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Database: UniProt
Entry: G3AHT7_SPAPN
LinkDB: G3AHT7_SPAPN
Original site: G3AHT7_SPAPN 
ID   G3AHT7_SPAPN            Unreviewed;       527 AA.
AC   G3AHT7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN   ORFNames=SPAPADRAFT_59677 {ECO:0000313|EMBL:EGW34251.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW34251.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC       ECO:0000256|RuleBase:RU000647}.
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DR   EMBL; GL996500; EGW34251.1; -; Genomic_DNA.
DR   RefSeq; XP_007373835.1; XM_007373773.1.
DR   AlphaFoldDB; G3AHT7; -.
DR   STRING; 619300.G3AHT7; -.
DR   GeneID; 18873019; -.
DR   KEGG; spaa:SPAPADRAFT_59677; -.
DR   eggNOG; KOG2675; Eukaryota.
DR   HOGENOM; CLU_015780_1_0_1; -.
DR   InParanoid; G3AHT7; -.
DR   OMA; KSQQTHK; -.
DR   OrthoDB; 1453907at2759; -.
DR   Proteomes; UP000000709; 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:UP000000709}.
FT   DOMAIN          367..505
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          44..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..281
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  57483 MW;  013A443F64D4BB73 CRC64;
     MSTEEGQYNV QGYNIVTILK RLEAATSRLE DITLYQEEAN KKRIANEPKT SIDSSSSMQT
     TQSNPEEKPK SIPEEKPKSV VVFEQFISDH VVPFADTSKS IDSVIGDAAQ LLVEAFKSQS
     SFLEIVSKSK KPDMNDPTFL KVLEPMNKRI NSIIEIKEAN RTSPFFNHLN TISEGVPVLG
     WIVSDTPVSL IPEFKDSSKF WSDRVLKEYK QKDEKHVDWV NKFMAIFDEL KNYVKEYHAT
     GPSWNSKGSH LEEVVKSQQP ATEGGAPPPP PPPPPPPPAN LFDDTSSAKS APAPAGGINA
     VFAELNKGSD ITAGLKKVDK SEMTHKNPEL RKQPPVAPKK PQSLSSRASD APAAAAAAAA
     PTPAAKPPKK ELVDGTKWVI QNYTKLDASE PIIIAVEMHQ SVFIGNCQDI TIQLQGKANA
     VSLSETKNVG LVIDSLISGV DVIKSIKFGL QVTGFVPMIS IDKSDEGTVY LSKESVDGDI
     QVFTSSTTAL NINVPIEDDY SELAVPEQFV HRVKNGKLVS EIVEHAG
//
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