ID U1HHD8_ENDPU Unreviewed; 581 AA.
AC U1HHD8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Histidine acid phosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EPUS_02715 {ECO:0000313|EMBL:ERF68259.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF68259.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; KE721523; ERF68259.1; -; Genomic_DNA.
DR RefSeq; XP_007806034.1; XM_007807843.1.
DR AlphaFoldDB; U1HHD8; -.
DR GeneID; 19237765; -.
DR eggNOG; ENOG502SM2K; Eukaryota.
DR HOGENOM; CLU_023111_0_1_1; -.
DR OMA; STQEWCL; -.
DR OrthoDB; 2681959at2759; -.
DR Proteomes; UP000019373; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF127; -; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..581
FT /note="Histidine acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004612580"
FT TRANSMEM 451..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 517..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 62725 MW; 9C1A8570EDF2C1AD CRC64;
MKFLGVVLAL TGLQVVRTAA QTVLREHIWS TVIYSRYGDR TPYILPTSNT LTPLGATQMY
SAGTRFRERY LVSAPGNGNT VIQGISPFQL DNDQVSVVSL NDQFIVASAQ AFMQGLYPPL
MASSNATFIN GQSQLANGSN ILSPLDGYQY PQISAVSPLD LNSIWLMGAN NCPMYSASRS
DYFNSAFYDN LLETNQDFYR SLQPALLNGI FANSSVNYLN AYLIFDYLNY GSVHNSSFLD
DLSFEDLTRA KILADNWVLA TYGNTSVSGL TEGDRIRAIA GRTLANKIVS ALYGNINTAG
TLHKMTLLFG GFEPMVSFAA LASLASEQNP QFLGIPEYGS SMVFELFSLT ENDTDIYPAT
ADLNVRFFFQ NSTDDTSNLV AYPLFGNGPS GISMTLSEFV ADMQKIMISS VGDWCQTCAS
VSIFCPAFQA DAGDGRSGPT RPRSRGGLRP VVAGVIGAVV TLAVVGLLIT AAAVFGGARL
YRQRSKKRSE LNGFKGGEKL ASDQDLTIPK SGASASIAVA GEGPTRGHER VGSWELGDQK
KAEEAQQPGL NSSATVMRRP SFEDDLHVSP FADPVKPNDR V
//
