ID A0A5N7D5U5_9EURO Unreviewed; 398 AA.
AC A0A5N7D5U5;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 22-FEB-2023, entry version 9.
DE SubName: Full=Adenylate cyclase associated N terminal-domain-containing protein {ECO:0000313|EMBL:KAE8401766.1};
GN ORFNames=BDV37DRAFT_253882 {ECO:0000313|EMBL:KAE8401766.1};
OS Aspergillus pseudonomiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1506151 {ECO:0000313|EMBL:KAE8401766.1, ECO:0000313|Proteomes:UP000325579};
RN [1] {ECO:0000313|EMBL:KAE8401766.1, ECO:0000313|Proteomes:UP000325579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119388 {ECO:0000313|EMBL:KAE8401766.1,
RC ECO:0000313|Proteomes:UP000325579};
RG DOE Joint Genome Institute;
RA Mondo S., Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Riley R.,
RA Salamov A., Simmons B.A., Magnuson J.K., Henrissat B., Mortensen U.H.,
RA Larsen T.O., Devries R.P., Grigoriev I.V., Machida M., Baker S.E.,
RA Andersen M.R., Cantor M.N., Hua S.X.;
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659}.
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DR EMBL; ML736796; KAE8401766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N7D5U5; -.
DR OrthoDB; 1453907at2759; -.
DR Proteomes; UP000325579; 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; 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:UP000325579}.
FT DOMAIN 239..378
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 118..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 42925 MW; 4EA7FF521AA551ED CRC64;
MTELHTASDS INMIRESNRA SPLFNHLSAV AEGIVALGWF FESKPGDFVS EIVGGIEYYG
NKVLKEYKEK DKTHVQYIQS YYQVFKSLAA YLKKHYPKGL TWNEQNGIDA LEALRQVKGG
PSTGASGSAP PPPPPPPVPT LNVPGGAPPP PPPPPGVPPP PSAAPGGDMS AVFAQLNQGE
AITSGLRKVD KSEMTHKNPS LRASSTVPER PDSQGSISRS KSPAPSKKPK PESMRVRKPP
RKELESNKWY IENFDNAGEI VEIPAQQNQS ILISRCNKTI VKVSSKANAI AIDNCKELSI
IVDSLVSSLD VIKCTKFALQ IDGVAPTLLL DQVDGATVYL GPQSLNTEVF SSKCTAINIM
LPPKEGTDED TKECPVPEQI KSYVKDGVLV NEIVEHAG
//
