ID G4ULN2_NEUT9 Unreviewed; 849 AA.
AC G4ULN2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Acyltransferase-domain-containing protein {ECO:0000313|EMBL:EGZ73719.1};
GN ORFNames=NEUTE2DRAFT_108607 {ECO:0000313|EMBL:EGZ73719.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ73719.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ73719.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
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DR EMBL; GL891217; EGZ73719.1; -; Genomic_DNA.
DR AlphaFoldDB; G4ULN2; -.
DR STRING; 510952.G4ULN2; -.
DR eggNOG; KOG3729; Eukaryota.
DR HOGENOM; CLU_015023_0_0_1; -.
DR OMA; ENMICKM; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
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; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR045520; GPAT/DHAPAT_C.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
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 SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:EGZ73719.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGZ73719.1}.
FT DOMAIN 216..343
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 95108 MW; 7366185A3A67F745 CRC64;
MADEQDGRDD SPAQVEDSAP DLRILGDRIT LQPSGFVAPS KGSLGDEKEE ALMKNMARFR
SEPLQFLREV SLYVSGTGWR AYDDVIGQPV FYPGYTEHIK SQVMSATLLQ AKIAQLAEMR
LAVEEKQGLL NKNDRNFETK RNQRRSVLVQ SLQEVAEQLT DNMVCKMESK TFIRGAYYMV
TQLLLRAYHQ GIHVSSEEVL RLRNVAREAE KKGQSIIFLP CHRSHVDYVA SQLLCYRLGL
TMPVVVAGDN LNFPLVGNFL QHAGAMFIRR SFGDDQLYTT LVQAYIDVLL QGGYNFECFI
EGGRSRTGKL LPPKFGILSF ILDSILSGRV QDTVICPVSY QYDKVVETEG YVTELLGVPK
KKENLADFLS GGSSVLSLRL GRVDVRFHEP WSLRGFIDEQ VIRLSKVPSS INWKDMKNPI
VRQKLLRTLG YKVLADINDV SVVMPTALIG TVLLTLRGRG VGRAELIRRV EWLTARVRAK
GGRVAHFGNT PVSDVIERGL EVLGKDLVGV AEGLAETTYY AVDRFQLSFY RNMTIHLFIS
EALVAAALYT RVKRGGGPAI QDIPYQDLHN QVLFLSSLFR GEFIYSGEGL AVNLEKTLMG
LEADNVVFLE RDELTGAITK VGLSDAERAA GRENYDFYCF LIWPFIEASW LASVSIMGLT
PPLGQKDDIW IQFSKAQESA QLLGKTLYHQ GDLSYFEAVN KETLKNSYQR FEEEGIIQVV
KSKDPKVPPR MRLAPEWRPA RDEISGVLIA SGRLWDFTEK IASSRREGKN RRDGATVSTR
VVRLTDDLGQ KLFEEAIAGT DGSKKGKGKG KGKGKGAAPA RLSREEEKIL TADLKESKRR
RTLENRAHL
//