ID   A0A010S175_9PEZI        Unreviewed;       466 AA.
AC   A0A010S175;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Acyl CoA binding protein {ECO:0000313|EMBL:EXF86646.1};
GN   ORFNames=CFIO01_05495 {ECO:0000313|EMBL:EXF86646.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF86646.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF86646.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF86646.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) 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:EXF86646.1}.
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DR   EMBL; JARH01000002; EXF86646.1; -; Genomic_DNA.
DR   RefSeq; XP_007589735.1; XM_007589673.1.
DR   AlphaFoldDB; A0A010S175; -.
DR   STRING; 1445577.A0A010S175; -.
DR   KEGG; cfj:CFIO01_05495; -.
DR   eggNOG; KOG0817; Eukaryota.
DR   HOGENOM; CLU_586598_0_0_1; -.
DR   OrthoDB; 948481at2759; -.
DR   Proteomes; UP000020467; 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   Pfam; PF00887; ACBP; 1.
DR   SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR   PROSITE; PS51228; ACB_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        185..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..53
FT                   /note="ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51228"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..96
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   466 AA;  52683 MW;  A68932B70BD9892F CRC64;
     MERPTSASGM PADELQREKD KWDAWNLQKG LSRTEAKRRY IEALIETMHK YATTPDAKEL
     VSELEFVWNQ IKNNSPSSTD SSPKGTGYTG ELRQFQPPLT GSEGPLKVLS PMSEDDAAER
     NSDGRIGYDD DDEGDALVAS SNWSRSVERA LEKLSAEVAA LREQITTGRE WKSKKSRSFP
     AWLRWFTWVI MKHLAIDMVL LAFILLWMRK RKDRRLEDLV RAGVKLMRES QHREFYLRCG
     QGPDWHSDFD NSDGFVGKMQ EAISDQSARL GKAGAVGDYT MEVEEEDIPQ AVPALAMFIP
     LEESLFDPYD APRTEIERIK LCQENLEKHT AAVEQNLVFV YEREHRRILQ VAKQEEAEMG
     FIETPAGLMQ GEEALIMDSV HAPIPPGADY NDRHLSTYKP PETPQVMPPR PSALQWSLYN
     AGQAVGQLHG YTNHAQELKE PYQEMLKAAL AASSANQGQG DEPARS
//