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Database: UniProt
Entry: D2VWR0_NAEGR
LinkDB: D2VWR0_NAEGR
Original site: D2VWR0_NAEGR 
ID   D2VWR0_NAEGR            Unreviewed;       549 AA.
AC   D2VWR0;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC38742.1};
GN   ORFNames=NAEGRDRAFT_52866 {ECO:0000313|EMBL:EFC38742.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC38742.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC38742.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
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DR   EMBL; GG738905; EFC38742.1; -; Genomic_DNA.
DR   RefSeq; XP_002671486.1; XM_002671440.1.
DR   AlphaFoldDB; D2VWR0; -.
DR   STRING; 5762.D2VWR0; -.
DR   EnsemblProtists; EFC38742; EFC38742; NAEGRDRAFT_52866.
DR   GeneID; 8858372; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_52866; -.
DR   eggNOG; KOG0540; Eukaryota.
DR   InParanoid; D2VWR0; -.
DR   OMA; ENTSYMF; -.
DR   OrthoDB; 864at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   PANTHER; PTHR43842:SF2; BIOTIN-DEPENDENT ACETYL-_PROPIONYL-COENZYME A CARBOXYLASE BETA5 SUBUNIT; 1.
DR   PANTHER; PTHR43842; PROPIONYL-COA CARBOXYLASE BETA CHAIN; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT   DOMAIN          40..296
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          305..546
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  60226 MW;  2D032916F27556DC CRC64;
     MGSRMFSQQL NRVSGSKGPT EIDISGVMDI PSKQAPPEIL RTLQERVDNV KKEAKLGGGV
     ERMEKQHQKG KLTARERIDL LVDEGSFREY DAFVRHRATD FGMEKDRPAG DGVVTGHGTI
     NGRLVFVFSQ DFTVFGGSLS ETHAQKICKI MDKAMEVGAP VIGINDSGGA RIQEGVASLA
     GYAEVFQRNV NASGVVPQIS LICGPCAGGA VYSPAMTDFI FMVRNTSYMF VTGPDVVHSV
     TRETVTSEQL GGAQTHTQVS GVAHRAFDND IELIKYTREF ISYLPSSNRE NAESRLLATN
     DPVDRKDMSL DFAVPSDTNA PYNMLSSIIK PIVDDHAFFE IMPDYAKNII TGFARMNGET
     VAIIANQPCE LAGVLDINSS IKAARFVRFA NAFNIPILTF VDVPGFLPGT AQEYGGIIRH
     GAKLLFAYAE ATVPKITVIT RKAYGGAYDV MSSKHLRGDY NYAWSTATIA VMGPEGAVKI
     IKGIEGETQK DREETYRNKF ATPLLAAERG FLDDVIKPHE TRQRIIEDLE ILRTKKKENP
     TKKLSNIPL
//
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