ID Q8ITY6_CAEEL Unreviewed; 405 AA.
AC Q8ITY6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 3.
DT 27-MAR-2024, entry version 129.
DE SubName: Full=Malonyl-CoA:ACP transacylase (MAT) domain-containing protein {ECO:0000313|EMBL:CCD65341.2};
GN Name=mcat-1 {ECO:0000313|EMBL:CCD65341.2};
GN ORFNames=C50D2.9 {ECO:0000313|WormBase:C50D2.9}, CELE_C50D2.9
GN {ECO:0000313|EMBL:CCD65341.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD65341.2, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD65341.2, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD65341.2,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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DR EMBL; BX284602; CCD65341.2; -; Genomic_DNA.
DR RefSeq; NP_871954.3; NM_182154.3.
DR AlphaFoldDB; Q8ITY6; -.
DR SMR; Q8ITY6; -.
DR STRING; 6239.C50D2.9.1; -.
DR EPD; Q8ITY6; -.
DR PaxDb; 6239-C50D2-9; -.
DR PeptideAtlas; Q8ITY6; -.
DR EnsemblMetazoa; C50D2.9.1; C50D2.9.1; WBGene00016812.
DR UCSC; C50D2.9; c. elegans.
DR AGR; WB:WBGene00016812; -.
DR WormBase; C50D2.9; CE50540; WBGene00016812; -.
DR eggNOG; KOG2926; Eukaryota.
DR GeneTree; ENSGT00390000013715; -.
DR HOGENOM; CLU_030558_2_3_1; -.
DR InParanoid; Q8ITY6; -.
DR OMA; AANYNCP; -.
DR OrthoDB; 2265421at2759; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016812; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR PANTHER; PTHR47170; MALONYL-COA ACP TRANSACYLASE, ACP-BINDING; 1.
DR PANTHER; PTHR47170:SF2; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
PE 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|EPD:Q8ITY6,
KW ECO:0007829|PeptideAtlas:Q8ITY6};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 97..402
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
SQ SEQUENCE 405 AA; 45112 MW; 2519DF0F084DB791 CRC64;
MLTPFNIARC STRLIRRKPP GGGILDEGVT FSDVHNVILN PTTRLPYPEE QLREHIEKTS
SEIMKERNKI RYGTRKKKDS GAIDFSQLPI EEHVVLLFPG QGAQFVGMGQ KVMDIPAARR
VFDEASEVLG YDMLKVCQDG PKQKLEQTLY CQPAIVTSSI AAFEALKASD PSIEENLTDT
AGFSVGEYAS LVAGKVLSFS DAIKIVKTRA EAMSECAKLV KSGMVTIRVK AASKLDKAMA
DARKVAAENR ELVVCEVANY LYCGVRVIGG SETCLKYLEE NQEKYNIQVM KRLAVSAAFH
TRQMESAVEQ VAKAFQNVEI HRPVCNVWSN YSGKVMSSKK GDVRGAVAKQ INSPVRWEQI
QQSLFRKHQN EAFPRFYEVG AGRQLGAMLF QTSKKAHKNY SHFSC
//
