ID A0A420HZL9_9PEZI Unreviewed; 772 AA.
AC A0A420HZL9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Putative acyltransferase {ECO:0000313|EMBL:RKF62870.1};
GN ORFNames=OnM2_029076 {ECO:0000313|EMBL:RKF62870.1};
OS Erysiphe neolycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF62870.1, ECO:0000313|Proteomes:UP000286134};
RN [1] {ECO:0000313|EMBL:RKF62870.1, ECO:0000313|Proteomes:UP000286134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG2 {ECO:0000313|EMBL:RKF62870.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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:RKF62870.1}.
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DR EMBL; MCFK01002990; RKF62870.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420HZL9; -.
DR STRING; 212602.A0A420HZL9; -.
DR Proteomes; UP000286134; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07992; LPLAT_AAK14816-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR31605; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR PANTHER; PTHR31605:SF0; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR Pfam; PF01553; Acyltransferase; 2.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 2.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:RKF62870.1};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000286134};
KW Transferase {ECO:0000313|EMBL:RKF62870.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 495..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 530..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..297
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 681..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 572..599
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 772 AA; 86850 MW; 5CF7B655D107400C CRC64;
MADNYGTQEQ MPAFKSRHLE KNPMTNWIYD FFLWIFSITI DLFFREIHPR GSWKVPRKGP
IILVAAPHAN QFVDPLILMK TLRNDCRRRA SFLIAAKSMD KWLIGWFARK VGAMPVARAL
DMVRPADGTI YMPKPDDDPL LIRGFGTKFG TKQANVGDLL VLPAVHGIAA NAEIAEIISL
EEIRLKKPFR DRASVIQLTP PKDLNEPGVE NLSNSSETVF RGSPFKIAPK VDQTKVYDAV
FDRLRSGGAV GIFPEGGSHD RTELLPLKAG VAIMALGALA ADPNSDLKII PCGLNYFHAH
KFRSRAVVEF GNPIDIPKEL VNLYRNGERR EAVGKLLETV YQSLVAVTVT SPDYDTLMLI
QAARRLYNPT SRHLPLPMVV ELNRKLVKGY TYYKNDPRVV SLQKAVTNYN KQLRYLNIKD
HQVEYAKHSI PKIIPLLLYR LGKISVLSIG VLPGLVLFSP VFAASKVISI KKSREALASS
TVKLQGRDVV ATWKLLVALI FAPILYNVYT FMLTYWTYRN RIQGYVPQWV PLKAVVIFGY
IIFPAITFAA LRFGEVGMDV VKSLRPLLLS LYPASSNNIR KLKERREKLS AQVTNVINTL
GPEIFPDFDA SRIVADPFVS EGSNPVTPTR LEFHRRGSDH SSISEMEWPG FYKISTDYVM
NRMNGNLPRS ESLSNLGNIS LFATRPPSRS RSRSSSRGEA TGCETFPLQS LSTLDSASGL
EVVSSKIRDA MRERRLQRRK TIESARSEDG RDEHYESSEK EISLDKDEAT YT
//
