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Database: UniProt
Entry: A0A158R9S4_TAEAS
LinkDB: A0A158R9S4_TAEAS
Original site: A0A158R9S4_TAEAS 
ID   A0A158R9S4_TAEAS        Unreviewed;       544 AA.
AC   A0A158R9S4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Cytosolic purine 5'-nucleotidase {ECO:0000313|WBParaSite:TASK_0000772601-mRNA-1};
GN   ORFNames=TASK_LOCUS7727 {ECO:0000313|EMBL:VDK38908.1};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000772601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000772601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK38908.1, ECO:0000313|Proteomes:UP000282613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR017434-2};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR017434-2};
CC   -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC       {ECO:0000256|ARBA:ARBA00009589}.
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DR   EMBL; UYRS01018664; VDK38908.1; -; Genomic_DNA.
DR   STRING; 60517.A0A158R9S4; -.
DR   WBParaSite; TASK_0000772601-mRNA-1; TASK_0000772601-mRNA-1; TASK_0000772601.
DR   Proteomes; UP000046400; Unplaced.
DR   Proteomes; UP000282613; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR016695; Pur_nucleotidase.
DR   NCBIfam; TIGR02244; HAD-IG-Ncltidse; 1.
DR   PANTHER; PTHR12103; 5'-NUCLEOTIDASE DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR12103:SF15; CYTOSOLIC PURINE 5'-NUCLEOTIDASE; 1.
DR   Pfam; PF05761; 5_nucleotid; 1.
DR   PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR017434-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR017434-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282613}.
FT   REGION          480..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         2
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017434-2"
SQ   SEQUENCE   544 AA;  62669 MW;  BF215C96F1902CD9 CRC64;
     MDYTLASYKS PQYEELAFKI LRDRLIEFGY PQELSQFEYE PSFPVRGLWF DQQYGTLMKI
     DQFGNILMCL VGFNVLSNEK IGELYPNRFI KYEKDRIRVM STLFDLPEIY LLACIIHYMH
     SNDAYIKEPN GVKYQSLYIS YRSILQDVEE AMSWMHMGEL KKQTMANIEK YIEQNPKLLV
     LLDKLRTERT NVFLLTNSDY EYSDAVMKYL CNLPDKDGNV RHWTSYFDYI VVDAKKPIFF
     QEGTLMRAVD MSTGRYKMGQ IAGPLERSKI YAGGSSATFT HLIGAQGKDV LYTGDHIFGD
     ILKSKRQVGW KTFLVVPELL NEIYVWKKKN SLFERLNELD NELADKYKDL NIASNLKPDV
     SKLHKEIRRV ANEMNEAYGL LGSIFRHGSR LTTFSSQAMQ FADLYSYSCY NLIYYPLCYM
     FRAPPMLMPH ESTVPHEETT FESFKDLEDS PCGLRRRTTT EAEMAQHIKA MLLKRMPDSM
     MATHSSAGEA EEEDEKGEDG ENTPIGTATF MTTTAPAALK NLSSHMETLD LSAITSSSSS
     SHSF
//
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