ID A0A1E3HZH0_9TREE Unreviewed; 469 AA.
AC A0A1E3HZH0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ACB domain-containing protein {ECO:0000259|PROSITE:PS51228};
GN ORFNames=L202_02066 {ECO:0000313|EMBL:ODN81667.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN81667.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN81667.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN81667.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:ODN81667.1}.
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DR EMBL; AWGJ01000003; ODN81667.1; -; Genomic_DNA.
DR RefSeq; XP_018995986.1; XM_019135583.1.
DR AlphaFoldDB; A0A1E3HZH0; -.
DR STRING; 1295533.A0A1E3HZH0; -.
DR GeneID; 30153375; -.
DR OrthoDB; 948481at2759; -.
DR Proteomes; UP000094065; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000094065};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 425..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..96
FT /note="ACB"
FT /evidence="ECO:0000259|PROSITE:PS51228"
FT REGION 118..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 51734 MW; 2EAF96BBF2F3D601 CRC64;
MSIEPNIDNK FHRAVDIVQS LPKGGPIQTT YEEKLWLYSL YKQATEGDIR IPRPGMLDLL
GKAKWDSWHK QEGKTKTEAK AHYVEALCKI LERNGGEEEV EGFLTELEGM SGLARFRDMA
PRPASPASST SSYHSSQASP PLSPGHSPRA PRDQNQDISL EPSSMDPQGV LLPPDPLLPP
PDVAPSFVPP SALTSSHRSL LSLSQEQEAA DTYQPLHLPP RPVPYVGSRA QSSRGDPQDS
RVVRDLLGES GPGSVQSFRQ RQGYDRPVAL DPRAGSRLAS PSIPPPLPRD YVHTPEMQGS
AFASLGLDGT PIYQSQKPPG PGSASTYGPP PPLNISYTLQ QIQTSLAALH ERLSTLERTQ
AMILRSDGRK KSWLWWSTEG DDLDQAEAEA ERERWGFTTV TRQRQKKKPL SLRVVWFLLK
ALRRVLVDAG VGAVLIFIVW IMLNGGVKRA RVLLGLIKMR ARRLITGGL
//
