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Database: UniProt
Entry: A0A179UAH3_BLAGS
LinkDB: A0A179UAH3_BLAGS
Original site: A0A179UAH3_BLAGS 
ID   A0A179UAH3_BLAGS        Unreviewed;       504 AA.
AC   A0A179UAH3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   02-APR-2025, entry version 33.
DE   RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN   ORFNames=BDBG_00887 {ECO:0000313|EMBL:OAT04308.1};
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT04308.1, ECO:0000313|Proteomes:UP000002038};
RN   [1] {ECO:0000313|Proteomes:UP000002038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC       ECO:0000256|RuleBase:RU000647}.
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DR   EMBL; GG657449; OAT04308.1; -; Genomic_DNA.
DR   RefSeq; XP_002627979.1; XM_002627933.1.
DR   AlphaFoldDB; A0A179UAH3; -.
DR   STRING; 559298.A0A179UAH3; -.
DR   GeneID; 8507298; -.
DR   KEGG; bgh:BDBG_00887; -.
DR   VEuPathDB; FungiDB:BDBG_00887; -.
DR   OrthoDB; 77251at2759; -.
DR   Proteomes; UP000002038; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0008179; F:adenylate cyclase binding; IEA:TreeGrafter.
DR   GO; GO:0007015; P:actin filament organization; IEA:TreeGrafter.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IEA:TreeGrafter.
DR   FunFam; 2.160.20.70:FF:000008; Adenylyl cyclase-associated protein; 1.
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; IPR053950; CAP_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; PF21938; CAP_N; 1.
DR   Pfam; PF01213; CAP_N-CM; 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:UP000002038}.
FT   DOMAIN          345..482
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          26..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..57
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..71
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..257
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..267
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   504 AA;  53856 MW;  9A94ABCDE88BE172 CRC64;
     MTTNQMNNFT TLIKRLEAAT SRLEDMATSL EGSGPGSPAA DGIATSTASV SSKTASSPLP
     PPPPVVEPPP RQIEDFDALI NKEVKNFVEL SEKLGEPAGE QSKAILRAFQ AERTYLYIAL
     KAKKPDQQSP DLLSDLRKAS DEINNIREAN RPSPLFNHLS AVAEGVVSLG WFFEPRPAEF
     VRESVAGAQF YGDRVLREYK GKALSEWPDM EQPGWSRRNG GPETAPIRFT DASAFPPPPP
     PPAAGAGGPP PPPPPPASVA APPKAAPTGD MSSVFEQLNQ GSAVTSGLRK VDKSEMTHKN
     PGLRAGSLVP ERADSRTGVT SPTSRGKSPV PSKKPKPESM RAKKPSRKQL DGNKWYIEHY
     DSPSDIIEIP AQLSHSILIS HCNKAIVKIN GKANAISIDN CTGLSVIVDS LVSSVDVIKS
     PKFALQIDGV VPTILLDQVD GASLYLSQES LNTEVFSSKS SNVNIVVPPK EGTDDDSKEL
     PVPEQIRTVI KNGAAVSEIV EHAG
//
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