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Database: UniProt
Entry: A0A024UNF8_9STRA
LinkDB: A0A024UNF8_9STRA
Original site: A0A024UNF8_9STRA 
ID   A0A024UNF8_9STRA        Unreviewed;      1192 AA.
AC   A0A024UNF8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   08-NOV-2023, entry version 41.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=H310_01792 {ECO:0000313|EMBL:ETW07168.1};
OS   Aphanomyces invadans.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Aphanomyces.
OX   NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW07168.1};
RN   [1] {ECO:0000313|EMBL:ETW07168.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJM9701 {ECO:0000313|EMBL:ETW07168.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC       {ECO:0000256|ARBA:ARBA00007937}.
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DR   EMBL; KI913954; ETW07168.1; -; Genomic_DNA.
DR   EMBL; KI913954; ETW07169.1; -; Genomic_DNA.
DR   RefSeq; XP_008863262.1; XM_008865040.1.
DR   RefSeq; XP_008863263.1; XM_008865041.1.
DR   AlphaFoldDB; A0A024UNF8; -.
DR   EnsemblFungi; H310_01792-t26_1; H310_01792-t26_1-p1; H310_01792.
DR   EnsemblFungi; H310_01792-t26_2; H310_01792-t26_2-p1; H310_01792.
DR   EnsemblProtists; ETW07168; ETW07168; H310_01792.
DR   EnsemblProtists; ETW07169; ETW07169; H310_01792.
DR   GeneID; 20078842; -.
DR   VEuPathDB; FungiDB:H310_01792; -.
DR   OrthoDB; 1434498at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IEA:InterPro.
DR   CDD; cd05236; FAR-N_SDR_e; 1.
DR   CDD; cd09071; FAR_C; 1.
DR   CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR033640; FAR_C.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR045520; GPAT/DHAPAT_C.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563:SF17; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF03015; Sterile; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          640..768
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   1192 AA;  133335 MW;  151BC8E1ACBEF4B2 CRC64;
     MEQFYAGKGL FVTGGTGFIG KTLIEKLLRS TPDIDKIYVM VRPKKGRSAH DRLESDVISS
     PIFNRLRAER PTDFDTFVRS KLVAVGGDIN SASLGMSRQD AQMLIDRVNV VVHSAASVSF
     NEPLDVAVEM NTLGAMYMLN FSKKIKSLAA YVHVSTAYVN SNRRNCTLME QLYPLDFDVE
     AAIDAVTKAS STEDIEKLHL NLIGTYPNTY TLTKSMAEHM VTKYREHVPL VLLRPTIVGA
     SWKEPIPGWV DQLAAAGAIF LAGGMGLLTI LPGDPRSIAD IVPVDFVVNA ILLSACAKAK
     EPVGSPPLIL HSGTSDPREQ PLRWRVPIGT VSSYFQQNPP EKGISRPSFT MFPSHQVFQI
     HWFLRYTLPS SAYSTIANAS GNAHHMKQAS RLWKLTWRAR QLVEVFKPFT ENQWVFRSDG
     LQFLRSMPEY SSTHWCCDAN DVMWERYLLN YSVGLRKWLL HEDVIDVDIE GVQHTEMALS
     TERMLEWDPD HHAISFPGLL PDISWAFTSS RKPGYTTSGI WGRFMGLTGW KEGVHHEATY
     VPRVPADPLS AIHDHVLHST GVQQVLANAM HVNPNADRAA MERQVHEMLT RMAATINYKT
     VRVAGWLLRK VWRQMYEKII VDEAGLETIR KLVQARDGPL VLIPTHRSYV DFLMMTYLFF
     AYNIPVPHIF AGEDFLNMGP MTRVLREGGA FFVRRSFKDD PLYAAVFSEY TQYLLTKGHT
     VEFFLEGTRS RSGKQLPPQF GMLSTVVKCF ESGRVDNIHL VPVTIDYDKP VELSVHQKEL
     LGEGKVKESV SALLKSYHVL RQDFGSVSVR FGPPIHLNEF VGAYKASPPV DSKTHQTVSL
     VTDLAYTITA SMIRRATCTP CHLVATILLM FRNGVTKEQL IGQTNWLRKE IVARGGRVLG
     SQGRTPAAMT ERALTLLGNL ICWRRSNLVE PAITNRDQYS NMIGLGYYRN KILHWFYKEG
     VIACTYHALH AATAASNASC GSASTTCSKQ TLLDKALFLH DILAVEFVRK DYGDSRADLE
     HALSMLTQRR VLSVDSQTST VALTDASQPT LSLLCAVLWP FIDSYWVALT SLVAMKGGER
     ISPKALVKRM QWLAETMYHD RIIAFYESCS METLSNAVTI LTTWGVVEEG VETKGPLQHK
     MSVIRLTDTY RSGSALEDLA AHLASFRKLP LAGPQSMDVA ALVAEFPSLS KL
//
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