ID A0A0D7BKE5_9AGAR Unreviewed; 499 AA.
AC A0A0D7BKE5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Phosphoglycerate mutase-like protein {ECO:0000313|EMBL:KIY71023.1};
GN ORFNames=CYLTODRAFT_391000 {ECO:0000313|EMBL:KIY71023.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY71023.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY71023.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY71023.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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DR EMBL; KN880459; KIY71023.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7BKE5; -.
DR STRING; 1314674.A0A0D7BKE5; -.
DR OrthoDB; 2404758at2759; -.
DR Proteomes; UP000054007; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd07040; HP; 1.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR016274; Histidine_acid_Pase_euk.
DR PANTHER; PTHR20963:SF18; ACID PHOSPHATASE PHO11-RELATED; 1.
DR PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000054007};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..499
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002317287"
FT ACT_SITE 61
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT ACT_SITE 339
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-1"
FT DISULFID 50..387
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 254..269
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 439..447
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 499 AA; 53577 MW; 43BDD26F7FC56BE5 CRC64;
MVHWSALIFG LVVSAEASFN PLQHSGPASP YFDAPSRYDI DADAVAPLGC KVDQAAYILR
HGSRYAEPGS LKGWQSLYAK VQNATFDAYG PLRFIGAWTV PEDDIEHMSP SAGAYLSTTG
AREAFDLGRD LRLRYGFTPG GDNLTIYSAG QQRCVDTATF FLRGYLSQGN YANATGNNRG
HIVTLPDSVK DAYFADSLTP SSACPAYSAA NNGSAISDAY RATFRQAIAD RLNKYLKGNL
VFEPSDIGVM QDLCGFGTQV SGWKAEPFCK LFTEKEWLDY EYAHDLNYYY GAGPGNALSA
TVGYSWVKAI SDLLASGPGA TSQGGDATPA PLIMSFTHDN NIPPIMSALG LWNSSALDPL
HPNPKREFRS SYLVPFRGTI ALERLTCIED AAKDPYNFDT WSPITHSANT TYDMFSGDVE
TAQYVRVRVN NAPVPIPGCQ SGPGKACALA SFGDHVAKMG RIAGGFAERC GLTNATGNTD
ELTFYTHSGA AGASTVLAV
//
