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Database: UniProt
Entry: A0A0U3PPQ3_9ACTN
LinkDB: A0A0U3PPQ3_9ACTN
Original site: A0A0U3PPQ3_9ACTN 
ID   A0A0U3PPQ3_9ACTN        Unreviewed;       438 AA.
AC   A0A0U3PPQ3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:ALV33669.1};
GN   ORFNames=AS200_17695 {ECO:0000313|EMBL:ALV33669.1};
OS   Streptomyces sp. CdTB01.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV33669.1, ECO:0000313|Proteomes:UP000068029};
RN   [1] {ECO:0000313|EMBL:ALV33669.1, ECO:0000313|Proteomes:UP000068029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CdTB01 {ECO:0000313|EMBL:ALV33669.1,
RC   ECO:0000313|Proteomes:UP000068029};
RA   Tian Y., Zhou G., Yang H., Lu X.;
RT   "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT   bacterium tolerant to cadmium.";
RL   Submitted (DEC-2015) 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; CP013743; ALV33669.1; -; Genomic_DNA.
DR   RefSeq; WP_058923327.1; NZ_CP013743.1.
DR   AlphaFoldDB; A0A0U3PPQ3; -.
DR   STRING; 1725411.AS200_17695; -.
DR   KEGG; scx:AS200_17695; -.
DR   OrthoDB; 9782855at2; -.
DR   Proteomes; UP000068029; 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; IPR020803; PKS_MeTfrase.
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   SMART; SM00828; PKS_MT; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068029};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          177..400
FT                   /note="Polyketide synthase methyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00828"
FT   REGION          418..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   438 AA;  47355 MW;  5E08C801B2F66A1D CRC64;
     MTTTPSTATR PGAAHRLAAL AGDVLGGPLP VRLRAWDGSE TGPAGAPVVV LRSRRALRRL
     LWQPGELGLA QAYVTGEVDI EGDLAEGLRT MWAAARERGP RPPRLTPADR ARALATAVRL
     GVVGPPPPAP ASQARLRGGL HSRARDRAAI SHHYDLSNDF YALLLDETMA YSCGYWASEK
     PGFTAADAQR AKLELICRKL GLVPGARLLD IGCGWGSLTL HAAERHGAQV TAVTLAREQA
     AYVRERVRER GLSERVQVVC QDYRDIEGGA YDAVATVEMG EHVGDAEYPA FAASLHRLVR
     PAGRVLVQQM SRGPGAPGGG PFIEAYIAPD MHMRPLGETV ALLEEAGLEV RHTESLREHY
     ARSVGAWHRT LEERWEAFVR LVGEETARVW RLYLVGAALA FEEGRMGVDQ ILSVRPAPGG
     DSGLPATTHG WYEGLEKP
//
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