ID A0A162KVE3_CORDF Unreviewed; 535 AA.
AC A0A162KVE3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:OAA80348.1};
GN ORFNames=LEL_03834 {ECO:0000313|EMBL:OAA80348.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA80348.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA80348.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA80348.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA80348.1}.
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DR EMBL; AZHF01000002; OAA80348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162KVE3; -.
DR STRING; 1081108.A0A162KVE3; -.
DR OrthoDB; 118474at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
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:UP000076881}.
FT REGION 234..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 60202 MW; 5ED7ECEEB9E35C4C CRC64;
MAKPRLIILI RHAQSEGNKN RDIHQSVPDH RVKLTSDGWA QAYDAGRRLR TLLRPDDKIH
FFTSPYRRTR DTTEGILTTL TSDTDGPSPF RRANIKVYEE PRLREQDFGN FQPCSAEMER
MWQERADYGH FFYRIPNGES AADAYDRVSG FNESLWRQFG EDDFASVCVL VTHGLMSRVF
LMKWYHFTVE YFEDLRNIDH CEFLLMRRQD NGKYNLETKL RTWSELKRER AALKEKEKEK
EKGKNGEGTP GRDEVKLQRN KTFVVTRRWG GCPDGCNHTS KYLKRHDLET LRQKDEEQAA
VTSNKAVAAH HRHRPRPAMS SDDEDEHIHI HSNHNGTPSS SSATATSADK KKPVVEITRT
ASTTKTTTLQ QPDAATAAST IKSPQFMHLG RDFGGSYSGH TSVVDSDSDK QHEDSDSESK
HAPAAPATGL HHRRRRGSIL NSIEARLLQS TINSHNNHAR QLSASSLGSA ASPGIGPFVN
RLGDAPPLSD SEGDVAKRAS LVKTPGEEKE ELGSGSLEDL EAAEKADRSI EGSVY
//
