ID B9R9F0_RICCO Unreviewed; 473 AA.
AC B9R9F0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DUF4005 domain-containing protein {ECO:0000259|Pfam:PF13178};
GN ORFNames=RCOM_1496740 {ECO:0000313|EMBL:EEF51427.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EQ973773; EEF51427.1; -; Genomic_DNA.
DR RefSeq; XP_002510825.1; XM_002510779.2.
DR AlphaFoldDB; B9R9F0; -.
DR STRING; 3988.B9R9F0; -.
DR GeneID; 8258281; -.
DR KEGG; rcu:8258281; -.
DR eggNOG; ENOG502QUBM; Eukaryota.
DR InParanoid; B9R9F0; -.
DR OrthoDB; 1130596at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
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:SF174; PROTEIN IQ-DOMAIN 24; 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:UP000008311}.
FT DOMAIN 375..433
FT /note="DUF4005"
FT /evidence="ECO:0000259|Pfam:PF13178"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 52351 MW; 8F092AA68FD90F36 CRC64;
MGLFRRLFGP KKAGSGSSPT AKDKKRWSFA RSSNTIPSLS NKRDISLSGP FDDSLDANKH
AIAVAAATAA VAEAALAAAQ AAAEVVRLTS GGGRSTTTSN VSGHVSGSHR RWQVEVAAVK
IQSAFRGYLA RRALRALKAL VKLQALVRGH IVRKQTADML RRMQTLVRVQ ARARASRSHV
SESFHTTRKS SLPHNTVPAS PHKDYHLQGY NTKFDGPSIL KRCGSNSNFR DINVMHLDEA
KLGANWLEHW MEESFYNNHG SIPMRKQHAD DERSDKILEV DTWKPHMKSQ SVGTFQMSQD
VLASEYKNQS LTTFDSPSKS STKAINQMPT VPSGEVLSLN SLKFPLGKDE AVLRTVENSP
HVFSPSSRPG SSGRRGTFTP TRSECSWGFF NGYSGYPNYM ANTESFRAKV RSQSAPRQRL
EFEKYSSSKR SVQGFYEADT ISERGFAQQT NFRNKAYPVS GRLNSRLGST DLR
//