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Database: UniProt
Entry: A0A178EFZ5_9PLEO
LinkDB: A0A178EFZ5_9PLEO
Original site: A0A178EFZ5_9PLEO 
ID   A0A178EFZ5_9PLEO        Unreviewed;       596 AA.
AC   A0A178EFZ5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   28-JUN-2023, entry version 18.
DE   SubName: Full=CRAL/TRIO domain-containing protein {ECO:0000313|EMBL:OAL54908.1};
GN   ORFNames=IQ07DRAFT_618819 {ECO:0000313|EMBL:OAL54908.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL54908.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL54908.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL54908.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV441638; OAL54908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178EFZ5; -.
DR   STRING; 765867.A0A178EFZ5; -.
DR   InParanoid; A0A178EFZ5; -.
DR   OrthoDB; 1539at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   InterPro; IPR001251; CRAL-TRIO_dom.
DR   InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR   InterPro; IPR011074; CRAL/TRIO_N_dom.
DR   InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR   PANTHER; PTHR46590:SF1; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN CSR1; 1.
DR   PANTHER; PTHR46590; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN CSR1-RELATED; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   SMART; SM01100; CRAL_TRIO_N; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          329..474
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   REGION          150..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          574..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   596 AA;  66555 MW;  09B54830CFA98BF0 CRC64;
     MLRRTLRTPL STAPIYRHSS RFAHQYQTRL KSLDSTRFAT CAEGAFRRSS TAAPNFAKRS
     GTGLWTVALL ITVAVGGAFV VPFVKSSPKH KRIENTQSSP FVVSDLTDSY LVMAPNTPAG
     RPGTLTPDEE QKLREMWTMT LQVFGVELLG EGTNGSTTPA AVPASEAPAD KEGKKEKEKK
     KSRLNVFRRN KGEKGADTDS IASGTSTPSD ISSLSISAEH DKHGQTAEFK AAIANMPPEE
     LRRAFWSMVK HDHPDALLLR FLRARKWDVE KALVMMVSTM HWRLEEQHVD DDIVKNGELA
     ALNTKGDDAK AKKNADDFLT QLRLGKSFLH GLDNEGRPMC FVRVKLHKAG EQTEESLERF
     TVYTIETARL LLRSPIDTAT IVFDMTDFSM ANMDYTPVKF MIKCFEANYP ESLGTVLVYK
     APWVFNAIWT IIRGWLDPVV ASKVHFARSV DELAAFVPKS QIPTELGGDE KWEYKYPEPV
     PGENDKMDDT AARDDLEAKR KDIVNKYEAT VLEWIAAGDA GKSLDERRKE RDGLAEELRK
     NYWTLDPYVR SRSLYDRIGI IQPGGALDFY GKEKGPAAAA PVEAPKTVET SAEDLD
//
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