ID E6ZUA7_SPORE Unreviewed; 541 AA.
AC E6ZUA7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=ALE1-broad-specificity lysophospholipid acyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=sr12475 {ECO:0000313|EMBL:CBQ70814.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ70814.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ70814.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FQ311441; CBQ70814.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZUA7; -.
DR EnsemblFungi; CBQ70814; CBQ70814; sr12475.
DR VEuPathDB; FungiDB:sr12475; -.
DR eggNOG; KOG2704; Eukaryota.
DR HOGENOM; CLU_011340_5_1_1; -.
DR OrthoDB; 5297955at2759; -.
DR Proteomes; UP000008867; Chromosome 2.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblFungi.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:EnsemblFungi.
DR InterPro; IPR004299; MBOAT_fam.
DR PANTHER; PTHR13906:SF4; OYSGEDART, ISOFORM A; 1.
DR PANTHER; PTHR13906; PORCUPINE; 1.
DR Pfam; PF03062; MBOAT; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 459..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 493..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 59897 MW; 1D8469C9A53593DF CRC64;
MLESVFQPIA DAAGAPVDYI KLFSCLLAAF PLAAAFPYLP SPAAKHLYSL AVSFVFLVPV
LNLYSGFLQL VGSALVTYAI CTFKVGGRNM AWLVFALQMG HLTYNHAVRK FGGIPLSTLE
ITAMQMVAVM NLTTFAWDCY DGQIRTAEQC DDSQRQSRIT KMPSVLEFLG YAFYFPGVLI
GPSTRFCDYQ AWSTGELYAS PKGKEKAATA ASLPRGRLFA SAVSLLAGLA FMAIYSVFAP
AYSYEKLIGL HGGVAHLAWY QKLLWIQVAG FMARTKYYGI WSLTDGACIL SGLGYNGVDA
KTGKTRWDRC RNIDIPKIEF ANNWKELLDH WNMNTNVWLR NNVYKRIARP GKKPGFKSTM
TTFFTSAFWH GLEPGYYLSF ILAGFMQSAA RQLRRHVRPL FFTQPNVPNP TFSNALTFTP
AQLAYCTASV VVSQFTLNYA VAPFMLLELE ASFRGWKAVY FYGHVVTFVA ILAFQNGLGR
ALDKRSGKAK KRVENGGGAF ATGFTTDADS DAEGVRRRAA RKQKLDEQAE DVTALAPEPI
S
//