ID M2PQH0_CERS8 Unreviewed; 357 AA.
AC M2PQH0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE RecName: Full=CRAL-TRIO domain-containing protein {ECO:0000259|PROSITE:PS50191};
GN ORFNames=CERSUDRAFT_112536 {ECO:0000313|EMBL:EMD38799.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD38799.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD38799.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD38799.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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DR EMBL; KB445794; EMD38799.1; -; Genomic_DNA.
DR AlphaFoldDB; M2PQH0; -.
DR STRING; 914234.M2PQH0; -.
DR HOGENOM; CLU_045138_0_0_1; -.
DR OrthoDB; 53323at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
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 InterPro; IPR044834; PATL.
DR PANTHER; PTHR45932:SF17; CRAL-TRIO DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45932; PATELLIN-1; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; 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 Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT DOMAIN 190..357
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 357 AA; 38826 MW; 21E8D18FAA220C66 CRC64;
MSEPTHEPTT AAPEPTLAIA TDAAPAAEAA TTAASAPEPT SVEPTKTTET TATTTEAAPP
LEPAQLAEPT VAAVPAPTSD QPFQDTVPVP TDDPQNALTE KFTEPERAAL KELRAQLSEA
IAGAVTDRES VTLWGVPLSG DAPATDARVS VVLMKFLRAR DLDVEAARKM LSDTLKWREE
FKVDEVTKAE YDEETFGGVG KIFGHDKDGR PVVYNLYGGN KKAFGNVEEF IRWRVAFMEK
CIAELDFVTQ DQMVQIHDYD GVPMIFGRDA NQKAAAAQAT KIFQDYYPEF LYRKFFVNVP
SLLTWVFWMF KPLMPAKTLS KMSMIGSGPS TIGAAVLPVI DAAELPKRYG GQASDFA
//
