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Database: UniProt
Entry: I1HJ52_BRADI
LinkDB: I1HJ52_BRADI
Original site: I1HJ52_BRADI 
ID   I1HJ52_BRADI            Unreviewed;       601 AA.
AC   I1HJ52;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=CRAL-TRIO domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=100843560 {ECO:0000313|EnsemblPlants:KQK06105};
GN   ORFNames=BRADI_2g24430v3 {ECO:0000313|EMBL:KQK06106.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK06106.1};
RN   [1] {ECO:0000313|EMBL:KQK06106.1, ECO:0000313|EnsemblPlants:KQK06105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK06106.1,
RC   ECO:0000313|EnsemblPlants:KQK06105};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQK06106.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK06106.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQK06105}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK06105};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the patellin family.
CC       {ECO:0000256|ARBA:ARBA00007155}.
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DR   EMBL; CM000881; KQK06105.1; -; Genomic_DNA.
DR   EMBL; CM000881; KQK06106.1; -; Genomic_DNA.
DR   RefSeq; XP_003568396.1; XM_003568348.3.
DR   RefSeq; XP_014755245.1; XM_014899759.1.
DR   AlphaFoldDB; I1HJ52; -.
DR   STRING; 15368.I1HJ52; -.
DR   EnsemblPlants; KQK06105; KQK06105; BRADI_2g24430v3.
DR   EnsemblPlants; KQK06106; KQK06106; BRADI_2g24430v3.
DR   GeneID; 100843560; -.
DR   Gramene; KQK06105; KQK06105; BRADI_2g24430v3.
DR   Gramene; KQK06106; KQK06106; BRADI_2g24430v3.
DR   KEGG; bdi:100843560; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   HOGENOM; CLU_023762_1_0_1; -.
DR   InParanoid; I1HJ52; -.
DR   OMA; NHEFSAP; -.
DR   OrthoDB; 53323at2759; -.
DR   Proteomes; UP000008810; Chromosome 2.
DR   ExpressionAtlas; I1HJ52; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:SF1; OS05G0429400 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:UP000008810}.
FT   DOMAIN          312..487
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000259|PROSITE:PS50191"
FT   DOMAIN          493..594
FT                   /note="GOLD"
FT                   /evidence="ECO:0000259|PROSITE:PS50866"
FT   REGION          21..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..238
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   601 AA;  65646 MW;  2E0FD2C7EE0BD2D3 CRC64;
     MAEETKQETA AAAAELVATE AEKKAEVEEK VDEAAAAAAE EAEEEKKIEE AETEAGAEEA
     AVIEGSTGSF KEESNLVSEL ADPEQKALAQ LKELIAAALA SGEFDLPPPP PPVQPDTATP
     AADDAKTEEA EEPKAEEAAK SDAAPEGEEP KAEEAEVSEP KTEAPAPEEP KTDDPAQEEP
     KTVEPTKEEP NTEAPVVAAA EQPKAVAAAE EAKPAEPTPE TEEKTVVVTE EEGTKAVEAT
     EETAVPAASE PEAAPAAELI WGVPLVGDDE RTDTVLLKFL RAREFKVKEA MAMLKAAVLW
     RKSFGIDALL GTDLGVPELE NVVFYRGADR EGHPVCYNVY SEFQDKELYE KAFGDDEKRE
     RFLKWRIQLL ERGILEQLDF SPSGICSMVQ VTDLKNSPPM LGKHRAVTRQ ALSLLQDNYP
     EFIAKKVFIN VPWWYLAANK MMSPFLTQRT KSKFTFCSPA KTAETLFRYI APEQVPVQFG
     GLFKEDDTEF STSDAVTELT VKPSSKETIE IPATENSTVV WELRVLGWEV SYGVEFTPDA
     EGGYTVIVQK TRKVPANEEP IMKGNFKVTE PGKVVLAVNN PTSKKKKLLY RLKVKSSTES
     A
//
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