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Database: UniProt
Entry: L7K0K3_TRAHO
LinkDB: L7K0K3_TRAHO
Original site: L7K0K3_TRAHO 
ID   L7K0K3_TRAHO            Unreviewed;       496 AA.
AC   L7K0K3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Nucleoside phosphatase {ECO:0000313|EMBL:ELQ76882.1};
DE            EC=3.6.1.15 {ECO:0000313|EMBL:ELQ76882.1};
DE            EC=3.6.1.5 {ECO:0000313|EMBL:ELQ76882.1};
GN   ORFNames=THOM_0123 {ECO:0000313|EMBL:ELQ76882.1};
OS   Trachipleistophora hominis (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC   Trachipleistophora.
OX   NCBI_TaxID=72359 {ECO:0000313|EMBL:ELQ76882.1, ECO:0000313|Proteomes:UP000011185};
RN   [1] {ECO:0000313|EMBL:ELQ76882.1, ECO:0000313|Proteomes:UP000011185}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23133373; DOI=10.1371/journal.ppat.1002979;
RA   Heinz E., Williams T.A., Nakjang S., Noel C.J., Swan D.C., Goldberg A.V.,
RA   Harris S.R., Weinmaier T., Markert S., Becher D., Bernhardt J., Dagan T.,
RA   Hacker C., Lucocq J.M., Schweder T., Rattei T., Hall N., Hirt R.P.,
RA   Embley T.M.;
RT   "The genome of the obligate intracellular parasite Trachipleistophora
RT   hominis: new insights into microsporidian genome dynamics and reductive
RT   evolution.";
RL   PLoS Pathog. 8:E1002979-E1002979(2012).
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283}.
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DR   EMBL; JH993807; ELQ76882.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7K0K3; -.
DR   STRING; 72359.L7K0K3; -.
DR   VEuPathDB; MicrosporidiaDB:THOM_0123; -.
DR   HOGENOM; CLU_564061_0_0_1; -.
DR   InParanoid; L7K0K3; -.
DR   OMA; GRMIDDK; -.
DR   Proteomes; UP000011185; Unassembled WGS sequence.
DR   GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IEA:UniProt.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ELQ76882.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011185}.
FT   REGION          196..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        145
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
SQ   SEQUENCE   496 AA;  57017 MW;  BB5939F473364B4E CRC64;
     MFQHALKLQT KRNLQMLLFA PFILAKQFVV ILDAGFTSTK LNVYTFSDMI VVSSYTRFYH
     PGVHELRMNE IEHMIECMLS DARKFVEENG GDVHRTRIAL VATEGLRSLG RTCADVILRC
     IKGLIDRSGF VSGRHSVSVM DGVFEGLYAY EALVYLLFLR DNKDILGEQL VDRYRKNKTR
     RDDEVGRSDR NAVRVSKNWW NEKKNNGQST ENRDKKTASD NTQDNITDSS NKLTHENRTA
     VISKVGQQEE TGDAKTGKKK LHGWYFFKAK SGENTSKNNL NELKNTEENE FDKVTYLKPR
     NNTTSSIKSE NYLQREHSTT SHSLTTNSKL SLGIIEMGGG SMQIAFSTNV GNKYQLFIHS
     FHNLGLIKGM NELLSLNLLE RCRDLKDECV HCIREHFNLN EFVRAAPLHS VHKFYLLSFF
     YDRLSEYQPI RKFDDIINVY KTRCVRRTKN CNDLEYMVLV LKGIGLKGDT RVEIGRMIDD
     KNLNWGLAKA LEMLIG
//
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