ID W0DH70_9AQUI Unreviewed; 393 AA.
AC W0DH70;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=SAM-dependent methyltransferase {ECO:0000313|EMBL:AHE96592.1};
GN ORFNames=THERU_07775 {ECO:0000313|EMBL:AHE96592.1};
OS Thermocrinis ruber.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX NCBI_TaxID=75906 {ECO:0000313|Proteomes:UP000018914};
RN [1] {ECO:0000313|EMBL:AHE96592.1, ECO:0000313|Proteomes:UP000018914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23557 {ECO:0000313|EMBL:AHE96592.1,
RC ECO:0000313|Proteomes:UP000018914};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; CP007028; AHE96592.1; -; Genomic_DNA.
DR RefSeq; WP_025306669.1; NZ_CP007028.1.
DR AlphaFoldDB; W0DH70; -.
DR STRING; 75906.THERU_07775; -.
DR KEGG; trd:THERU_07775; -.
DR PATRIC; fig|75906.3.peg.1498; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_6_2_0; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000018914; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; 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; IPR003333; CMAS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43667; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR PANTHER; PTHR43667:SF1; CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE; 1.
DR Pfam; PF02353; CMAS; 1.
DR PIRSF; PIRSF003085; CMAS; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Methyltransferase {ECO:0000313|EMBL:AHE96592.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHE96592.1}.
FT BINDING 130..131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 165..173
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 191..196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
FT BINDING 220..221
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR003085-2"
SQ SEQUENCE 393 AA; 45920 MW; 0340785C22106511 CRC64;
MIENLVKDLA KFVEGGLSVE LYDGRVIGEG KCKVVVKDPK VIRDIIKDPE MGFGEHYMKG
NIQIIGDLEK FLRGCTKYLK DGGEKLRFMP LRSLLKILGL LKFVEEKEVQ RHYDLGNDFY
SLWLDSSMTY SCAFFKSPDC TLEEAQEEKR RIIYEKLQLS EGDRLLDIGC GWGSIILESA
KLYPITTVGI TLSKNQYEYV KERIKQEGLE GRVEVYLMHY EDLPKLGLKF NKVVSVGMFE
HVGKGRHRKF FEVVSKIMED GGLFLLHTIG KVHPSSQSRW IRKYIFPGGY LPSIEEVLRA
VRHLDFNLID IDDWRLHYYF TLKEWLRRFY SVGDYVKEKY GEEFFRMWEL YLVASAVSFY
NGSNHLFQFL FSKGVVNNYP VMRRSFLQPL LMA
//
