ID K2RNX0_MACPH Unreviewed; 630 AA.
AC K2RNX0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Phospholipid/glycerol acyltransferase {ECO:0000313|EMBL:EKG16433.1};
GN ORFNames=MPH_06343 {ECO:0000313|EMBL:EKG16433.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG16433.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG16433.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG16433.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG16433.1}.
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DR EMBL; AHHD01000268; EKG16433.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RNX0; -.
DR STRING; 1126212.K2RNX0; -.
DR VEuPathDB; FungiDB:MPH_06343; -.
DR eggNOG; ENOG502QQ2N; Eukaryota.
DR HOGENOM; CLU_007860_1_0_1; -.
DR InParanoid; K2RNX0; -.
DR OrthoDB; 2728187at2759; -.
DR Proteomes; UP000007129; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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 SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:EKG16433.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007129};
KW Transferase {ECO:0000313|EMBL:EKG16433.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 467..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 516..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..264
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 606..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 70480 MW; 1230DF4BF3D12048 CRC64;
MARKHKVVPW IYDLGLWIFT LCLDIFFREV YPRNAWRVPK RGPVVLIAAP HANQFVDSVL
LMRILKQHAA RRVSFLIAQK SMNEPYIGAM AARMGALPVV RAMDNIKPGQ GQIYLPDPEN
DPTLVRAKGA NFTDDIFMVS GALILPKVGN ESPEQQPIAE ILGPDELRLK VPFKKFEPDH
PLYKALREGT SFKVAPHIDQ HEMFDAVYTE LCEGGCIGIF PEGGSHDRPS LLPLKAGAAI
IALGTLARDP SCGLTIIPTG MNYFHPNKFR SRAVIEFGNP IHVHPDQVAA FREGGDSKRT
AVSSLLDTIQ AALAAVTQQA PDHQTLMLIQ ATRRLYKPLR MKLPLPTIIE INRRLLEGYT
RFQHEPQVKA LTRSVTAYNR QLRALGIKDH QVEWGNVRQR PWLFVLGTLI YRIGFLLTLV
AGTLPSLALF WPVFVTSKII SVKKQRKALA GSSVKLQARD VVGTWKMLVA LGLAPALYVW
YTGAMTAWLV YCRRGGAYCE NAPWWLQATT WVPDSLPLRA FVPAFFALMV GVTFAGLRIG
EVGIDVVKSL PPLLVALNPM SLGSLVLLRE RRKALAREVR DVVETFGPEI FPDFERQKLI
VRAEMDEAEE DEDEMNDYDG AVESEMKKTV
//
