ID D2V1W7_NAEGR Unreviewed; 495 AA.
AC D2V1W7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN ORFNames=NAEGRDRAFT_56829 {ECO:0000313|EMBL:EFC49235.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC49235.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC49235.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC ECO:0000256|RuleBase:RU000647}.
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DR EMBL; GG738848; EFC49235.1; -; Genomic_DNA.
DR RefSeq; XP_002681979.1; XM_002681933.1.
DR AlphaFoldDB; D2V1W7; -.
DR STRING; 5762.D2V1W7; -.
DR EnsemblProtists; EFC49235; EFC49235; NAEGRDRAFT_56829.
DR GeneID; 8862554; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_56829; -.
DR eggNOG; KOG2675; Eukaryota.
DR InParanoid; D2V1W7; -.
DR OMA; KSQQTHK; -.
DR OrthoDB; 1453907at2759; -.
DR Proteomes; UP000006671; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 334..472
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 226..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 495 AA; 53430 MW; A602B4E9CF1520E4 CRC64;
MSQQQLETLV SRLESAVSKL EHLKFSGASS SSDDSATGEA PSVGAFKEYL NTNVKPLVDT
CTTIGAECAK GGEFINNAFN EMLKIVTLAS NNKKPSDEEF GKILSGLAKI LKDSGDYRFK
NNKSEFYNHL YSIEEGLKCL VWPTVPAPVS YVKETVNSAQ FYNNKILMGY KNTDKVELHR
GFVSQFKTAI EELSVYVKEY HMTGLSWNAK ATTVATAAAL NGQVATPTAT PSVPSTPSVG
GGVPPPPSKI IPVSEDLIKS TSSAKQDSSS GSAGALFAEI AARKDNASVG LKHVTKDMKT
KNQTDKPPAI VPGSTTATPK SGVVGGSTAQ KKGTPKFEKD GSGKKWQVEW QSGAHDLKIT
DTALNQSVYM YQCNDTMLEV SGKVNNIVLD KCTKTCLILD NVVSGIELVN CKSCQVQIRG
AAPILSIDKT DGIIVYLSKE AINCRVVSAK SSEMNICVPD LDTEDDVIEI PLPEQFVHTF
DPKTKKFNTD MMKHE
//
