ID A0A2I2GDN6_9EURO Unreviewed; 347 AA.
AC A0A2I2GDN6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Phosphoenolpyruvate/pyruvate domain-containing protein {ECO:0000313|EMBL:PLB51014.1};
GN ORFNames=P170DRAFT_406503 {ECO:0000313|EMBL:PLB51014.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB51014.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB51014.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB51014.1,
RC ECO:0000313|Proteomes:UP000234275};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLB51014.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MSFO01000003; PLB51014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2GDN6; -.
DR STRING; 1392250.A0A2I2GDN6; -.
DR VEuPathDB; FungiDB:P170DRAFT_406503; -.
DR OrthoDB; 554215at2759; -.
DR Proteomes; UP000234275; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR42905:SF13; CARBOXYVINYL-CARBOXYPHOSPHONATE PHOSPHORYLMUTASE (AFU_ORTHOLOGUE AFUA_2G00120); 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:PLB51014.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000234275}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 38006 MW; 22191FCA0B62561F CRC64;
MSKSTINQNP YPWTFQANQP TTGINTGTSQ DLAMTIPQVR GSIPSFQASR LRSMMQEAHA
DPAKIVAHVC SYDALSSRLC QEAGFPMVFL SGYAMSSAFG LPDTGYIAFQ EVAAKIQEVV
RETSVPVMVD GDTGYGSPMN VRRTVQGFAL AGAAGVMIED QTWPKRCGHT KGKNVVSRDE
AYARWQAAVD ARNEGTDIWI LARTDSYMHG YEEALTRARK AIEIGVDAVF VEALPDRAAM
AQMRSDLDFP MLANIIEGGK TENLSAKELG ELGFAAVAYP WTLVAAKLKS IREALEGVKG
SLLTGKPPMI LPYDEVCEGV GFNRYYELEE RYQYEGSVTG TKGYQFE
//
