ID A0A1E7KBK3_9ACTN Unreviewed; 438 AA.
AC A0A1E7KBK3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:OEV01322.1};
GN ORFNames=AN217_16495 {ECO:0000313|EMBL:OEV01322.1};
OS Streptomyces qinglanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=943816 {ECO:0000313|EMBL:OEV01322.1, ECO:0000313|Proteomes:UP000175829};
RN [1] {ECO:0000313|EMBL:OEV01322.1, ECO:0000313|Proteomes:UP000175829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO M10379 {ECO:0000313|EMBL:OEV01322.1,
RC ECO:0000313|Proteomes:UP000175829};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEV01322.1}.
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DR EMBL; LJGV01000022; OEV01322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7KBK3; -.
DR PATRIC; fig|943816.4.peg.2770; -.
DR Proteomes; UP000175829; Unassembled WGS sequence.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000175829};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 438 AA; 47653 MW; B4CF5FCEAF1D8D32 CRC64;
MQLVSRTGAA QRLAAVAEEF LGGALPFRLR AWDGSEAGPS GAPLVVLRSR TALRRLLWQP
GELGLADAYI SGDLEVVGDP ADALAALWQA ARARGLSRPR LTARQWAEAA ALLVRLGAVG
PPPRPPGRRA RQGGTLHSVA RDRSAISHHY DLSNDFYELL LDETMAYSCG YWRQPPGTEG
YGPAQSQYDK LDLICRKLAL RPGARLLDMG CGWGSLTVHA AEHFQAQVTA VTLSAEQARH
TRERVRARGL EDRVRVRHCH YRDLPDGGFD AAATVEMGEH VGADAYPHFA ARLRHALAPR
GRLLVQQMSR GADAPGGGPF IETYIAPDMH MRPLGETVAL LEEAGLEVRA ATSLREHYVH
TIDAWRDTLE AHWDAATALV GAPTARLWRL YLAGGRLAFA ERRMGVDQIL AVRPDEDGRS
GLGANPLGGH EGTWGTWS
//
