ID A0A178E6D8_9PLEO Unreviewed; 269 AA.
AC A0A178E6D8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=PH domain-like protein {ECO:0000313|EMBL:OAL51202.1};
GN ORFNames=IQ07DRAFT_586749 {ECO:0000313|EMBL:OAL51202.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL51202.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL51202.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL51202.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DCP1 family.
CC {ECO:0000256|ARBA:ARBA00008778}.
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DR EMBL; KV441643; OAL51202.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178E6D8; -.
DR STRING; 765867.A0A178E6D8; -.
DR InParanoid; A0A178E6D8; -.
DR OrthoDB; 385293at2759; -.
DR Proteomes; UP000077535; 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; cd13182; EVH1-like_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:UP000077535}.
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 30038 MW; 5BCF103415E631F7 CRC64;
MAPPKAKARA SHALPPPLPS DYETDAPPPA VDVPLPPPRS NEELNFAVLQ RVYPELHAIE
HVTPYAALYT FNLETQQWEK VGVEGTLFVC QLTPLPNGVE RFCVVIFNRR GLDNFYLDLT
SSEEMEIAEP YIILQGDDVV YGIWIFADPP PASTSNCRVE TATKMMEIAD RAKASREAKE
NHASNGSNDV VEQVEPASSA PMGRQLSLRE LFGQQREQDA DFSLHNHHSQ PTPHAYPHVY
VPNQNSRPPP QDVLSQLFQK AKQDYNSLG
//