ID A0A058ZYY6_EUCGR Unreviewed; 372 AA.
AC A0A058ZYY6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=ACB domain-containing protein {ECO:0000259|PROSITE:PS51228};
GN ORFNames=EUGRSUZ_K00399 {ECO:0000313|EMBL:KCW46581.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW46581.1};
RN [1] {ECO:0000313|EMBL:KCW46581.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW46581.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ACBP family.
CC {ECO:0000256|ARBA:ARBA00005567}.
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DR EMBL; KK198763; KCW46581.1; -; Genomic_DNA.
DR RefSeq; XP_010035287.1; XM_010036985.2.
DR AlphaFoldDB; A0A058ZYY6; -.
DR STRING; 71139.A0A058ZYY6; -.
DR EnsemblPlants; KCW46581; KCW46581; EUGRSUZ_K00399.
DR GeneID; 104424525; -.
DR Gramene; KCW46581; KCW46581; EUGRSUZ_K00399.
DR KEGG; egr:104424525; -.
DR eggNOG; KOG0817; Eukaryota.
DR InParanoid; A0A058ZYY6; -.
DR OMA; RPMGPVF; -.
DR OrthoDB; 7787at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
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; 3.
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 122..212
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REPEAT 283..315
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 316..348
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 42..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 39220 MW; 3EEE281A78693089 CRC64;
MGGDWQPLLQ SVFIGLIFSY LLAKLISLLF TFKEEGLTVA RAPAPAPAPA PAPAPAAAAA
KRPGSGAGDA AEPDGADGGG ESRDSDSVVA EHGSVRNESA AGTDDDGGGS DSDWEGVEST
ELDEIFSAAT AFAAAAAADR LSQRVSSDAQ LQLYGLYKIA TEGPCTAPQP SALKMTARAK
WQAWNKLGAM PPEEAMQKYI DIVTELYPTW IAGSSMKSKG SHGDAPSTEA KGPMGPVFST
FVHEEPGTES KLDAIHAFAR EGEIDNLLKC VEAGVSVNVK DSEGRTPLHW AVDRGHSKVV
EMLVSKDADV NAKDDEGQTP LHYAVVCDRE GIAEFLVKQN ASTDVKDNDG NTPHDVCESD
WPWMRSAVVH AD
//
