ID F9W7X7_TRYCI Unreviewed; 258 AA.
AC F9W7X7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 08-NOV-2023, entry version 24.
DE SubName: Full=WGS project CAEQ00000000 data, annotated contig 1672 {ECO:0000313|EMBL:CCD13299.1};
GN ORFNames=TCIL3000_0_40660 {ECO:0000313|EMBL:CCD13299.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCD13299.1, ECO:0000313|Proteomes:UP000000702};
RN [1] {ECO:0000313|Proteomes:UP000000702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL3000 {ECO:0000313|Proteomes:UP000000702};
RA Jackson A.P., Berry A., Allison H.C., Burton P., Anderson J., Aslett M.,
RA Brown R., Corton N., Harris D., Hauser H., Gamble J., Gilderthorp R.,
RA McQuillan J., Quail M.A., Sanders M., Van Tonder A., Ginger M.L.,
RA Donelson J.E., Field M.C., Barry J.D., Berriman M., Hertz-Fowler C.;
RT "Divergent evolution of antigenic variation in African trypanosomes.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCD13299.1, ECO:0000313|Proteomes:UP000000702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCD13299.1,
RC ECO:0000313|Proteomes:UP000000702};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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:CCD13299.1}.
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DR EMBL; CAEQ01001100; CCD13299.1; -; Genomic_DNA.
DR AlphaFoldDB; F9W7X7; -.
DR VEuPathDB; TriTrypDB:TcIL3000_0_40660; -.
DR OMA; CRHGQDM; -.
DR OrthoDB; 9136at2759; -.
DR Proteomes; UP000000702; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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 InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR48100:SF44; BROAD-SPECIFICITY PHOSPHATASE YOR283W; 1.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000702}.
FT ACT_SITE 82
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 157
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 81..88
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 258 AA; 29236 MW; 309F25BE93393CEC CRC64;
MKVPLLLYGG LTYFYPHPSL RIYRFIPHGL QAPVSTGPNI RIARTWVPTE PIHWKNNKKF
SFFDFGILSS EGDMATVHIC RHGQDEDNRD GLLNGRRDRP LTALGREQAN RVADKLKSSG
VSYDIILSSP LQRAYETACI IASALGKEVQ KDEDLIERDF GVMTGKPIND IRRLAGENVL
QGDKVLYFLD VKEAETFDQC FSRAARLLER VDNQFAGKRV LFVCHGDIGK MVQAVRKNIT
WRDALLLPYI SNTDIVEL
//