ID A0A075AN11_ROZAC Unreviewed; 440 AA.
AC A0A075AN11;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Adenylyl cyclase-associated protein {ECO:0000256|RuleBase:RU000647};
GN ORFNames=O9G_001037 {ECO:0000313|EMBL:EPZ31126.1};
OS Rozella allomycis (strain CSF55).
OC Eukaryota; Fungi; Fungi incertae sedis; Cryptomycota;
OC Cryptomycota incertae sedis; Rozella.
OX NCBI_TaxID=988480 {ECO:0000313|EMBL:EPZ31126.1, ECO:0000313|Proteomes:UP000030755};
RN [1] {ECO:0000313|EMBL:EPZ31126.1, ECO:0000313|Proteomes:UP000030755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSF55 {ECO:0000313|EMBL:EPZ31126.1,
RC ECO:0000313|Proteomes:UP000030755};
RX PubMed=23932404; DOI=10.1016/j.cub.2013.06.057;
RA James T.Y., Pelin A., Bonen L., Ahrendt S., Sain D., Corradi N.,
RA Stajich J.E.;
RT "Shared signatures of parasitism and phylogenomics unite Cryptomycota and
RT microsporidia.";
RL Curr. Biol. 23:1548-1553(2013).
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000256|ARBA:ARBA00007659,
CC ECO:0000256|RuleBase:RU000647}.
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DR EMBL; KE561300; EPZ31126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075AN11; -.
DR STRING; 988480.A0A075AN11; -.
DR EnsemblFungi; EPZ31126; EPZ31126; O9G_001037.
DR HOGENOM; CLU_015780_1_0_1; -.
DR OMA; HEDRNDL; -.
DR OrthoDB; 1453907at2759; -.
DR Proteomes; UP000030755; 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; 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:UP000030755}.
FT DOMAIN 291..419
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
SQ SEQUENCE 440 AA; 48495 MW; 92B2C6E53FB72F5C CRC64;
MSQSDQQLQL LIKRLEAATA RLEGLTGLKT NATNSEESRV PQDEELSQSV KEFDVFITEN
IQKFMEISSA TNDLVIQQPL SINSFMGALT KPVMELAKQV TEIKDSNRPS KFFNHLSCVA
EGFPAVGWFV VEPTPASYIK DMRESAQFYS NRIMKEYKDV DKMQVEWASC FLNVLDALHK
YVKAHHTTGL VWNAKGDEAK IEDFVAPGPP PPPPGPVPIF SAPAPSNNNA PDMTNLFAEL
NKGDLVTKGL RKVDKSEMTH KNPNLRSTSV VKAENKQNES LSPKINETTK PARIELEGNK
WFIIGNENII ISETEIKNVI NIYNCSNSVI QVKNKVNAIS AVNCKKVAIV ADQIVSTVEI
VNSKGMQIQI LGKCPTISVD KTDGTSLDTE ILSAKCSELN VSLPGANDDD DLIEKPVPEQ
FKTIIKNGKL ETTPVEHSGA
//
