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Database: UniProt
Entry: A0A094CK99_9PEZI
LinkDB: A0A094CK99_9PEZI
Original site: A0A094CK99_9PEZI 
ID   A0A094CK99_9PEZI        Unreviewed;       551 AA.
AC   A0A094CK99;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 32.
DE   RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN   ORFNames=V493_06169 {ECO:0000313|EMBL:KFY22982.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY22982.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY22982.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC       ECO:0000256|RuleBase:RU000647}.
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:KFY22982.1}.
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DR   EMBL; JPJV01002336; KFY22982.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094CK99; -.
DR   STRING; 1420906.A0A094CK99; -.
DR   HOGENOM; CLU_015780_1_0_1; -.
DR   OrthoDB; 1453907at2759; -.
DR   Proteomes; UP000029327; 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:UP000029327}.
FT   DOMAIN          393..528
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          24..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..286
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..304
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..396
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  59183 MW;  C39ED64A0B591BBB CRC64;
     MSANMNNMTT LIKRLEAATS RLEDLVTPAF EDPAGTTPKE NSSNSTTTRS NPVSEGNSPE
     HAVPAPPAAA AAASTVSPPK PAEDPVPESV EDFDTFLNTS VKKYVDLSNE IGGAIAAQAA
     RVAQVFQNER TLLLISTMSK KPESAGSDYM ELLKPLQQEI RTVIDVKESN RGSELINQLS
     AVAESIGVIA WVTMDNKPFK HVDDSLGSAQ YFGNRVLKEF KEKDPKQVQW IQSYYQIFKD
     LSEYVKNTFP HGLTWNANGV SPKEAMKIVN SPSSSPSTTT TTSAGAGGSP PPPPPPPPPG
     PAPKLDIKEA AKPAAAVGGI GAVFSELNKG DSVTKGLKKV SADEMTHKNP SLRASSLVPD
     RSESLSPTSS INRNKSPAPR KTPKPESLRT KKPPKKELDG NKWIIEHYDN ESEPIEIEAS
     ISQSILISRC SKTTIRIIGK ANAISIDNSP RLSLVIDSLV SSVDVIKSSN FALQVLGTLP
     TILLDQVDGA QVYLGKDSMN TEVFSSKCSS INLNIISGED EDYKEVALPE QIRTYIGNNG
     QLISEIVEHA G
//
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