ID A0A074X4S8_AURPU Unreviewed; 391 AA.
AC A0A074X4S8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=PH domain-like protein {ECO:0000313|EMBL:KEQ80515.1};
GN ORFNames=M438DRAFT_348747 {ECO:0000313|EMBL:KEQ80515.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ80515.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ80515.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ80515.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the DCP1 family.
CC {ECO:0000256|ARBA:ARBA00008778}.
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DR EMBL; KL584997; KEQ80515.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074X4S8; -.
DR STRING; 1043002.A0A074X4S8; -.
DR HOGENOM; CLU_058649_0_1_1; -.
DR OrthoDB; 385293at2759; -.
DR Proteomes; UP000030706; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 279..315
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 222..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 391 AA; 44603 MW; 7DE282BEE18BE865 CRC64;
MPPKNRNNRN SHPRPTAHHH VPSDYDTDTA YATDAMSLPQ PAPIPARTNE ELNLSVLQRH
DPSVHQILSV APFAVVYTFN PVSTSWEKQG AEGTLFVCSL LPPVGGPQIE RYSCIVLNRR
GLENFSSELF SAESVQVTDD YVILQVEGED GSANIYGLWI FAEEGGSTVQ TRVVNALIIQ
ECAKRAEDSR DAAAVADVED EYIEEELPPS MQPNFEEPPP PTIHRQQKEP EQQRYEYEQE
AQGQQVNLLH LFKSNQQQQR PALASPFQSH DQQQYYAMQH QHQLQHQQHQ QQLQQQQHQQ
QLAAMQQQQQ LQQQQMLQQH QAMQHQHQQH QHQPQNFNAA PPPLPGYGAP QQYSQQYPQQ
HPQQHPPPPQ AQPQGQADVL MSLFSNARRG Y
//
