ID A0A0E0DZ48_9ORYZ Unreviewed; 389 AA.
AC A0A0E0DZ48;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DUF4005 domain-containing protein {ECO:0000259|Pfam:PF13178};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI06G09120.3};
RN [1] {ECO:0000313|EnsemblPlants:OMERI06G09120.3}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI06G09120.3};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI06G09120.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: May be involved in cooperative interactions with calmodulins
CC or calmodulin-like proteins (By similarity). Recruits calmodulin
CC proteins to microtubules, thus being a potential scaffold in cellular
CC signaling and trafficking (By similarity). May associate with nucleic
CC acids and regulate gene expression at the transcriptional or post-
CC transcriptional level. {ECO:0000256|ARBA:ARBA00024682}.
CC -!- SUBUNIT: Binds to multiple calmodulin (CaM) in the presence of Ca(2+)
CC and CaM-like proteins. {ECO:0000256|ARBA:ARBA00024378}.
CC -!- SIMILARITY: Belongs to the IQD family. {ECO:0000256|ARBA:ARBA00024341}.
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DR AlphaFoldDB; A0A0E0DZ48; -.
DR STRING; 40149.A0A0E0DZ48; -.
DR EnsemblPlants; OMERI06G09120.3; OMERI06G09120.3; OMERI06G09120.
DR EnsemblPlants; OMERI06G09120.4; OMERI06G09120.4; OMERI06G09120.
DR Gramene; OMERI06G09120.3; OMERI06G09120.3; OMERI06G09120.
DR Gramene; OMERI06G09120.4; OMERI06G09120.4; OMERI06G09120.
DR eggNOG; ENOG502QVYZ; Eukaryota.
DR Proteomes; UP000008021; Chromosome 6.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.190; -; 1.
DR InterPro; IPR025064; DUF4005.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR32295; IQ-DOMAIN 5-RELATED; 1.
DR PANTHER; PTHR32295:SF108; PROTEIN IQ-DOMAIN 20; 1.
DR Pfam; PF13178; DUF4005; 1.
DR Pfam; PF00612; IQ; 2.
DR SMART; SM00015; IQ; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 2.
PE 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021}.
FT DOMAIN 271..353
FT /note="DUF4005"
FT /evidence="ECO:0000259|Pfam:PF13178"
FT REGION 34..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 43636 MW; E8D0A46E68D26FE0 CRC64;
MLLVLQKRNH SGMGRVIRWL KKLLTGRKEA HKGLKENHAV SDGAEKETSR WSFAKHRRSG
VDSGRRPSEA ALAAVAAVAA EPSEVRRPCH CGEVENAIAW REKAAMVIQK AYRGYLARKA
LRALRSLVKL QALVRGYLVR KQAATTLHRL QALMRLQASS RAATRASYRK SMEQERISVE
ETRLKTTTPG HRRRLSDSAD SNYERSPRIV EMDTCHRLSR SSRIAIRHSR DHSSDCLTPA
PMPPPLSCSS PISIKQPPRL SIQRSQHHER DTRHAKTAHN TPRLGAPPYG SSPANKSVDG
MARARLSHRD ALVSPRYMAG TASSAARTRC QSAPRQRQAA EAPARSRRSC SRTTQDSGFC
FECSEDSRPG YSEELSDEAA RDYYLDRMW
//
