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
//