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Database: UniProt
Entry: A0A1Y5S616_9RHOB
LinkDB: A0A1Y5S616_9RHOB
Original site: A0A1Y5S616_9RHOB 
ID   A0A1Y5S616_9RHOB        Unreviewed;       449 AA.
AC   A0A1Y5S616;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:SLN30560.1};
DE            EC=2.1.1.79 {ECO:0000313|EMBL:SLN30560.1};
GN   Name=cfa_2 {ECO:0000313|EMBL:SLN30560.1};
GN   ORFNames=PEL8287_01430 {ECO:0000313|EMBL:SLN30560.1};
OS   Roseovarius litorisediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN30560.1, ECO:0000313|Proteomes:UP000193827};
RN   [1] {ECO:0000313|EMBL:SLN30560.1, ECO:0000313|Proteomes:UP000193827}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN30560.1,
RC   ECO:0000313|Proteomes:UP000193827};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) 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; FWFL01000003; SLN30560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5S616; -.
DR   Proteomes; UP000193827; Unassembled WGS sequence.
DR   GO; GO:0008825; F:cyclopropane-fatty-acyl-phospholipid synthase activity; IEA:UniProtKB-EC.
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:SLN30560.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193827};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SLN30560.1}.
FT   REGION          402..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..441
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   449 AA;  50872 MW;  BA8836C241E8BCF4 CRC64;
     MTGVWQHALD RMLRSLIKLG SLRVVMPSGG IRDYGETSCA PVKVRLLDPA TVRRLVLNPE
     LAFGEAYMNR SLEIDGDELQ GLLAIVVRNA RHAEANPVWW QKLSEKARGA LRGLAQNNIV
     TRARRNVAHH YDLSGKLFDL FLDDDRQYSC GYFRTPDATL EQAQADKKAH IARKLLIRPG
     MSVLDIGCGW GGMALTLARD HGAKVVGITL SEEQHAYATE RVAHAGLSDR IEFRLCDYRQ
     VEGTFDRVVS VGMFEHVGLP HYLDYFATIR KRLSPDGVAL VHTIGWAGTA KATNPWIAKY
     IFPGGYIPAV SEVMTAVEQN RLWATDIECW RLHYAYTLRH WYDRFRAHED EARVLYDDRF
     ARMWRFYLAA SEQTFRHAPQ AVFQIQLSPN VDAVPLTRDY QYDTGQTAPR PQPDASRKPV
     LVAHSGRTAS RNKTSHPHAV SLEKQNNDR
//
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