ID   A0A2K1QH25_9PEZI        Unreviewed;       326 AA.
AC   A0A2K1QH25;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Autophagy-related protein 37 {ECO:0000313|EMBL:PNS14465.1};
GN   ORFNames=CAC42_3751 {ECO:0000313|EMBL:PNS14465.1};
OS   Sphaceloma murrayae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX   NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS14465.1, ECO:0000313|Proteomes:UP000243797};
RN   [1] {ECO:0000313|EMBL:PNS14465.1, ECO:0000313|Proteomes:UP000243797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS14465.1,
RC   ECO:0000313|Proteomes:UP000243797};
RA   Cheng Q.;
RT   "Draft genome sequence of a variant of Elsinoe murrayae.";
RL   Submitted (JUN-2017) 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:PNS14465.1}.
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DR   EMBL; NKHZ01000086; PNS14465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K1QH25; -.
DR   STRING; 2082308.A0A2K1QH25; -.
DR   InParanoid; A0A2K1QH25; -.
DR   OrthoDB; 948481at2759; -.
DR   Proteomes; UP000243797; 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:UP000243797};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        259..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..105
FT                   /note="ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51228"
FT   REGION          49..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..187
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   326 AA;  35953 MW;  043688A67C586D21 CRC64;
     MSDSIDRVFG HALNTINKIR TGSLKPPLPD RLMLYGLYKQ AMEGDVAPIT ARPSVGPTPT
     STSTSSSAKE AEKWDAWHAN AGMGRTEAKK RYIEKLIETM HAYATSTPEA RELVAELEFV
     WDQVKGNSLA GSGSGSGSGQ GSSPRRQGTG GQGMRVLRPE TGRAVDEAGD GVGGGDGDED
     EDEREEFVDA PVSQFGEMEE KSEGPGEGER AVRRRVPVAD VKWRRRVETA IVKMTTEVAA
     LRELVESRRY TAQRRRTSFV SWILGFGWFA VRLVVADVFL LWLVILYLRR RKDRRLEGAI
     RVMLGDAQAV AKNLATSMQN KLPSRK
//