ID A1C9C5_ASPCL Unreviewed; 273 AA.
AC A1C9C5;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Phosphoglycerate mutase family protein {ECO:0000313|EMBL:EAW13449.1};
GN ORFNames=ACLA_054960 {ECO:0000313|EMBL:EAW13449.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW13449.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW13449.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS027048; EAW13449.1; -; Genomic_DNA.
DR RefSeq; XP_001274875.1; XM_001274874.1.
DR AlphaFoldDB; A1C9C5; -.
DR STRING; 344612.A1C9C5; -.
DR EnsemblFungi; EAW13449; EAW13449; ACLA_054960.
DR GeneID; 4707027; -.
DR KEGG; act:ACLA_054960; -.
DR VEuPathDB; FungiDB:ACLA_054960; -.
DR eggNOG; KOG0235; Eukaryota.
DR HOGENOM; CLU_033323_0_0_1; -.
DR OMA; DFNRHEH; -.
DR OrthoDB; 9136at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; PTHR46517; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR PANTHER; PTHR46517:SF1; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT REGION 67..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7..14
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 273 AA; 29029 MW; 2ED27B6B8D113EC4 CRC64;
MKLYLIRHAE TTDNVAHNLA GTKDSPLTNH GALQITHLAK HFHSHNISFT HIFSSDLSRA
ALTAHGLAIP PQSPSPSPSP SPTPNLLPTL RERDFGSLEG TKWHAGWDAP RVPHPRPPET
ETSMRTRARS FVTEVLIPVL AAEGDEGVVA VVSHGILLGV LWGVLVSCFA AGRVSMVGDG
AGAGEGGVFR PAWANTGFLE VMIEPVVGLG VDADGGEVAE GDGVMPLLAG YAMQVLNVNS
RSHLAGLRRA RGVGSATFDQ RQRRIEHFFG GKK
//
