ID A0A0N1PG96_LEPSE Unreviewed; 352 AA.
AC A0A0N1PG96;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=FCP1 homology domain-containing protein {ECO:0000259|PROSITE:PS50969};
GN ORFNames=ABL78_0853 {ECO:0000313|EMBL:KPI89993.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI89993.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI89993.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI89993.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(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:KPI89993.1}.
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DR EMBL; LJSK01000012; KPI89993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1PG96; -.
DR EnsemblProtists; KPI89993; KPI89993; ABL78_0853.
DR VEuPathDB; TriTrypDB:Lsey_0012_0120; -.
DR OMA; NQPKNTS; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR12210:SF171; PHOSPHATASE HERZOG; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
FT DOMAIN 163..323
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 352 AA; 38230 MW; 9CE3AADBD4016285 CRC64;
MDGEQETTAT PTSFFRGISD KLDSQQRQHG GKGSSSKAGV HHTGSTSGNP NYSGGSSPPG
PPAPNTLITQ VSQQHAPTST APHGGGRAGS YGEAHSTTSN NSGGVRAGFS NGGVRHGGRS
GSRQRVHATE LVEWARYIRN QPKNTSPIDA SAHPSLLPEP LPMMRHKKCL VLDVDETLVH
SSYQSNARYD VHLPIQLDRD TQVNVYVAFR PHLRRFLEVI APLFEVVTFT ASMSAYCDPL
MNAIDGGRIL GGLRLFREHC SVVGTTYVKD LSLLGRNLDQ IAIIDNSPIA YLFQQRNAIP
VTSWFDDPND EELLRLIPVL EALAEADTVY DVLDNYNALL QLQQFQAGSG EC
//
