ID A0A1L9X8R5_ASPA1 Unreviewed; 543 AA.
AC A0A1L9X8R5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN ORFNames=ASPACDRAFT_74394 {ECO:0000313|EMBL:OJK04823.1};
OS Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=690307 {ECO:0000313|EMBL:OJK04823.1, ECO:0000313|Proteomes:UP000184546};
RN [1] {ECO:0000313|Proteomes:UP000184546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 16872 / CBS 172.66 / WB 5094
RC {ECO:0000313|Proteomes:UP000184546};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC ECO:0000256|RuleBase:RU000647}.
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DR EMBL; KV878970; OJK04823.1; -; Genomic_DNA.
DR RefSeq; XP_020061162.1; XM_020204204.1.
DR AlphaFoldDB; A0A1L9X8R5; -.
DR STRING; 690307.A0A1L9X8R5; -.
DR GeneID; 30978018; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_74394; -.
DR OMA; KSQQTHK; -.
DR OrthoDB; 1453907at2759; -.
DR Proteomes; UP000184546; 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:UP000184546}.
FT DOMAIN 384..523
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 245..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..275
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..303
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 58234 MW; 362E935C40E1B01A CRC64;
MASGSHMHNL TTLIKRLEAA TSRLEDMAMS LDDPNSPKTI GAIAAPETAT PETPKAAPPA
TPAAPPVPPQ IQDFDTLING DVRTFVELGQ KINGLVGEQS RAVQQAFEAE RTYLYVSTKA
KKPDQQPPEL MTELHNASDS INNIRESNRA SHLFNHLSAV AEGIVALGWF FASKPADFVT
EIVGGIEYYG NKVLKDYKEK DRTHVQYIQA YYQIFKSLAA YLKKHYPKGL TWNDQDGIDA
QEALRQVKSG SSSASFPSES RSAPPPPPPP PVPTINVSGG NGGAPPPPPP PPGVPPPPSS
APGSSPDMSA VFDQLNRGNA VTSGLRKVDK SEMTHKNPSL RTSSVVPERP SSQGSSVSSP
TSRARSPAPP STKPKPESMR SRKPPRKDLE GNKWLVEHFD NPGGIVEINA QQNQSILISR
CNKTIIKVSN KANAISIDNC TGLSIIVDSL VSSLDVIKSA KFALQIDGVV PTLLLDQVDG
ATVYLGQQSL ATEVFSSKST AINVMLPPKE GTDDDTKECP LPEQIKSYVK DGVLVSEIVE
HAG
//
