ID A0A183ABP5_9TREM Unreviewed; 825 AA.
AC A0A183ABP5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=CoA carboxyltransferase C-terminal domain-containing protein {ECO:0000313|WBParaSite:ECPE_0000439201-mRNA-1};
GN ORFNames=ECPE_LOCUS4380 {ECO:0000313|EMBL:VDP72416.1};
OS Echinostoma caproni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC Echinostoma.
OX NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0000439201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ECPE_0000439201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP72416.1, ECO:0000313|Proteomes:UP000272942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Egypt {ECO:0000313|EMBL:VDP72416.1,
RC ECO:0000313|Proteomes:UP000272942};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UZAN01041237; VDP72416.1; -; Genomic_DNA.
DR WBParaSite; ECPE_0000439201-mRNA-1; ECPE_0000439201-mRNA-1; ECPE_0000439201.
DR Proteomes; UP000050740; Unplaced.
DR Proteomes; UP000272942; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR InterPro; IPR049076; ACCA.
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; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF01039; Carboxyl_trans; 2.
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:UP000272942}.
FT DOMAIN 1..63
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 152..478
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 139..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 825 AA; 91356 MW; 26B760E8DA26B33B CRC64;
MALNKLLGRE VYTSNSQLGG VQVMANNGVS HLVASDELLA LQQTLEWLSY VPARKGLPVP
VLYRPVPVRR PAGWTDPNDY VVISAGSNPG SCASGGTKDS TEQLPFDPID RLIDYAPSRD
RPNDDPRWLF TGVLASQLNQ SNDLPPKNAS STSSTPTARS FHGNYTPESQ ARAGDHWLSG
FFDWGTWRET LTTWAAGVVV GRARLGGIPC GAITAETRSV TCRVPADPAN LSTEAQVVNQ
AGQVWYPDSA YKTAQAIADF ARERIPLFIF ASWRGFSGGM KDMYDQVLKF GSMIIDALRR
YPEPVFVYLP PQSQLRGGAW VVVDPAINPD RMEMYADPIA CRAGVLEPEG TVEIKYRKPD
LIQTMRRLDE QCLRLLTEID QLQTGCPVPS NQINSDSTLS VKERVRQLQM ALEARQKELR
PYYHQVACTF ADLHDTPGRL QTRGLVHGLV AWSESRSFFY ARLRRRLLEM HAIRLMDTVC
LNPANDVLMI GKELSEHLSR LSRVRCHGRV RTISELATVE ELSQKAGNAT ADRTKPGKSY
DTIAVPDCPL QLDPLFIWKN TNAVGPVIQR TTHQLKKSHE VYQKLIINVL LYFLCTSFPK
GVEYSSQFAR GLAILQQWFL QAHTSSELTR TTDTVNSSVH NTKTPGDHGI NNTGSKKGRK
SARSRSQRST SSNLADENAK QPDSMTRTSS TMEPEAAERA WSDDHLGVGA WLAQQLGCKQ
FCYVPKLANL VPNVGKPNPE SPGSLVDGLD EIAVSDPPEK SPVTFLGSQI EALKRRHMFE
RIQSTLSASS DMTKELASVL HQLLSPTDCA HLVQLLSVPK DHETG
//
