ID A0A0K0D5M8_ANGCA Unreviewed; 992 AA.
AC A0A0K0D5M8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=ACC_central domain-containing protein {ECO:0000313|WBParaSite:ACAC_0000537301-mRNA-1};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000537301-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0000537301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0K0D5M8; -.
DR STRING; 6313.A0A0K0D5M8; -.
DR WBParaSite; ACAC_0000537301-mRNA-1; ACAC_0000537301-mRNA-1; ACAC_0000537301.
DR Proteomes; UP000035642; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR049076; ACCA.
DR InterPro; IPR049074; ACCA_BT.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF21385; ACCA_BT; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000035642}.
FT DOMAIN 64..174
FT /note="Acetyl-CoA carboxylase BT"
FT /evidence="ECO:0000259|Pfam:PF21385"
FT DOMAIN 258..507
FT /note="Acetyl-CoA carboxylase central"
FT /evidence="ECO:0000259|Pfam:PF08326"
SQ SEQUENCE 992 AA; 113113 MW; 2228DA1E65FD6939 CRC64;
MLCALQELEL RASFSSQVSY LVDMLKEPDF TENRFNTQWL DNRIANKVLQ KAPLPKHEMI
AVSSAVIGHA RVTTAFNNFK NAVERGQVLP TKDLTETFLF DLVKDMNIYK VTVTRSGPLN
YIVTLNGGKT QVEIRLLGDG SLLVTHQERS YTCNLEETSD KFKVTIGRSI VVFEKDNDPT
ILKSPYTGKL LTYKKANREW VGVGSVYASV ESMKLVFNVE VKKAPGRLEH VAKEGDLLYP
GSVIARLVDQ KDGEKYKPKP FLETFPEWAE FSENERVLPE TKRHNICFDM CMNVLNGSIP
PGADFCMTDL VDELFSYLES PTLPHALFKQ ALSSMVNRLP EKFSSRIKDT VQVESMRNFA
LVKSILDEYF GSLSHTEWET AKAVCNMVYH ICERFENGIL SNTSYVLNSL LSEYKQCEKF
FEGRVYDDAV ALLNDEFGSD KDRVVAMIYS HTQLKGKNKL MLALFKAIEQ RGAHLVAPLI
ENLREIGNMF HTDEIVWDME KVSLAERDSK EVLSVNEAVS KLRSIFAQMV DSGMSPKDML
NASPWIHKVI HEFFFDEKLA DFAIRAYIGL HFAVDDVTCS ALSCANHDAQ VYDFFVDNSN
LVHYMISPSV DSNQYLSIIK LSVNQDNFAQ AITHENLINS LVSKFSECGI KSNGIRSQLR
VTLLVNVVQK TTLAESKKGY REAQLEELPF HSDYDDLIVA EAENASIVIR NALAKKLVAV
DIITHVLVCS PYKPLTQVDL LGAERLELWR LPKESRLVSD RLSNLNVFKY DDPDKHFSRL
FVRQILEIPI RSADEGLDIV GSTVSAQLDS ACGAINVSMR KFKKNIFVSN HVFMYVTFPK
MPVTFTVEHQ NVLDFLFEEA IKEQRDVLYK HHVTEVEIVF TKLSENGGVR QLWRRRIKFL
DETGVTPEFG IYDEYKTIIF PQKLSHLLYK SKLEPHTKIK KIEKKRSSTR ANGTTYVYDY
PTLIGRACLE EWKKLQDRCE GVVEGCERNL FQ
//