ID A0A0A2TTQ0_9BACL Unreviewed; 286 AA.
AC A0A0A2TTQ0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KGP79069.1};
GN ORFNames=P364_0125985 {ECO:0000313|EMBL:KGP79069.1};
OS Paenibacillus sp. MAEPY2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1395587 {ECO:0000313|EMBL:KGP79069.1, ECO:0000313|Proteomes:UP000030061};
RN [1] {ECO:0000313|EMBL:KGP79069.1, ECO:0000313|Proteomes:UP000030061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAEPY2 {ECO:0000313|EMBL:KGP79069.1,
RC ECO:0000313|Proteomes:UP000030061};
RX PubMed=24526641;
RA Chua P., Yoo H.S., Gan H.M., Lee S.M.;
RT "Draft Genome Sequences of Two Cellulolytic Paenibacillus sp. Strains,
RT MAEPY1 and MAEPY2, from Malaysian Landfill Leachate.";
RL Genome Announc. 2:0-0(2014).
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:KGP79069.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWUK01000037; KGP79069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2TTQ0; -.
DR eggNOG; COG2226; Bacteria.
DR Proteomes; UP000030061; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR041698; Methyltransf_25.
DR InterPro; IPR048647; RlmA_N.
DR InterPro; IPR016718; rRNA_m1G-MeTrfase_A_prd.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF13649; Methyltransf_25; 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 S-adenosyl-L-methionine {ECO:0000256|PIRSR:PIRSR018249-2};
KW Zinc {ECO:0000256|PIRSR:PIRSR018249-1}.
FT DOMAIN 19..54
FT /note="23S rRNA (guanine(745)-N(1))-methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF21302"
FT DOMAIN 104..184
FT /note="Methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13649"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-1"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
FT BINDING 111..112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR018249-2"
SQ SEQUENCE 286 AA; 32906 MW; 89CD75EAC76A9DD8 CRC64;
MQRRERSAAL IYRYIHMLTC PICHQTMTTV NPHSIQCSSK HTFDLARQGY VNFMTRFFKG
NYDKRLFTAK RNILSQTAIY TPLTEIIRHW IEGYSNSKSQ PLHILDAGAG EGSLLQQITQ
NTSSVGWGID IAKEGIATAS STYDQQVWFV GDLAHSPFAE GQLDVILNIL SPSNYEEFGR
VMKKDGWIIK VIPRKQYLME MREFLFRGRS HQLDGREHVL DRFTEHHYLI DSIPLTYTMP
VTKVMMDSLI HMTPLAWHGK ESAIASIQET LTQITIDLEI LVGKRR
//
