ID B8LSW2_TALSN Unreviewed; 816 AA.
AC B8LSW2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Acyltransferase, putative {ECO:0000313|EMBL:EED22958.1};
GN ORFNames=TSTA_064270 {ECO:0000313|EMBL:EED22958.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED22958.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
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DR EMBL; EQ962652; EED22958.1; -; Genomic_DNA.
DR RefSeq; XP_002340345.1; XM_002340304.1.
DR AlphaFoldDB; B8LSW2; -.
DR STRING; 441959.B8LSW2; -.
DR GeneID; 8102481; -.
DR VEuPathDB; FungiDB:TSTA_064270; -.
DR eggNOG; KOG3730; Eukaryota.
DR HOGENOM; CLU_015023_0_0_1; -.
DR InParanoid; B8LSW2; -.
DR OMA; ENMICKM; -.
DR OrthoDB; 5478811at2759; -.
DR PhylomeDB; B8LSW2; -.
DR Proteomes; UP000001745; 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:EED22958.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EED22958.1}.
FT DOMAIN 212..339
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 816 AA; 91132 MW; 9DD229F72699F5F7 CRC64;
MSSKKDAIEA GQTAPDLEIV GDQVTLHPSG FTGGSDSQEN NGITERNLVR HMARFRENPF
DFLREVSLFV SGTGWRAYDS VIGQPIYYPG YSDNIKRLIV ESPLLRNKVT ELAEARLQVE
QSEGLYGDTP DAVGKARARR KTEIVQSLRD VVESMMDNMI CKMDSNAFIR SAYYIATQLL
TRAYHQGIHV SSEEVLRLRS VAQAAAEKKQ SIVFLPNHKS HVDYVSLQVI CYRLGIALPI
VVAGDNLNIP VVGPFLQHAG AMWIRRSFGD DQLYSTLVQT YIDVLLQQGH NFECFIEGGR
SRTGKLLSPK FGILNFILDS LLSGRVKDTI ICPVSTQYDK VIETESYISE LLGQPKQKEN
LANFLSQSSV LSLKLGRVDV RFHEPWSLKE FLVQQLQRIQ VTQALGSNIT LSYSERGRVL
RALGYRVLSD INDVSVMMPT ALVGTVLLTL RGRGVGKAEL VRRVEWLSER VRAKGGRVAH
FYRAPTSQVV DRALEVLGPK LVGEVTGLAE PTYYAVDRFQ LSFYRNMTIH LFIPEALVSA
AMYTKVKQGG GPANQDITYE ALLDQVTFLS QLFRGEFIFP PEGLIANLEK SLSGLEKDDV
IKITRNAAGT PTAVGLSDAE RQCGRENFDF YCFLIWPFIE ATWLGAVSLM GLTPPLNGPS
DIWVGLNKAQ DSAQLLGKTL YHQGDLSYFE AVNKESLKNA YQRFAEEGMI LIARSKDQPK
TPATMRLAPE WTPQRDPETG RLSDRGRLWD FTEKIAQSRR EGKNRRDGAT VSSRVLIMTD
TVGRQLFQSA ARAAETEVNV STRKARRTAI AERANL
//
