ID   A0A319CVT8_9EURO        Unreviewed;       369 AA.
AC   A0A319CVT8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=ACB domain-containing protein {ECO:0000259|PROSITE:PS51228};
GN   ORFNames=BO71DRAFT_423338 {ECO:0000313|EMBL:PYH88950.1};
OS   Aspergillus ellipticus CBS 707.79.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH88950.1, ECO:0000313|Proteomes:UP000247810};
RN   [1] {ECO:0000313|EMBL:PYH88950.1, ECO:0000313|Proteomes:UP000247810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH88950.1,
RC   ECO:0000313|Proteomes:UP000247810};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KZ826056; PYH88950.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319CVT8; -.
DR   STRING; 1448320.A0A319CVT8; -.
DR   Proteomes; UP000247810; 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   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; ACYL-COA-BINDING PROTEIN, ACBP; 1.
DR   PANTHER; PTHR23310:SF135; COA BINDING PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12300)-RELATED; 1.
DR   Pfam; PF00887; ACBP; 1.
DR   SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR   PROSITE; PS51228; ACB_2; 1.
PE   4: Predicted;
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247810};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        312..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..99
FT                   /note="ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51228"
FT   REGION          167..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..219
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   369 AA;  42841 MW;  EE57D0676B128867 CRC64;
     MSDSVDRVFV HALNTVKRIP RTGTARPPAS ERLKLYGLYK QSMEGDVEGV MDRPVGNTAD
     VFMECEKWDA WSTQRGLSRT EAKRRYISTL ISTMHNYASQ TAEARELVAE LEFVWDQIKS
     NPGSSSSQEL NSPISAREVP PVQYQSRLSR PEYEQLLATA RGDSRLRVLS PVSQPEGRIY
     RHEDEGEEEE EEEEEEEEVY AEAQDNLFEG DDENEDGNVD HDRDESHEYQ QQSYPLPDPD
     PDRGGSDASH HHHHHNIHHA ARKPPSSDRR WRRRVEQALT KMTAEIAAVR EQLEARALAH
     RRRTGIWAWL KWLVWVTMRQ LVVDLAVLGI LLVWMRLRGD RRLEQKLKVG WAEVKSRLAR
     WKVLWRRGI
//