ID A0A1H6KC59_9BACT Unreviewed; 430 AA.
AC A0A1H6KC59;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=S-adenosyl-l-methionine-dependent methyltransferase {ECO:0000313|EMBL:SEH69362.1};
GN ORFNames=PYTT_0028 {ECO:0000313|EMBL:SEH69362.1};
OS Akkermansia glycaniphila.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=1679444 {ECO:0000313|EMBL:SEH69362.1, ECO:0000313|Proteomes:UP000176204};
RN [1] {ECO:0000313|Proteomes:UP000176204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Koehorst J.;
RL Submitted (SEP-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; LT629973; SEH69362.1; -; Genomic_DNA.
DR RefSeq; WP_067772968.1; NZ_LT629973.1.
DR AlphaFoldDB; A0A1H6KC59; -.
DR STRING; 1679444.PYTT_0028; -.
DR KEGG; agl:PYTT_0028; -.
DR OrthoDB; 9805492at2; -.
DR Proteomes; UP000176204; Chromosome i.
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:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 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; 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 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:SEH69362.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000176204};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SEH69362.1}.
FT DOMAIN 54..103
FT /note="RlmI-like PUA"
FT /evidence="ECO:0000259|Pfam:PF17785"
FT DOMAIN 217..382
FT /note="S-adenosylmethionine-dependent methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF10672"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 48595 MW; 1919C818D0FD6FDB CRC64;
MREFHKPRYQ DRPFRPKPSG NRPVQPVSRM RREDAPEGSE EWTAPWVQLK YFSYNPAIFP
RMLGAVSPDA RDGQLINVYD KNGELFGGGF WNEKSRTPLR VLAHGRDVLT EKALDDAIRK
AVAWRRDVCR LDEVTNAYRV LHGDSDGIGG LIVDRYNDVL SLEVSTLGAW LRLDRWLPLL
HELCGTSRHV VQVDESIARM EGIDTRQAPS SDPVRLVRIH ENGVQFEVDF AQGHKTGFFC
DQRDNRLKLS QLVQGKTVLD LCCYSGGFSI LAKKLGGAAE VTAVDLDEKA IAMAKRNANI
NGQQRIDFVH ADAFVYARQM VRNGRLFDVV LLDPPKFVQG RDEAYEEGIK KYHDLNMLGL
QCVRPGGLFV TCSCSGLVSP GEFEKTVIKA AQRLGRRLQI VQMSGPGWDH PFLSTYPEGR
YLKVLWARVL
//
