ID E3QID6_COLGM Unreviewed; 824 AA.
AC E3QID6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 08-NOV-2023, entry version 47.
DE SubName: Full=Acyltransferase {ECO:0000313|EMBL:EFQ30546.1};
GN ORFNames=GLRG_05690 {ECO:0000313|EMBL:EFQ30546.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
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DR EMBL; GG697350; EFQ30546.1; -; Genomic_DNA.
DR RefSeq; XP_008094566.1; XM_008096375.1.
DR AlphaFoldDB; E3QID6; -.
DR STRING; 645133.E3QID6; -.
DR EnsemblFungi; EFQ30546; EFQ30546; GLRG_05690.
DR GeneID; 24411055; -.
DR VEuPathDB; FungiDB:GLRG_05690; -.
DR eggNOG; KOG3730; Eukaryota.
DR HOGENOM; CLU_015023_0_0_1; -.
DR OrthoDB; 5478811at2759; -.
DR Proteomes; UP000008782; 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:EFQ30546.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EFQ30546.1}.
FT DOMAIN 204..331
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 717..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 87..114
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 824 AA; 93051 MW; 58E8E10D2A350A81 CRC64;
MAKNDDSAPD LKILGDQITL QPRGYVKPSQ PRHDEKEEAL MKHMARFRSE PLQFLREVSL
YVSGTGWRAY DNAIGQPIFY PGFSDKMKEA VLSAKLLQER IADLAEKRVA VEEKEGLLNK
QDKDFDLKRA RRRAVIDSGI QEVAEKMTDD MICKFESKTF IRSAYYLTTQ LLLRAYNQGI
HVSSEEVLRL RKVAEEAEKK KQSIIFLPCH RSHVDYVSLQ LICYRLGLGL PVVVAGDNLN
FPLVGSFLQH AGAMWIRRSF GDDILYTTLV QTYIDTLLQG GYNFECFIEG GRSRTGKLLP
PKFGILSFVL DSILSGRVED AIICPVSTQY DKVIETEGYV TELLGVPKKK ENLADFLSGG
SSVLSLRLGR VDVRFHEPWS LRGFINEQLT RVSRLPTSLN LDVKDPENAA IRQRLLRILG
YKVLSDINDV SVVMPTALIG TVLLTLRGRG VGKAELERRV MWLTDRVRAK GGRVAHFGNA
PLSDIIERGL EVLGKDLVGV VKDLPEPTYY AVDRFQLSFY RNMTIHLFIS EAIVSAAMYM
KVKQGGGPAM QDISFDELQN QIRFLSSLFR GEFIFPSEGL AANLEKTLRD LEADKVLKLN
RDDQGRVTVV GLSDHERTVG RENYDFYCFL IWPFIEASWL AAVSLMGLTP PLGQNNDIWI
EAAKAQGSAQ LLGKTLYHQG DLSYFEAVNK ETLKNAYQRF EEEGILQVVK SKDPKVPPRL
RLDPEWRPSR DPETGSLNAS GRLWDFTEKI ASSRREGKNR RDGATVSTRV LRLTDLLGSK
LFDAARNVDG KGVSPTLSVE DARQLKKSVK EQRRRRSLEN RAHL
//