ID R0F7P3_9BRAS Unreviewed; 372 AA.
AC R0F7P3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=ACB domain-containing protein {ECO:0000259|PROSITE:PS51228};
GN ORFNames=CARUB_v10006316mg {ECO:0000313|EMBL:EOA17907.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA17907.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- SIMILARITY: Belongs to the ACBP family.
CC {ECO:0000256|ARBA:ARBA00005567}.
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DR EMBL; KB870811; EOA17907.1; -; Genomic_DNA.
DR RefSeq; XP_006285009.1; XM_006284947.1.
DR AlphaFoldDB; R0F7P3; -.
DR STRING; 81985.R0F7P3; -.
DR GeneID; 17879265; -.
DR KEGG; crb:17879265; -.
DR eggNOG; KOG0817; Eukaryota.
DR OrthoDB; 411549at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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 PRINTS; PR00689; ACOABINDINGP.
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:UP000029121};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..372
FT /note="ACB domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004340319"
FT DOMAIN 241..328
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REGION 168..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 40079 MW; D9AB094C831D7399 CRC64;
MDFFLEFILT ALLALLSSFL VAYLVSSATP SSDHAENKPE IIGVGDQFET DEVLLSGKKM
DARVMESVMN SSAVDDNVEL VDRFLNEADR VYEVEEAITG NAVIRGVHEA ESTAVLSPEN
SAIAEKIESA GEIGVEREEL VVRTTEAAES TGSVSPGNVV AEEIVLPGQE DRSESTELGT
SSCVEKEESG GDVAVAKFEE EVRVEETNTV AENHAQGDDE QKQELSIEDD DDWEGIERSE
LEKAFAAVAN HLEESGKSEG MGAEAKMDLY GLHKIATEGP CREAQPMAVM LSARAKWNAW
QKLGNMSQEE AMEQYLALVS KEVPGLMNAG HTVGKMSEME TSVCLPPNSG SLEDPTNLDT
TGVDEASKNG IP
//
