ID   I1T3W6_GOSDA            Unreviewed;       445 AA.
AC   I1T3W6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
OS   Gossypium darwinii (Darwin's cotton) (Gossypium barbadense var. darwinii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=34276 {ECO:0000313|EMBL:AEN70778.1};
RN   [1] {ECO:0000313|EMBL:AEN70778.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22381639; DOI=10.1016/j.ympev.2012.01.025;
RA   Zhu H., Lv J., Zhao L., Tong X., Zhou B., Zhang T., Guo W.;
RT   "Molecular evolution and phylogenetic analysis of genes related to cotton
RT   fibers development from wild and domesticated cotton species in
RT   Gossypium.";
RL   Mol. Phylogenet. Evol. 63:589-597(2012).
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC       ECO:0000256|RuleBase:RU000647}.
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DR   EMBL; JF722077; AEN70778.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1T3W6; -.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
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; IPR013992; Adenylate_cyclase-assoc_CAP_N.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR036223; CAP_C_sf.
DR   InterPro; IPR018106; CAP_CS_N.
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   Pfam; PF01213; CAP_N; 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.
DR   PROSITE; PS01088; CAP_1; 1.
PE   3: Inferred from homology;
FT   DOMAIN          312..445
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          219..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..243
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  47728 MW;  5DA92C19D6F37DAA CRC64;
     MEAKLIERLE AAVARLESLS AGGISARGLP DGVDEVSSDP SILAFDDLMA QYAARVSAAA
     EKIGGQVLDV TKLVLEAFSV QKKLLIEIEQ TQKPDMAGLV EFLKPLNEVI LKVNAMTEGR
     RSDFFNHLKS AGDSLSALAW IAYTGKDCGM SMPIAHVEES WQMAEFYNNK VLVEYRNKDQ
     IHVEWAKALK ELYLPGLRDY VKSHYPLGPV WSASGKKASS ALSKAPPPGA PAPPPPPPAS
     LFSSEPSQPS SSNPKQGMSA VFQEISSGNV SVGLKKVTAD MKTKNRTDRT GVVSASGKET
     HSSSPSFSKA GPPKLELQMG RKWAVENQIG RKNLVIDDCD AKQSVYIYGC KDSVLQIQGK
     VNNITIDKCT KMGVVFKDVV AACEVVNCNG VEVQCQGSAP TISVDNTSGC QLYLSKDSLG
     TSITTAKSSE INVLMPTGPD GDWVS
//