ID A0A0L1IKI2_ASPNO Unreviewed; 563 AA.
AC A0A0L1IKI2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phosphoglycerate mutase family domain protein {ECO:0000313|EMBL:KNG80002.1};
GN ORFNames=ANOM_011808 {ECO:0000313|EMBL:KNG80002.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG80002.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG80002.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG80002.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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:KNG80002.1}.
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DR EMBL; JNOM01000744; KNG80002.1; -; Genomic_DNA.
DR RefSeq; XP_015400925.1; XM_015557064.1.
DR AlphaFoldDB; A0A0L1IKI2; -.
DR STRING; 1509407.A0A0L1IKI2; -.
DR GeneID; 26813612; -.
DR OrthoDB; 118474at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR46192; BROAD-RANGE ACID PHOSPHATASE DET1; 1.
DR PANTHER; PTHR46192:SF11; BROAD-RANGE ACID PHOSPHATASE DET1; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000037505}.
FT REGION 295..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..505
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 563 AA; 64130 MW; 3F9A4B3E8694AE9C CRC64;
MGKPRMIILI RHAQSEGNKN REIHQTIPDH RVKLTAEGHR QAHEAGSTLR ALLRPDDTIH
FFTSPYRRTR ETTEGILQSL TSDSPSPSPF PRHTIKVYEE PRLREQDFGN FQPCSAEMER
MWLERADYGH FFYRIPNGES AADAYDRISG FNESLWRLFG ENDFASVCVL VTHGLMTRVF
LMKWYHWSVE YFEDLRNINH CEFVIMKLNE DNGKYVLQNQ LRTWSELRKE KELERQRDRV
VNAVPPAVPP SESLVPIRRK WGGCPDGCNH GIRRKGSTRS NRTTGMDLAR NTLDAQHRKA
HDSIHTHNQP AQESNKSKGP STDVKAQVEG QFITAPEPAL GDRSKEARFF TNIIPAPAPQ
YGDFPNPQPT RSDFPPNEPN SNDQESNSNN ATTRASPIPK RPDLSRLHRD SEDHLLHPPR
SNYALLHLSG RDGGGTLSGA NSVAPSEDER EDKPPKPTTH QPKPSHDLGN DGDDEGSGTQ
AQRLRRSRSH HTSHRHNHPP TPGRRHLSKK PPNGYPDKDR NLDSDHPDSS IDHEEDPDPE
YHEPNDDLEA ARREDQSVRG SVY
//
