ID A0A059AMY6_EUCGR Unreviewed; 427 AA.
AC A0A059AMY6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=C-CAP/cofactor C-like domain-containing protein {ECO:0000259|PROSITE:PS51329};
GN ORFNames=EUGRSUZ_I01265 {ECO:0000313|EMBL:KCW55347.1};
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:KCW55347.1};
RN [1] {ECO:0000313|EMBL:KCW55347.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW55347.1};
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 -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659}.
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DR EMBL; KK198761; KCW55347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059AMY6; -.
DR STRING; 71139.A0A059AMY6; -.
DR EnsemblPlants; KCW55347; KCW55347; EUGRSUZ_I01265.
DR Gramene; KCW55347; KCW55347; EUGRSUZ_I01265.
DR eggNOG; KOG2675; Eukaryota.
DR InParanoid; A0A059AMY6; -.
DR OMA; KSQQTHK; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR Gene3D; 2.160.20.70; -; 1.
DR Gene3D; 1.25.40.330; Adenylate cyclase-associated CAP, N-terminal domain; 1.
DR InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR036223; CAP_C_sf.
DR InterPro; IPR036222; CAP_N_sf.
DR InterPro; IPR006599; CARP_motif.
DR PANTHER; PTHR10652; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR10652:SF0; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1.
DR Pfam; PF08603; CAP_C; 1.
DR SMART; SM00673; CARP; 2.
DR SUPFAM; SSF69340; C-terminal domain of adenylylcyclase associated protein; 1.
DR SUPFAM; SSF101278; N-terminal domain of adenylylcyclase associated protein, CAP; 1.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE 3: Inferred from homology;
FT DOMAIN 267..404
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 170..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..196
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 45875 MW; 101E5442EBA04B8A CRC64;
MAQYVARVSS AAEKIGGRVL DVTKVVGEAF SAQKELLIQI KQTQKPDLAG LGEFLKPLNE
VIMKANALTE GRRSDFFNHL KAAADSLAAL AWIAYTGKDC GMSMPIAHVE ESWQMAEFYN
NKVLVEYRNK DPDHVEWAKA LKELYLPGLR EYVKAFYPLG PVWSPNGKVA TPAVSKAPAK
SAPAPAPPPP PPASLFSSDS PQASSSRPKQ GMAAVFQEIN SGKPVTSGLR KVTADMKTKN
RTDRTGVVGA GEKECRTASP SFSKAGPPKL ELLMGRKWAV ENQIGKKNLV IDDCDSKQTV
YVFGCKDSVL QIQGKVNNIT VDKCTKMGIV FTDVVAACEI VNCNGVEVQC QGSAPTISVD
NTAGCQLYLS KDSLGASITT AKSSEINVLV PGAEPDSDWA EHSLPQQYIH AYKDGQFVTT
PVSHSGG
//