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Database: UniProt
Entry: A0A1R1Y9R2_9FUNG
LinkDB: A0A1R1Y9R2_9FUNG
Original site: A0A1R1Y9R2_9FUNG 
ID   A0A1R1Y9R2_9FUNG        Unreviewed;       514 AA.
AC   A0A1R1Y9R2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   SubName: Full=Adenylyl cyclase-associated protein {ECO:0000313|EMBL:OMJ23600.1};
GN   ORFNames=AYI70_g2167 {ECO:0000313|EMBL:OMJ23600.1};
OS   Smittium culicis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX   NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ23600.1, ECO:0000313|Proteomes:UP000187283};
RN   [1] {ECO:0000313|EMBL:OMJ23600.1, ECO:0000313|Proteomes:UP000187283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSMNP {ECO:0000313|EMBL:OMJ23600.1,
RC   ECO:0000313|Proteomes:UP000187283};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659}.
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:OMJ23600.1}.
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DR   EMBL; LSSN01000511; OMJ23600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1Y9R2; -.
DR   STRING; 133412.A0A1R1Y9R2; -.
DR   Proteomes; UP000187283; 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; 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; 1.
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:UP000187283}.
FT   DOMAIN          354..492
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          35..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..284
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  56464 MW;  3C79FBB7AD485ECD CRC64;
     MEQLNTAGAS GPNLISRLKQ ATSKLQTIAT TLVHAKPESQ AHPETHSSDA AEVASSAPQA
     VLVTNIKEVD EYAKRLNEAV SEFQAVCQQL EDPALLEMAQ LVQELTDNQA KLIQAAAQTQ
     KPAIPEFQKM LARIQASLES ISNLKNSNRR SKLFNNFSAI SEGVAAYGWV AIEKTPMGYI
     TDMKESSQFY TNRVLKEFRE SNPIQVEFVK KFLHIIEQLF LYVKMYHTTG LKFGYSRPLL
     TSDQAIEFIN SSPENAHNVA NNSSNSAGGP PPPPPPPPPP VFDDAPMNSD TSSSKPMTGG
     INALFSEINQ GEGITKNLKK VDKNAPKPPP TSSQPLEPKP IGKYKNSLST PSLPPKKELN
     GKRWAIENFV NEEISLEITD ITQTVYIYNC TGCTISISNK LNNLSIDKCS KSGIIFDAVV
     SSCDLINSQS IKLQPNLAIP LINIDKSNGV QLFLNDSNKD SIEILTAKSS EINVCYTDHT
     SEDAYDYREF FVPEQMKTTV VDGKLITTVL EHNG
//
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