ID A0A3E2YTT4_9ACTN Unreviewed; 447 AA.
AC A0A3E2YTT4;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:RGC69736.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:RGC69736.1};
GN Name=cfa {ECO:0000313|EMBL:RGC69736.1};
GN ORFNames=C5N14_04860 {ECO:0000313|EMBL:RGC69736.1};
OS Micromonospora sp. MW-13.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2094022 {ECO:0000313|EMBL:RGC69736.1, ECO:0000313|Proteomes:UP000258607};
RN [1] {ECO:0000313|EMBL:RGC69736.1, ECO:0000313|Proteomes:UP000258607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW13 {ECO:0000313|EMBL:RGC69736.1,
RC ECO:0000313|Proteomes:UP000258607};
RA Jahanshah G., Miess H., Busche T., Ruckert C., Kalinowski J.,
RA Rokni-Zadeh H., Gross H.;
RT "Draft Genome Sequence of Micromonospora sp. MW-13, a Bacterical Strain
RT Isolated from the Rhizosphere of Wheat in Iran with antibacterial and
RT possibly plant growth promotion properties.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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:RGC69736.1}.
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DR EMBL; QKKX01000009; RGC69736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2YTT4; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000258607; 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:RGC69736.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000258607};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RGC69736.1}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 447 AA; 48581 MW; B137A49C5182A6E6 CRC64;
MSLTDREQGA ASVPSTPPTG GLRPAPTVAD VIRAVTAGPL PVRITGYDGS AVGPADAGIT
LSIRSQRGLS YLLTAPGDLG MARAYVSGDL ALSGVHLGDP YEALRVLKDE LRIRPPALAD
GLALVRGLGW ERLMPPPPPP QEAAPRWKRV VNGLRHSRSR DSTAISHHYD VSNAFYEKVL
GPSMTYTCAV FRDPDDTLEQ AQAAKYDLVA GKLALKPGMR LLDVGCGWGG MVRHAAREYG
VKALGVTLSR AQAQWAQAAI EREGLTDLAE VRHLDYRDAP REQFDAVSSI GLTEHIGVRN
YPVYFGALRD RLRPGGRLLN HCITRADNRA PHRSGAFIDR YVFPDGELAG PGRLIGEIHD
AGLEVHHEEN LRQHYALTLA GWCRNLVANW DECVAEVGEG TARVWGLYMA GSRLAFERNE
IQLHQVLATR NGPAGVNGYP LRPDWTA
//
