ID A0A1Q7R8S8_9BACT Unreviewed; 208 AA.
AC A0A1Q7R8S8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Methyltransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=AUI33_15665 {ECO:0000313|EMBL:OLD60406.1};
OS Ignavibacteria bacterium 13_1_40CM_2_61_4.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1805219 {ECO:0000313|EMBL:OLD60406.1, ECO:0000313|Proteomes:UP000186155};
RN [1] {ECO:0000313|EMBL:OLD60406.1, ECO:0000313|Proteomes:UP000186155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLD60406.1}.
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; MNHF01001636; OLD60406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7R8S8; -.
DR Proteomes; UP000186155; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1901663; P:quinone biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004033; UbiE/COQ5_MeTrFase.
DR InterPro; IPR023576; UbiE/COQ5_MeTrFase_CS.
DR PANTHER; PTHR42912; METHYLTRANSFERASE; 1.
DR PANTHER; PTHR42912:SF107; METHYLTRANSFERASE-LIKE PROTEIN 7A-RELATED; 1.
DR Pfam; PF01209; Ubie_methyltran; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51608; SAM_MT_UBIE; 1.
DR PROSITE; PS01184; UBIE_2; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 208
FT /evidence="ECO:0000313|EMBL:OLD60406.1"
SQ SEQUENCE 208 AA; 23664 MW; E9060AE5B2E1880A CRC64;
METSQRHRGE ASRTVQDRLP ERLPPHPPLA RYYADEQERQ RQVSRWFDES AARYDFITQA
MSFGSGNRYR QQALLQAGLA EGMSLLDIAC GTGVLAAHAQ SIVGVRGFVV GLDPSPGMLR
EARGRGVLKL VRGVAESLPL ESERFDLLSM GYALRHVSDL RATFGEYRRV LRPGGKVLIL
EISRPRYRFM FRLLKLYLGR MVPWFARL
//
