ID A0A058ZYW6_EUCGR Unreviewed; 224 AA.
AC A0A058ZYW6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Calcineurin B-like protein {ECO:0000256|RuleBase:RU369080};
GN ORFNames=EUGRSUZ_K00380 {ECO:0000313|EMBL:KCW46556.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW46556.1};
RN [1] {ECO:0000313|EMBL:KCW46556.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW46556.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a calcium sensor. CBL proteins interact with CIPK
CC serine-threonine protein kinases. Binding of a CBL protein to the
CC regulatory NAF domain of a CIPK protein lead to the activation of the
CC kinase in a calcium-dependent manner. {ECO:0000256|RuleBase:RU369080}.
CC -!- SUBUNIT: Homodimer. Interacts with CIPK.
CC {ECO:0000256|RuleBase:RU369080}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU369080}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000256|ARBA:ARBA00023774, ECO:0000256|RuleBase:RU369080}.
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DR EMBL; KK198763; KCW46556.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A058ZYW6; -.
DR STRING; 71139.A0A058ZYW6; -.
DR EnsemblPlants; KCW46556; KCW46556; EUGRSUZ_K00380.
DR Gramene; KCW46556; KCW46556; EUGRSUZ_K00380.
DR eggNOG; KOG0034; Eukaryota.
DR InParanoid; A0A058ZYW6; -.
DR OMA; YRGFKNX; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019900; F:kinase binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:UniProtKB-UniRule.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR045198; CNBL1-10.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR23056; CALCINEURIN B; 1.
DR PANTHER; PTHR23056:SF110; CALCINEURIN B-LIKE PROTEIN 4; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR PRINTS; PR00450; RECOVERIN.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU369080};
KW Membrane {ECO:0000256|RuleBase:RU369080};
KW Metal-binding {ECO:0000256|RuleBase:RU369080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369080}.
FT DOMAIN 67..102
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 104..139
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 148..183
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 224 AA; 25762 MW; 70D537544EE6F62B CRC64;
MGCIISKNSE QTPGYEEPNV LAAATPFTAG EVKALYVLFK KLSSSIVADG LIHKEEFQLA
LFRNRNCRNL FADRIFDLFD MKGNGVIEFG EFVRSLGIFH PNAPIEEKIA FAFRLYDLRH
TGYIEREELK EMVLALLHES DLELSEDVVE TIVDKAFREA DTKDDGRIDR EEWEDFVSKN
PSLIRNMTLP YLKYVSPIEI NILVTSMWRA ASLLQNLNPL QRKR
//
