ID Q0RHH6_FRAAA Unreviewed; 464 AA.
AC Q0RHH6;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 28-JAN-2026, entry version 97.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:CAJ63051.1};
DE EC=2.1.1.79 {ECO:0000313|EMBL:CAJ63051.1};
GN Name=cfa {ECO:0000313|EMBL:CAJ63051.1};
GN OrderedLocusNames=FRAAL4409 {ECO:0000313|EMBL:CAJ63051.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
OC Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ63051.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ63051.1, ECO:0000313|Proteomes:UP000000657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45986 / CECT 9034 / ACN14a
RC {ECO:0000313|Proteomes:UP000000657};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
CC -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC {ECO:0000256|ARBA:ARBA00010815}.
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DR EMBL; CT573213; CAJ63051.1; -; Genomic_DNA.
DR RefSeq; WP_011605532.1; NC_008278.1.
DR AlphaFoldDB; Q0RHH6; -.
DR STRING; 326424.FRAAL4409; -.
DR KEGG; fal:FRAAL4409; -.
DR eggNOG; COG2230; Bacteria.
DR HOGENOM; CLU_026434_6_2_11; -.
DR OrthoDB; 9782855at2; -.
DR Proteomes; UP000000657; Chromosome.
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; IPR050723; CFA/CMAS.
DR InterPro; IPR003333; CMAS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_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.
DR SUPFAM; SSF55718; SCP-like; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CAJ63051.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ63051.1}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 50654 MW; AB745287094841F9 CRC64;
MTISRELEEH EPAAPTTHAP DPRWSPELAR ATRTLLETFI GTAPPVRVVL WDGSALGPDT
PTQVVVRSPQ AMHRALFRPG ELGFARAFVA GDLDVEGDIF AALELRNHLS ALPRRPTPAT
ASALLTLLRE LGARPPAPPP EEARLHGRRH SRHRDAAAIS HHYDVSNAFY RVFLGPTMTY
SCGVWESPAG GLDAAQTAKH ELVCRKLGLR PGERLLDVGC GWGSMLIHAA RHHGVRGVGV
TISVEQAAEA RRRIAEAGLT DAVEIRLQDY REIPDGPFDA ISSVGMVEHV GRAMLPTYFA
SLYGLLRPGG RLLNHGISSP GDPAGAYRYQ PHLGPIPLPK GRDFLRRYVF PDGELHEIGL
MTSLTQAAGF EVRHVENLRE HYGLTLRAWV RALEENWDAA VAQVGAGRAR VWRLYMAGSA
LSFEAGQTQI HQTLAVRPDA GRSGQPLRPR YDSPAPLPTQ PTTG
//
