ID T0L1V1_COLGC Unreviewed; 446 AA.
AC T0L1V1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Histidine acid phosphatase {ECO:0000313|EMBL:EQB58893.1};
GN ORFNames=CGLO_00795 {ECO:0000313|EMBL:EQB58893.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB58893.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB58893.1}.
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DR EMBL; AMYD01000186; EQB58893.1; -; Genomic_DNA.
DR AlphaFoldDB; T0L1V1; -.
DR STRING; 1237896.T0L1V1; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_3_1_1; -.
DR OMA; FPWVNAS; -.
DR OrthoDB; 2404758at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
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 InterPro; IPR016274; Histidine_acid_Pase_euk.
DR PANTHER; PTHR20963:SF14; ACID PHOSPHATASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000894-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..446
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004579630"
FT DISULFID 54..355
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 242..255
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
FT DISULFID 381..389
FT /evidence="ECO:0000256|PIRSR:PIRSR000894-2"
SQ SEQUENCE 446 AA; 49687 MW; AFF9FD175DBD2CC7 CRC64;
MAGKLLHLLP LVAYTSASTL YSSYKFNPLE HLGGIAPYFE PQDPPTSPDA PQGCTASRAA
YLVRHAAIYA NDFDFEEYIE PFLEKLGNKT NLNWSKVPSL SFLADWDAPV SEAETSILTR
VGRLEATQLG VDLEFRYPNL KLPQRVWTSS AERTYKSAQS LVRGLEIDDD TMNVVSIYES
KESGADSLTP YKACPAYSSS AGSEQSGEFQ KKFATPITKR LNALASDFNF TVNDVFGMQQ
LCGYETVIRG RSPFCDLDLF SPDDWLGWEY TEDIRYHYNV GYGNNVAPYV GMPWLNATAN
LLMAETADED LYPGFGAAAD INATFPLDRI NYRRAWRSSN ILSFLSNIAI ERLNCTGSYG
YEDGEYYRVL VNSSPQPLPD CADGPGTTCS RSGFETYIQD RVERFTGFSE QCGVEYDNST
DVMSIYQDQS VGNGTTVGKR YTATFQ
//
