ID A0A161WJ18_9PEZI Unreviewed; 592 AA.
AC A0A161WJ18;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Histidine acid phosphatase {ECO:0000313|EMBL:KZL70946.1};
GN ORFNames=CT0861_01945 {ECO:0000313|EMBL:KZL70946.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL70946.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL70946.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL70946.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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:KZL70946.1}.
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DR EMBL; LFIV01000081; KZL70946.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161WJ18; -.
DR STRING; 708197.A0A161WJ18; -.
DR OrthoDB; 2681959at2759; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UP000076552};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..592
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007828557"
FT TRANSMEM 464..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 592 AA; 64805 MW; BA4F71480BE15F77 CRC64;
MGALSLAVLM GVLLSTTSAQ SSNPSVWASV AMVMHGERTP LRSELQNTLT PQGARQLYAQ
GSAFRMRYLA SGTRTNVSEG RITSRAAIKG VARNVIEHEQ LSILSVPDAH VVAGANAFMQ
GLYPSITQAF AADTGGANIS YSTLSGNSTQ YPLDGYQYPV IETLGFSDER SVAIRGNTEC
PQWTISTTTI MQRDPYMDNL YEASLPGYQA LFSTPPLNDG IISLSNANFW DAYNLYQYVR
YRYSHEQAIY DAMQDDYAQQ SQFLMMYARQ QQLNMTSNQA VSGLKKGDMI RTIAGRTLAR
KVVDAFKANG NYAGYSNKMT LMFSSHEPFM SFFSLAKLQR EDQTLLSPFW NIPENGAAMV
FELIGDQPDE PNTYPTEENL YVRFLYRENA NADTPFKEYS LFGLSDTETR VTYSYFKQEM
LRFGVDISTW CSICGSVQSF CEWRTTKTQP TVGESIRSAV QKPVVAGVIG AAIVLAVLGL
VVVAAAVLGG FRIHRAGPGA GPEAKGQDSR VAGLGGFKAA EKMASDPDLS ISKRGVHHER
QGSWELRDGL DVTTGQAGIV VDKSSSTFRS KSIDEDAISV LGASPVKPRE NV
//