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Database: UniProt
Entry: A0A2H3I934_9EURO
LinkDB: A0A2H3I934_9EURO
Original site: A0A2H3I934_9EURO 
ID   A0A2H3I934_9EURO        Unreviewed;       391 AA.
AC   A0A2H3I934;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=FERM/acyl-CoA-binding protein, 3-helical bundle {ECO:0000313|EMBL:PCG90060.1};
GN   ORFNames=PENO1_101070 {ECO:0000313|EMBL:PCG90060.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG90060.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCG90060.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCG90060.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
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:PCG90060.1}.
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DR   EMBL; NPFK01000527; PCG90060.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3I934; -.
DR   STRING; 290292.A0A2H3I934; -.
DR   OrthoDB; 948481at2759; -.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
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:SF77; LD25952P; 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   Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT   DOMAIN          5..99
FT                   /note="ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51228"
FT   REGION          124..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..230
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  45049 MW;  E679ECB403C0FF12 CRC64;
     MSDSVDRVFV HALNTVKKIP RTGTARPPAA ERLKLYGLYK QSMEGDVEGI MDRPIGDAPD
     VQAEREKWDA WYSQRGSSRT EAKRRYITTL INTMHLYASQ TAEARELVAE LEFVWDQIKY
     NAASSSTSSS SPIQATRTLP SVSVSAAASA PRRYGSIDDR MTRSPAADVE DQDEDLAIYR
     RRSGDSRLRV LSPVSQSDEA EVRSHRHANE DHDDDDEDED DEDDEEDDFQ EARTGTSFSD
     TSHHDANIEE DAANHRTRKK RKRRPSHSQS KDWRHRIEQA LTKMTTEIAA LREQLDSLPI
     THHSHSHSLR RPSNFFAWLL SWGKWFLFHT LRQLLWQSII LSVVLVWLRA RGDTRLERRV
     VAILLQLRRR MMNAIQSVPR RLPKLLHLPL L
//
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