ID S8EBL0_9LAMI Unreviewed; 362 AA.
AC S8EBL0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=ACB domain-containing protein {ECO:0000259|PROSITE:PS51228};
GN ORFNames=M569_04861 {ECO:0000313|EMBL:EPS69902.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS69902.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS69902.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
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:EPS69902.1}.
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DR EMBL; AUSU01001905; EPS69902.1; -; Genomic_DNA.
DR AlphaFoldDB; S8EBL0; -.
DR OrthoDB; 7787at2759; -.
DR Proteomes; UP000015453; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR PANTHER; PTHR24119; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 6; 1.
DR PANTHER; PTHR24119:SF0; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 6; 1.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF12796; Ank_2; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS51228; ACB_2; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 109..199
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REPEAT 273..305
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 306..338
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 200..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 39498 MW; 12FE07453A6F2F56 CRC64;
MAEWQQLLQS VIFGIVFSFF LAKLFSVIFA FREDNLRIAR SHSVEAESEA PPESEPAGLV
SETHVLEENE PFIRQEDAKS GDVNAVDRYQ AEIEESDDDD WEGVEITELD ETFSAATVFV
AATAADRSSL KVSNEVQLQL YGLYKIATEG PCTAPQPSPL KMTARAKWQA WQKLGSMPIE
EAMQKYIDIV TELYPSWAAG SSANESKNEG SSDEPASGSS GPMGPVFSTL AFEEEPGSEL
KMDAIHGFAR EGDGEKVLKC IESGIGVNLQ DSEGRTPLHW AVDRGHLNIS ELLLKNNADI
NAKDNEGQTA LHYAAICERS DIAKLLVENG ADIEATDNEG NAPKDICASS WSGSVFRVKS
LE
//
