ID A0A1B7MRM1_9AGAM Unreviewed; 451 AA.
AC A0A1B7MRM1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=ACBP-domain-containing protein {ECO:0000313|EMBL:OAX35265.1};
GN ORFNames=K503DRAFT_802970 {ECO:0000313|EMBL:OAX35265.1};
OS Rhizopogon vinicolor AM-OR11-026.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX35265.1, ECO:0000313|Proteomes:UP000092154};
RN [1] {ECO:0000313|EMBL:OAX35265.1, ECO:0000313|Proteomes:UP000092154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX35265.1,
RC ECO:0000313|Proteomes:UP000092154};
RG DOE Joint Genome Institute;
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (JUN-2016) 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; KV448516; OAX35265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7MRM1; -.
DR STRING; 1314800.A0A1B7MRM1; -.
DR InParanoid; A0A1B7MRM1; -.
DR OrthoDB; 948481at2759; -.
DR Proteomes; UP000092154; Unassembled WGS sequence.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR Gene3D; 1.20.80.10; -; 1.
DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
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:SF143; ACB DOMAIN-CONTAINING PROTEIN; 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; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 4: Predicted;
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000092154}.
FT DOMAIN 7..96
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REGION 110..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 49549 MW; 65B70F4C7AC8675A CRC64;
MDSRELIDAQ FDRAVEIVQG LPKTGPIQTG YEEKLTMYSL YKQATVGNVQ GARPGMWDML
GRAKWDAWAK HKDLDSCEAK WLYVDALLKV LNKYSDKTVA RDLMNELQSY GGDPSNLVMS
HSLSRSRGSQ SSGSSASDNE IPVIPGQLFS PTRPDILQAA QTAVIDESSS SSEDGESGDE
ARELPSLRDS AQQTRPISSM SSRYRTPVTG TLALSPPPAR LASVPPMQPM PAFETESAFA
GPQSASIPSS SVYLPQTPYS GTYQPPVFAP QINSAHSLRG GRSYIETPIR SASRLPLEQA
VENVQTHLAA ITERLDVLES QMVHQQRSNI SLPLRSSSGR GSPTHNLPEA LEWDLDDMGM
WSFVLKPLSR VVGSLKQLLI FFARSENRSP VLTIVRRLCL DISFSLAVLG LLRMTWKKTA
TRRREVNAAL VLLWAALSGR NRGRPLISRG V
//