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Database: UniProt
Entry: A0A165PT27_9APHY
LinkDB: A0A165PT27_9APHY
Original site: A0A165PT27_9APHY 
ID   A0A165PT27_9APHY        Unreviewed;       448 AA.
AC   A0A165PT27;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Phosphoglycerate mutase-like protein {ECO:0000313|EMBL:KZT68591.1};
GN   ORFNames=DAEQUDRAFT_727715 {ECO:0000313|EMBL:KZT68591.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT68591.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT68591.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT68591.1,
RC   ECO:0000313|Proteomes:UP000076727};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000256|ARBA:ARBA00005375}.
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DR   EMBL; KV429065; KZT68591.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165PT27; -.
DR   STRING; 1314783.A0A165PT27; -.
DR   OrthoDB; 2786306at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   PANTHER; PTHR11567:SF195; ACID PHOSPHATASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G14570)-RELATED; 1.
DR   PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..448
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007864253"
SQ   SEQUENCE   448 AA;  50300 MW;  E22E4A204BA4B2C8 CRC64;
     MKWAKARWLG LILQVPAQMT LALSTEIPVY NGICSTTGVY NTSFTPANLP WNTYNYCNAP
     HVNAAHYEAP GDAPNATLIY LNAVIRHHKR TPDNLYPEEG ELNQESWNCS NFLQFNHGGG
     TTHIFHETYS PPWHPFLIQI WNGTCDEGQL TYEGLQDAIH HGQDFWSVYA QKLGFLQSVN
     EEEIFVRTSV ADRTYQVAGG VLTGMDPTMA TKTFPVLTQP SVIDSIVPDY SCPNADNIRD
     AYQSVPAWND HLQENANFQD QLCTMLGVTG NTAWTSWYDH FFDTFSSRTC HDHPLPCNAS
     GACVTVEDAA RVFAIGDWEY NYIWNTAENA TTYSQLTFGV FIMELVHNFR LFRSGGETHK
     LRFYVGHDGS MIRLASLLGI GKVAPLRWPA MGSEIIMEVW KTTAGEQYVR IMHEGTPVPG
     LQWLVLDDFI DMLEAQIPAN VFAACMGS
//
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