ID A0A0D3EWV7_9ORYZ Unreviewed; 490 AA.
AC A0A0D3EWV7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=CRAL-TRIO domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART01G38960.2};
RN [1] {ECO:0000313|EnsemblPlants:OBART01G38960.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART01G38960.2};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART01G38960.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the patellin family.
CC {ECO:0000256|ARBA:ARBA00007155}.
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DR AlphaFoldDB; A0A0D3EWV7; -.
DR STRING; 65489.A0A0D3EWV7; -.
DR PaxDb; 65489-OBART01G38960-2; -.
DR EnsemblPlants; OBART01G38960.2; OBART01G38960.2; OBART01G38960.
DR Gramene; OBART01G38960.2; OBART01G38960.2; OBART01G38960.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_023762_1_0_1; -.
DR Proteomes; UP000026960; Chromosome 1.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 2.60.120.680; GOLD domain; 1.
DR Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 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; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_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; 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 SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960}.
FT DOMAIN 201..376
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 382..483
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 54100 MW; 00E3E207FD9EEC48 CRC64;
MAEEPQPEAA PAAVAATTEV AVAEKAPVEA EKEKKVEEET PAVEAEAKEE KKDEAAAAAA
AGGDEAGAIE GTGSFKEESN LVADLPDPEK KALDEPSWSP RKRRPPRRWK RSEETVVPAA
AAPAAAATEE AAAPEPEVQA AAAPEPVLIW GVPLVGDDER TDTVLLKFLR AREFKVKEAM
AMLRSAVLWR KRFGIESLLD ADLALPELDS VVFYRGADRE GHPVCYNVYG EFQDKDLYEK
AFGDEEKRER FLKWRIQLLE RGILSQLDFS PSGICSMVQV TDLKNSPPML GKHRAVTRQA
VALLQDNYPE FIAKKVFINV PWWYLAANKM MSPFLTQRTK SKFIFASPAK SAETLFRYIA
PEQVPVQFGG LFKEDDPEFT TSDAVTELTI KPSSKETVEI PVTENSTIGW ELRVLGWEVS
YGAEFTPDAE GGYTVIVQKT RKVPANEEPI MKGSFKVGEP GKIVLTINNP ASKKKKLLYR
SKVKSTSESV
//