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Database: UniProt
Entry: A0A0A2KHM5_PENIT
LinkDB: A0A0A2KHM5_PENIT
Original site: A0A0A2KHM5_PENIT 
ID   A0A0A2KHM5_PENIT        Unreviewed;       299 AA.
AC   A0A0A2KHM5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Histidine phosphatase superfamily, clade-1 {ECO:0000313|EMBL:KGO66411.1};
GN   ORFNames=PITC_067070 {ECO:0000313|EMBL:KGO66411.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO66411.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO66411.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO66411.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000256|ARBA:ARBA00038362}.
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:KGO66411.1}.
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DR   EMBL; JQGA01001418; KGO66411.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2KHM5; -.
DR   HOGENOM; CLU_039184_0_1_1; -.
DR   OMA; CDRRSTA; -.
DR   OrthoDB; 1456057at2759; -.
DR   PhylomeDB; A0A0A2KHM5; -.
DR   Proteomes; UP000030104; 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; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR   PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104}.
SQ   SEQUENCE   299 AA;  33971 MW;  8ACA9141BBFEE7B1 CRC64;
     MNSSPLLHFA AVTGYFLQDD PATDPDTFDY VKTNFGLIEK YYDEHLEVEQ TDSQWRRFDA
     HIQRLNASKT KKLKVLFLGR HGEGVHNVAE RKYGTKEWDD YWSLQDGDED GNWVDARLTE
     QGRCQAQVAH AAWEQQIEAG IPPPESYYVS PLNRCLETAH ITFQGLSIPG TAPFKPTIKE
     LLRETMGQHT CDRRSTASEI AKEYPEYRFE AGFSEEDKLW DAKVRESNEH RNDRLRRLLN
     DIFAHDESTY ISLTAHSGAI TSILEVVGHR RFALATGAVI PVVISVEKGA PSQPESQSS
//
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