ID B9RER0_RICCO Unreviewed; 415 AA.
AC B9RER0;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Calmodulin binding protein, putative {ECO:0000313|EMBL:EEF49681.1};
GN ORFNames=RCOM_1427840 {ECO:0000313|EMBL:EEF49681.1};
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}.
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DR EMBL; EQ973777; EEF49681.1; -; Genomic_DNA.
DR RefSeq; XP_002512229.1; XM_002512183.2.
DR AlphaFoldDB; B9RER0; -.
DR STRING; 3988.B9RER0; -.
DR GeneID; 8289354; -.
DR KEGG; rcu:8289354; -.
DR eggNOG; ENOG502S0AM; Eukaryota.
DR InParanoid; B9RER0; -.
DR OrthoDB; 546056at2759; -.
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:SF263; DUF4005 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR32295; IQ-DOMAIN 5-RELATED; 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 274..351
FT /note="DUF4005"
FT /evidence="ECO:0000259|Pfam:PF13178"
FT REGION 313..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 47404 MW; 0D5D2EAAE82E0C42 CRC64;
MGKASRWIMN FLVGKKEEKE KRKNITFYED YMRTPNGSIP STPNYKRRWS FGKSSGREKV
NKNSKSLDAI TPLITQHAAS LEWENRQNRN KTVAAVPAPA EAIKRVVATR EDRIIRSVEE
AAATRIQAAY RSYLARRALC ALRALVKLQA LVRGHLVRRQ TAATLQQMQA LMAIQVRARC
QRIQMAKESA QLVVRSLSSR HGNFPLDSEL RGALKEVMDL NVYETKRVLK DDHGYLDHPQ
MGRREHGKTK YYSGEIYISK RKDQYEEFSF PTVLNSPENY SPSPVAIRGR ASFTYQKPDY
MQPICHPNYM ANTESSRAKV RSQSEPKQRP KGSMRPEGKG TAPMNGSNAQ QDGRLQGSSS
YSMSLAYENR DPWLTKVFQS SRHEDCEYDA KSKARSSYSN CNKLLAACEP HLYLY
//
