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Database: UniProt
Entry: A0A1B7MRM1_9AGAM
LinkDB: A0A1B7MRM1_9AGAM
Original site: A0A1B7MRM1_9AGAM 
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.
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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
//
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