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
//