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Database: UniProt
Entry: A0A0C3JBG9_PISTI
LinkDB: A0A0C3JBG9_PISTI
Original site: A0A0C3JBG9_PISTI 
ID   A0A0C3JBG9_PISTI        Unreviewed;       535 AA.
AC   A0A0C3JBG9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   28-JUN-2023, entry version 27.
DE   RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN   ORFNames=M404DRAFT_999083 {ECO:0000313|EMBL:KIO06428.1};
OS   Pisolithus tinctorius Marx 270.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO06428.1, ECO:0000313|Proteomes:UP000054217};
RN   [1] {ECO:0000313|EMBL:KIO06428.1, ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|EMBL:KIO06428.1,
RC   ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC       ECO:0000256|RuleBase:RU000647}.
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DR   EMBL; KN831963; KIO06428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3JBG9; -.
DR   STRING; 870435.A0A0C3JBG9; -.
DR   HOGENOM; CLU_015780_1_0_1; -.
DR   InParanoid; A0A0C3JBG9; -.
DR   OrthoDB; 1453907at2759; -.
DR   Proteomes; UP000054217; 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; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054217}.
FT   DOMAIN          376..513
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          48..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..304
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   535 AA;  57230 MW;  2C491A32C62C8DB6 CRC64;
     MSLDAYARVP LESFTDHTAM SNTNQGLYTL ATIIKRLEAV ASRFEDLEET TRSRTSKRQS
     TSTVTDVPEA QAVHSPRLEP LVPPAVVIQP LSPPSVTAFD TIVIDGKLRA FVELTKAFAP
     QFLTDQVTLF VDELNLLRNL LLTAAACKKP DHKAFVQLLE PLQTAIESIS RAKVTHGKET
     AWVNHLSAVA ESAPCVGWVT VEPKPAAYVN DVKDSSRFFT DRVLKEYKGK DPKHTDWVRA
     LMAVLDEMKR YVLENHPVGL AWNASGVPVS EYKAPSPTPV VSGAAAPPPP PPPPPPPPPV
     EVAAAPPAVG GTAAVMAELN RGAEVTKGLR KVDKSEMTHK NPALRAGSVV PASTATSSGK
     KPVKPAKPHA LMGKKPAKFA LEGNKWLIEY QENEPALEVS GAEINQIVNI FGCKNTTVVI
     KGKVNAVTML NCTKTSVLVD SVISSVEITK SASFALQITG TAPTIQVDST DSGQIYLSKA
     CLGVEITTAK CSAINVSVPV EGEEDGIFQE QAVPEMLKTV VQNGKLVTSV VEHVG
//
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