ID B4WFR1_SYNS7 Unreviewed; 299 AA.
AC B4WFR1;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase superfamily {ECO:0000313|EMBL:EDX84671.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:EDX84671.1};
GN ORFNames=S7335_2368 {ECO:0000313|EMBL:EDX84671.1};
OS Synechococcus sp. (strain ATCC 29403 / PCC 7335).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=91464 {ECO:0000313|EMBL:EDX84671.1, ECO:0000313|Proteomes:UP000005766};
RN [1] {ECO:0000313|EMBL:EDX84671.1, ECO:0000313|Proteomes:UP000005766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29403 / PCC 7335 {ECO:0000313|Proteomes:UP000005766};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) 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}.
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DR EMBL; DS989904; EDX84671.1; -; Genomic_DNA.
DR RefSeq; WP_006454418.1; NZ_DS989904.1.
DR AlphaFoldDB; B4WFR1; -.
DR STRING; 91464.S7335_2368; -.
DR eggNOG; COG2226; Bacteria.
DR HOGENOM; CLU_039068_0_1_3; -.
DR OrthoDB; 9769602at2; -.
DR Proteomes; UP000005766; Unassembled WGS sequence.
DR GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IEA:UniProtKB-EC.
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:EDX84671.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005766};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00914};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU00914,
KW ECO:0000313|EMBL:EDX84671.1}.
FT DOMAIN 69..178
FT /note="Methyltransferase type 11"
FT /evidence="ECO:0000259|Pfam:PF08241"
FT REGION 68..77
FT /note="SAM motif I"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
FT REGION 143..151
FT /note="SAM motif II"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
FT REGION 170..179
FT /note="SAM motif III"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00914"
SQ SEQUENCE 299 AA; 33260 MW; A42D5C8D1B57A56A CRC64;
MTASTPLVEK IQRFYDASSP LWEKTWGEHM HHGYYGRNGR HRKNRRQAQI DLIEALIDWA
GLTTAHTILD VGCGIGGSTL YLAKKFDAQA VGITLSPVQA KRAGERAAEQ GIDLLAYENF
ETAQAPAVQF QVTDALATPF PDGAFDFVWS MESGEHMPDK QGFLQECYRV LKPGGTFLMA
TWCHRSTRTL AGSLTDSETQ HLDRLYELYH LPYVISLEDY GILARDVGFA GVRMADWSRQ
VEFFWQDVVR SALSVEAITG ILQAGEETIR GTAAIALMTT GFDRGLIRYG ILSGTKESL
//
