ID B8P5V7_POSPM Unreviewed; 306 AA.
AC B8P5V7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 22-FEB-2023, entry version 50.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EED83739.1};
GN ORFNames=POSPLDRAFT_95611 {ECO:0000313|EMBL:EED83739.1};
OS Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS (Poria monticola).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Postiaceae; Postia.
OX NCBI_TaxID=561896 {ECO:0000313|Proteomes:UP000001743};
RN [1] {ECO:0000313|EMBL:EED83739.1, ECO:0000313|Proteomes:UP000001743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44394 / Madison 698-R {ECO:0000313|Proteomes:UP000001743};
RX PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA Brettin T., Rokhsar D., Berka R., Cullen D.;
RT "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT placenta supports unique mechanisms of lignocellulose conversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
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DR EMBL; EQ966262; EED83739.1; -; Genomic_DNA.
DR RefSeq; XP_002471082.1; XM_002471037.1.
DR AlphaFoldDB; B8P5V7; -.
DR KEGG; ppl:POSPLDRAFT_95611; -.
DR HOGENOM; CLU_014001_1_0_1; -.
DR InParanoid; B8P5V7; -.
DR OMA; RITWIID; -.
DR OrthoDB; 878418at2759; -.
DR Proteomes; UP000001743; Unassembled WGS sequence.
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; IPR036273; CRAL/TRIO_N_dom_sf.
DR PANTHER; PTHR45824; GH16843P; 1.
DR PANTHER; PTHR45824:SF6; GH16843P; 1.
DR Pfam; PF00650; CRAL_TRIO; 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 Reference proteome {ECO:0000313|Proteomes:UP000001743}.
FT DOMAIN 100..253
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 273..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 306 AA; 35683 MW; B9FCAC84C59DD296 CRC64;
MGKTHQVLTA PAPATEIGPV RTYTAEQQDK IRALREYADT LLLPESDSYH EWEKRWLDRW
DTVPRYMRAA KWHLDDGKRR IKGTLEWRRE FKPDLIPPDE VRIESETGKI ILNGFDNQGR
PILYMRPGRE NTETSPRQLR HLVWCLERAK DFMPPGQDSL VIIVDYKSTT LRTNPSISVA
RKVLTILQQH YVETLGRALV VNLPVLLNFF YKGIAPFLDP ITRDKMRFNP DLFELIPKEQ
LDADFGGDFE YEFEPVSYWE QVVSHCRIAS DGTRVEEHEH EQGERPADRE AEKADMSTDE
VDSPYV
//
