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Database: UniProt
Entry: A0A0A2KV97_PENIT
LinkDB: A0A0A2KV97_PENIT
Original site: A0A0A2KV97_PENIT 
ID   A0A0A2KV97_PENIT        Unreviewed;       454 AA.
AC   A0A0A2KV97;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Phosphoesterase {ECO:0000313|EMBL:KGO71747.1};
GN   ORFNames=PITC_027600 {ECO:0000313|EMBL:KGO71747.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO71747.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO71747.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO71747.1,
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   -!- 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:KGO71747.1}.
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DR   EMBL; JQGA01000918; KGO71747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2KV97; -.
DR   STRING; 40296.A0A0A2KV97; -.
DR   HOGENOM; CLU_027977_2_0_1; -.
DR   OMA; EHIPYAG; -.
DR   OrthoDB; 2218179at2759; -.
DR   PhylomeDB; A0A0A2KV97; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042578; F:phosphoric ester hydrolase activity; IEA:UniProt.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR007312; Phosphoesterase.
DR   PANTHER; PTHR31956:SF8; ACID PHOSPHATASE PHOA (AFU_ORTHOLOGUE AFUA_1G03570); 1.
DR   PANTHER; PTHR31956; NON-SPECIFIC PHOSPHOLIPASE C4-RELATED; 1.
DR   Pfam; PF04185; Phosphoesterase; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..454
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001990610"
FT   TRANSMEM        430..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          404..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  49878 MW;  18BE82044D18145C CRC64;
     MKAVLAVVMG AAALASAQTA TTSEPAIADI HAAAATTKPE VTVSNVKGLA FDRFFQVWLE
     NINYSDAASD ANMQWLASQG ILLTNFYAVT HPSEPNYCAS AGGDTFGMDN DDFHQIPANI
     STVADLLDTK GVSWAEYQEH IPYAGFQGYN YSNQETFHND YVRKHNPLVL YDSVTSNNSR
     ARHIKSFDDF ENDLQDQKLP QWAFITPNMT NDAHDTNITF AAKWERPWVT QLLENEYFTN
     NTLLLLTFDE DETYTNDNRI FSILVGGAVP EHLKGTKDDT FYTHYSTIAS VSANWGLPSL
     GRWDCGANLF EIVANKTGYV NYEVDKTYLT LNQTYPGPLS IGDPSIGNTS TFSPVWPVPI
     TDSNEKCSAG HGILDIVKKT YGHLNTTYDT KPFPWEAKTH YNDKVTAKRS SNETTSKTNS
     TTVHPSSSGA GVAAAAPMTT VVLGALLAIA AYSF
//
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