ID A0A0D9WFC1_9ORYZ Unreviewed; 431 AA.
AC A0A0D9WFC1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=CRAL-TRIO domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR05G09880.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR05G09880.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR05G09880.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR05G09880.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the patellin family.
CC {ECO:0000256|ARBA:ARBA00007155}.
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DR AlphaFoldDB; A0A0D9WFC1; -.
DR STRING; 77586.A0A0D9WFC1; -.
DR EnsemblPlants; LPERR05G09880.1; LPERR05G09880.1; LPERR05G09880.
DR Gramene; LPERR05G09880.1; LPERR05G09880.1; LPERR05G09880.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_023762_0_1_1; -.
DR Proteomes; UP000032180; Chromosome 5.
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 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; PATELLIN-1; 1.
DR PANTHER; PTHR45932:SF4; PATELLIN-6; 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:UP000032180}.
FT DOMAIN 143..317
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 293..428
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 47671 MW; BC2ED72404E8EEF7 CRC64;
MSPTATPSPA PAAAAPKSQP PPPPSSGAKR SLMSSLMEAT ALLRSSSFKE DSYVASALPA
SDLRALADLR ALLSTHPDPI SIWGVPLNPT PGCGEEDAAA DERADVVLLK FLRARDFRVR
DAHAMLLRCA AWRAEFRADA VVDEDLGFKD LEGVVAYMHG WDREGHPVCY NAYGVFKDRD
MYDRVFGDGE RLARFLRWRV QVMERGVRAL HLRPGGVNAI IQVTDLKDMP KRELRAASNQ
ILSLFQDNYP EMVARKVFIN VPWYFSVLFA MISPFLTERT KSKFVIAREG NVAETLFKFI
RPELVPVQYG GLSRTGDLEN GPPKPASEFT IKGGEKVFLE IDGIEAGATI TWDLVVGGWD
LEYGAEYVPA AEDSYTLCVE RTRKVPAAAD EPVHNAFTAR EAGKMVLSID NSGSRKRKVA
AYRYFVRKPS A
//
