ID A0A1R3HVI0_COCAP Unreviewed; 472 AA.
AC A0A1R3HVI0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN ORFNames=CCACVL1_16851 {ECO:0000313|EMBL:OMO74274.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO74274.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO74274.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO74274.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC ECO:0000256|RuleBase:RU000647}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO74274.1}.
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DR EMBL; AWWV01011125; OMO74274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3HVI0; -.
DR STRING; 210143.A0A1R3HVI0; -.
DR EnsemblPlants; OMO74274; OMO74274; CCACVL1_16851.
DR Gramene; OMO74274; OMO74274; CCACVL1_16851.
DR OMA; KSQQTHK; -.
DR OrthoDB; 1453907at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000188268}.
FT DOMAIN 312..449
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 214..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 50597 MW; 196E0CCCEA02034F CRC64;
MEGKLIERLE AAVARLEALS AGGGVSSRDL PDIGVDVSSD PSIVAFDDLM AQYASKLSAA
AEKIGGQVLD VTKILIEAFS VQKKLLMEIK QTQKPDMAGL AGFLKPLNEV IMKANAMTEG
RRSDFFNHLK SAGDSLAALA WIAYTGKDCG MSMPIAHVEE SWQMSEFYCN KVLVEYKNKD
PNHVEWAKAL KELYLPGLRD YVKSHYPLGP VWSASGKKAS SAPPKAPPGA PAPPPPPPAS
LFSSEPSQPS SSRPKEGMSA VFSEINSGNV TAGLKKVTAD MKSKNRADRT GVVSASEKEP
RSSPSSFSKA GPPKFELQMG RKWVVENQIG RKNLVIDECD SKQSVYVYGC KDSVLQIQGK
VNNITIDKCT KMGVVFKDVV AACEIVNCNG VEVQCQGSAP TISVDNTSGC QLYLSKDSLG
ASITTAKSSE INVLVPAADS DGDWAEHALP QQYIHTFKDG QFETTSISHS GG
//
