP000018442};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
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DR EMBL; GG705012; EEY92481.1; -; Genomic_DNA.
DR RefSeq; WP_004964610.1; NZ_GG705012.1.
DR AlphaFoldDB; D0SNG7; -.
DR GeneID; 70091126; -.
DR HOGENOM; CLU_050931_0_0_6; -.
DR Proteomes; UP000018442; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR048647; RlmA_N.
DR InterPro; IPR016718; rRNA_m1G-MeTrfase_A_prd.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43460:SF1; METHYLTRANSF_11 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43460; METHYLTRANSFERASE; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF21302; RlmA_N; 1.
DR PIRSF; PIRSF018249; MyrA_prd; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR018249-1};
KW Methyltransferase {ECO:0000313|EMBL:EEY92481.1};
KW S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR018249-2};
KW Transferase {ECO:0000313|EMBL:EEY92481.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR018249-1}.
FT DOMAIN 5..47
FT /note="23S rRNA (guanine(745)-N(1))-methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF21302"
FT DOMAIN 88..172
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 68
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
FT BINDING 94..95
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
FT BINDING 179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
SQ SEQUENCE 272 AA; 30523 MW; 50838E4808761884 CRC64;
MSLLMCPVCR HSLDLVENSW RCENGHHYDV AKQGYVNLHV VQHKHSKSPG DTAESVLARR
EFLQKGFYAP LQNAVVELLQ TLQPSSILDI GCGEGYYTSA MQGCAKVCIG VDIAKTAVQR
AAKLNNKVTW VVGTGATLPV RDSVIDVCSS LFSPIPQSEI GRVLKPEGYL IVVTPAPKHL
FALREALFEQ VNLHEPQKFV DQLNDEFDLK QAQVIEASLR LEQQDLKNLI AMTPYAYKAN
PERRAQLEQQ NEFEVTAAFQ IYLFQKRKKP SN
//
