ID   A0A2G5EU17_AQUCA        Unreviewed;       371 AA.
AC   A0A2G5EU17;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=WH1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AQUCO_00400240v1 {ECO:0000313|EMBL:PIA59220.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA59220.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA59220.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DCP1 family.
CC       {ECO:0000256|ARBA:ARBA00008778}.
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DR   EMBL; KZ305021; PIA59220.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5EU17; -.
DR   STRING; 218851.A0A2G5EU17; -.
DR   InParanoid; A0A2G5EU17; -.
DR   OrthoDB; 385293at2759; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:InterPro.
DR   CDD; cd09804; Dcp1; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR010334; Dcp1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR16290:SF0; DECAPPING PROTEIN 1, ISOFORM A; 1.
DR   PANTHER; PTHR16290; TRANSCRIPTION FACTOR SMIF DECAPPING ENZYME DCP1; 1.
DR   Pfam; PF06058; DCP1; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069}.
FT   REGION          222..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..246
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   371 AA;  41220 MW;  384A7D18DB23A672 CRC64;
     MAQSGKLMPN LDQQSTKQLN LTVLQRIDPF VEEILITAAH VTFYEFNIEL NQWSRKDVEG
     SLFVVKRNTQ PRFQFIVMNR RNTDNLVENL LGDFEYEVQV PYLLYRNAAQ EVNGIWFYNS
     RECEDVANLF SRILNAYSKV PPKLKVSSNK SEFEELEAVP TMDVMEGPLE PTSSNASAVV
     DSPDDSTFVN FFSAAMNIGN TSNAVIPGQQ IQAPAMLSLS SHAPSIAPSP VPSLQKPPPL
     PISSSPMMPL PDTSDLNCNN HAANLVKPSS FFVPPPSSSV LMVPQVSSST PSSIPSAPPL
     HPPVNLQRPY GTPMLQPFPP PTPSPSLTPA PAQNYVPIIT KDKVRETLMR VFQKDEFIEM
     FYQELLNVHY S
//