ID A0A0P8DLJ9_9CYAN Unreviewed; 336 AA.
AC A0A0P8DLJ9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=2-methyl-6-solanesyl-1,4-benzoquinol methyltransferase {ECO:0000313|EMBL:KPQ37796.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:KPQ37796.1};
GN ORFNames=HLUCCA11_01685 {ECO:0000313|EMBL:KPQ37796.1};
OS Phormidesmis priestleyi Ana.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Phormidesmis.
OX NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ37796.1, ECO:0000313|Proteomes:UP000050465};
RN [1] {ECO:0000313|EMBL:KPQ37796.1, ECO:0000313|Proteomes:UP000050465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ana {ECO:0000313|EMBL:KPQ37796.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. gTMT family. {ECO:0000256|PROSITE-ProRule:PRU00914}.
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:KPQ37796.1}.
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DR EMBL; LJZR01000001; KPQ37796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8DLJ9; -.
DR STRING; 1666911.HLUCCA11_01685; -.
DR PATRIC; fig|1666911.3.peg.2749; -.
DR Proteomes; UP000050465; Unassembled WGS sequence.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR025774; MTs_g-TMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR44068:SF11; GERANYL DIPHOSPHATE 2-C-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR44068; ZGC:194242; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51581; SAM_GTMT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00914,
KW ECO:0000313|EMBL:KPQ37796.1};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00914};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00914,
KW ECO:0000313|EMBL:KPQ37796.1}.
FT DOMAIN 97..192
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
FT REGION 96..105
FT /note="SAM motif I"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
FT REGION 156..164
FT /note="SAM motif II"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
FT REGION 183..192
FT /note="SAM motif III"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
FT REGION 317..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 336 AA; 36896 MW; ED2798A6ECDCD553 CRC64;
MNLLLLGFGL FLLLLLLSLA IYLLTARKYE SASSVAQSYD SWTQDGILEF YWGEHIHLGH
YGSPPRRKNF KKAKHDFVHE MVRWGGLDAL APGTTVLDVG CGIGGSSRIL ARDYNFAVTG
ITISPQQVQR AQALTPANVN AQFKVDDALN LSFPDASFDV VWSIEAGPHM PDKARYAQEM
LRVLKPGGIL VVADWNQRDD RHNPLNSWER LVMQQLLDQW AHPAFASIEG FAEELAATGL
VAGGVTTADW TQQTLPSWID SIWQGIVRPA GLVKFGSVGF IKSLREVPTL LLMRLAFGAG
LCRFGMFRAV RAASPSPITS DAASDQNSDN IKTATI
//
