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Database: UniProt
Entry: A1CPI6_ASPCL
LinkDB: A1CPI6_ASPCL
Original site: A1CPI6_ASPCL 
ID   A1CPI6_ASPCL            Unreviewed;       529 AA.
AC   A1CPI6;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN   ORFNames=ACLA_022710 {ECO:0000313|EMBL:EAW07557.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07557.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW07557.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC       ECO:0000256|RuleBase:RU000647}.
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DR   EMBL; DS027059; EAW07557.1; -; Genomic_DNA.
DR   RefSeq; XP_001268983.1; XM_001268982.1.
DR   AlphaFoldDB; A1CPI6; -.
DR   STRING; 344612.A1CPI6; -.
DR   EnsemblFungi; EAW07557; EAW07557; ACLA_022710.
DR   GeneID; 4700962; -.
DR   KEGG; act:ACLA_022710; -.
DR   VEuPathDB; FungiDB:ACLA_022710; -.
DR   eggNOG; KOG2675; Eukaryota.
DR   HOGENOM; CLU_015780_1_0_1; -.
DR   OMA; KPESMRA; -.
DR   OrthoDB; 1453907at2759; -.
DR   Proteomes; UP000006701; 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:UP000006701}.
FT   DOMAIN          370..509
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          29..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..71
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..294
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..376
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  56745 MW;  5E5D6DFB47736C56 CRC64;
     MASGSHMHNL TTLIKRLEAA TSRLEDMAMS LDDPHTPPKH IGAAATPEPV ASIPPKQAPA
     PPAPPAAPSL PPQIEDFDAL INGDVRSLVE LGDKIGGLVA EQSKAVLQAF EAERTYLYVS
     TKARKPTPQP PELMTELHTA SDTINNIRES NRASPLFNHL SAVAEGIVAL GWFFEPKPSE
     FVSEMIGGIE YYGNKVLKEY KEKDRTHVQY IQAYYQIYKS LAAYLKKHYP KGLTWNEESG
     IDAQEALRQI KGGAGSGRGV PPPPPPPPVP TLNVPGGVPP PPPPPPPGAP PAPAAAPADM
     SAVFAQLNQG DAITSSLRKV DKSEMTHKNP NLRTGSTVSE RPISQGSISR SKSPAPSKKP
     KPDSMRGRKP PRQELEGNKW LLENFDNPDG IIEIGAQQNQ SILISRCNKT VVKVSNKANA
     ISIDNCTGLS IIVDSLVSSL DVIKSSKFAL QIDGVVPTLL LDQVDGATVY LGSQSLGTEV
     FSSKSTAVNI MLPPKEGTDE DTKECPIPEQ IKTYIKDGVL VSEIVEHAG
//
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