ID A0A445CXL8_ARAHY Unreviewed; 392 AA.
AC A0A445CXL8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=ACB domain-containing protein {ECO:0000259|PROSITE:PS51228};
GN ORFNames=Ahy_A06g030857 {ECO:0000313|EMBL:RYR55677.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR55677.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR55677.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR55677.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ACBP family.
CC {ECO:0000256|ARBA:ARBA00005567}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYR55677.1}.
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DR EMBL; SDMP01000006; RYR55677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445CXL8; -.
DR STRING; 3818.A0A445CXL8; -.
DR Proteomes; UP000289738; Chromosome a06.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR Gene3D; 1.20.80.10; -; 1.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR PANTHER; PTHR23310:SF122; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR23310; ACYL-COA-BINDING PROTEIN, ACBP; 1.
DR Pfam; PF00887; ACBP; 1.
DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 3: Inferred from homology;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..392
FT /note="ACB domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019289902"
FT DOMAIN 244..330
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REGION 117..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 43862 MW; 0FE3F1B0CEE9E7DF CRC64;
MELVTASDLF VTASLALLLS LLVAKLVSMA MASDPNTHNS HHRQQQQTLV TLQQERLTVQ
KPHSERKVEF LSPIQISTVE TARNREEESK VEIESRVVDF EVEALSTIAE LSEEHVAAEA
AEEEEGEVIE TNGDSEEFDP REAVEDSMEQ SKTEPVEDFE EQKETEPVKD SEEQRGTEDC
EEQREEECLQ VCEEQRETEC CEEKKGCSED CEEQRKTEGI TVEPFNDEDD HDDDGWEGIE
RSELEKEFIS ASEFVVGGGG NGLGSDVLME LYGLHKIATE GPCHEPQPMP LKLNARAKWN
AWQKLGNMTP DAAMEKYISV LSDKALGWIK DTSDGTIELE PKGSEVSEFA VPESSTSLSH
PQMTINEREL EQESGAQDHS TPAETEKNNV SL
//
