ID A0A1Q9URR8_9PSEU Unreviewed; 416 AA.
AC A0A1Q9URR8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Cyclopropane-fatty-acyl-phospholipid synthase {ECO:0000313|EMBL:OLT40339.1};
GN ORFNames=BJF85_25225 {ECO:0000313|EMBL:OLT40339.1};
OS Saccharomonospora sp. CUA-673.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=1904969 {ECO:0000313|EMBL:OLT40339.1, ECO:0000313|Proteomes:UP000186761};
RN [1] {ECO:0000313|EMBL:OLT40339.1, ECO:0000313|Proteomes:UP000186761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CUA-673 {ECO:0000313|EMBL:OLT40339.1,
RC ECO:0000313|Proteomes:UP000186761};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(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:OLT40339.1}.
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DR EMBL; MKKE01000061; OLT40339.1; -; Genomic_DNA.
DR RefSeq; WP_075849959.1; NZ_MKKE01000061.1.
DR AlphaFoldDB; A0A1Q9URR8; -.
DR STRING; 1904969.BJF85_25225; -.
DR Proteomes; UP000186761; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
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:SF2; TUBERCULOSTEARIC ACID METHYLTRANSFERASE UFAA1; 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:UP000186761};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 45958 MW; 9A955F8A426FD9B1 CRC64;
MGRPAPTSAP PPPWQRLDRP PHAPVRARLA ERLFRHAVRT LPVRVALAGG KRLGRGTAGS
PLMRIDRPGE FFHRLGLNGK IGFGESYMAG DWSSPDLAAL LTPFAARMAG LVPKPLQVLR
SSVDAPQPDA ERNTVSGARS NIHRHYDLSN DFFATFLDET MTYSGAPLTP GGDLHTAQLS
KLDSILDLAG VEAGTRLLEI GTGWGSLAIR AGQRGARVTT VTLSEQQRAL AVRRLAEAGL
SDRVDVRLAD YRDTEGTYDA VVSIEMIEAV GAEYWPTYFR TLDRLLVSGG RVALQAITMP
HDRLLATKNS YTWIHKYVFP GGLLPSVEVI ERNVAANTAM TLAERRAFGP GYAETLRQWG
QRFTERWVDG TDRGSDDPLN RMWEFYLAYS EAGFRSGYLD VWQFGMHKQP GDDRRG
//
