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Database: UniProt
Entry: D2R616_PIRSD
LinkDB: D2R616_PIRSD
Original site: D2R616_PIRSD 
ID   D2R616_PIRSD            Unreviewed;       377 AA.
AC   D2R616;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:ADB19101.1};
GN   OrderedLocusNames=Psta_4457 {ECO:0000313|EMBL:ADB19101.1};
OS   Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS   staleyi).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Pirellula.
OX   NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB19101.1, ECO:0000313|Proteomes:UP000001887};
RN   [1] {ECO:0000313|EMBL:ADB19101.1, ECO:0000313|Proteomes:UP000001887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC   {ECO:0000313|Proteomes:UP000001887};
RX   PubMed=21304671; DOI=10.4056/sigs.51657;
RA   Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA   Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL   Stand. Genomic Sci. 1:308-316(2009).
CC   -!- SIMILARITY: Belongs to the CFA/CMAS family.
CC       {ECO:0000256|ARBA:ARBA00010815}.
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DR   EMBL; CP001848; ADB19101.1; -; Genomic_DNA.
DR   RefSeq; WP_012913360.1; NC_013720.1.
DR   AlphaFoldDB; D2R616; -.
DR   STRING; 530564.Psta_4457; -.
DR   KEGG; psl:Psta_4457; -.
DR   eggNOG; COG2230; Bacteria.
DR   HOGENOM; CLU_026434_6_0_0; -.
DR   OrthoDB; 9782855at2; -.
DR   Proteomes; UP000001887; 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; 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:UP000001887};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   377 AA;  42948 MW;  3650149922B810AE CRC64;
     MASSLKSAVA RSLADADIII GGSRAWDITV HDTRMYTALA TSGSLGAGES YMNGWWDCDA
     LDQMAERYLR SISTSKIAGG RFYGLLERIR AKYIDLQVGL GGREIARVHY DLPSDLFESM
     LGPTMNYSCG YWREANDLTT AQNAKMHLIC RKLGLRPGMR VLDVGCGWGG LIQFVVREYS
     CSVVGITVSA EQARYASKKC NASSSEVYLL DYRDLRPETH GTFDAITSVG MLEHVGPRNY
     ARYFDIMRRL LKPSGLLLVQ SFGRERSEPV DRWINRYIFP NSYVPNGTEL LTATRGRFIV
     EDWHNFGADY DRTLLAWHTN FENWAIDKWK VTAPKRYRMW RYYLLTFAAG FRVRDRVQLW
     QIVLSPEGVP KGYVSLR
//
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