ID J4D9R7_THEOR Unreviewed; 338 AA.
AC J4D9R7;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Nudix hydrolase domain-containing protein {ECO:0000259|PROSITE:PS51462};
GN ORFNames=TOT_030000818 {ECO:0000313|EMBL:BAM41555.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41555.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM41555.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM41555.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
CC {ECO:0000256|ARBA:ARBA00005279}.
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DR EMBL; AP011948; BAM41555.1; -; Genomic_DNA.
DR RefSeq; XP_009691856.1; XM_009693561.1.
DR AlphaFoldDB; J4D9R7; -.
DR STRING; 869250.J4D9R7; -.
DR EnsemblProtists; BAM41555; BAM41555; TOT_030000818.
DR GeneID; 20715965; -.
DR KEGG; tot:TOT_030000818; -.
DR VEuPathDB; PiroplasmaDB:TOT_030000818; -.
DR eggNOG; KOG2937; Eukaryota.
DR OrthoDB; 1472at2759; -.
DR Proteomes; UP000003786; Chromosome 3.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016070; P:RNA metabolic process; IEA:UniProt.
DR Gene3D; 1.10.10.1050; Dcp2, box A domain; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR007722; DCP2_BoxA.
DR InterPro; IPR036189; DCP2_BoxA_sf.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR23114; M7GPPPN-MRNA HYDROLASE; 1.
DR PANTHER; PTHR23114:SF17; M7GPPPN-MRNA HYDROLASE; 1.
DR Pfam; PF05026; DCP2; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SMART; SM01125; DCP2; 1.
DR SUPFAM; SSF140586; Dcp2 domain-like; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 99..227
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
SQ SEQUENCE 338 AA; 39728 MW; 995F02376D59E345 CRC64;
MELSESESSI LESALLDCYG RFITLLPEDV LRDHIHLPFH LQEAFWWYCD KWQVRHPELP
SYSFSDFLEF ICRDCPILKK FVTTNDLKNM ISNWREYAKK IPVRGGIIFN TACEKVLLVQ
SYKSKSWSFP RGKRDEAEDD AKCAAREIQE ETGLDLNSSI NGDFYLEIVE NDMNLKLFLI
PGVDDNVRLK SFSDYEICKF KWIHLRQLEN IHYLRFSTFQ VKPFIKKIIE FSKDFQGGKY
ASQFPEAYQR YLKLANINQI TFGLAAHGSA PGSASGWTPE EMFRVNFEKF GIVSTYKEDE
VKQESIFQSW TPVEIRPKNK RYKERELVKF DPDQFSSK
//
