ID G8Y0U3_PICSO Unreviewed; 532 AA.
AC G8Y0U3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN Name=Piso0_004936 {ECO:0000313|EMBL:CCE86446.1};
GN ORFNames=GNLVRS01_PISO0N04347g {ECO:0000313|EMBL:CCE86446.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE86446.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC ECO:0000256|RuleBase:RU000647}.
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DR EMBL; FO082046; CCE86446.1; -; Genomic_DNA.
DR AlphaFoldDB; G8Y0U3; -.
DR STRING; 559304.G8Y0U3; -.
DR eggNOG; KOG2675; Eukaryota.
DR HOGENOM; CLU_015780_1_0_1; -.
DR InParanoid; G8Y0U3; -.
DR OMA; KSQQTHK; -.
DR Proteomes; UP000005222; Chromosome N.
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; IPR028417; CAP_CS_C.
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.
DR PROSITE; PS01089; CAP_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005222}.
FT DOMAIN 372..510
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 48..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..292
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 58113 MW; 4E7407051C74FF0D CRC64;
MSGEENQFTV QGCNIVTILK RLEAATSRLE DIMVYQTQAD KAQARALQQG SVSTQAGGAP
KQLQDSTAAT EDSGSYEKSK SVIEFEKLIS DYVKTFVDKS SSIGAEVAES ANELLDAFKS
QARFLEVVSI SKKPDFSNPK FLSLLNPINS RIGKINQIKD ENRKSEFSNH LSTISEGSPM
LGWIVSETPV SLIPEFKGSA QFWSNRILKD YKEKDQKHVD WVNSFLQIID NLRSYVKEFH
ATGPSWNAHG MPLEEAISKF DTSGPAQSKP AQPEPPKGGA PPPPPPPPLP SQEFLNDSSK
STKSTPGGIN AVFADINKGE GITSGLRKVD KSEMTHKNPT LRSSEPLNKK VTPKPPKKPQ
SLSSGSVPTK KPPKKELIDD TKWIINNFTE EDVSEPITIE AEKHQSIFVG NCSGVTLNIK
GKANAISVSQ AKKTALIVDS LISGIDIIKS SKFGLQILGT VPMVNVDKSD EGSIYLSKDS
IESDVQIFSS CSTSLNINVP EKDDYEELPV PEQFKHTVKN GKLQSEVVEH KG
//
