ID   J4DNT9_THEOR            Unreviewed;       258 AA.
AC   J4DNT9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=3' exonuclease, exosome component {ECO:0000313|EMBL:BAM39539.1};
GN   ORFNames=TOT_010000994 {ECO:0000313|EMBL:BAM39539.1};
OS   Theileria orientalis strain Shintoku.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM39539.1, ECO:0000313|Proteomes:UP000003786};
RN   [1] {ECO:0000313|EMBL:BAM39539.1, ECO:0000313|Proteomes:UP000003786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shintoku {ECO:0000313|EMBL:BAM39539.1,
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 RNase PH family.
CC       {ECO:0000256|ARBA:ARBA00006678}.
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DR   EMBL; AP011946; BAM39539.1; -; Genomic_DNA.
DR   RefSeq; XP_009689840.1; XM_009691545.1.
DR   AlphaFoldDB; J4DNT9; -.
DR   STRING; 869250.J4DNT9; -.
DR   EnsemblProtists; BAM39539; BAM39539; TOT_010000994.
DR   GeneID; 20713825; -.
DR   KEGG; tot:TOT_010000994; -.
DR   VEuPathDB; PiroplasmaDB:TOT_010000994; -.
DR   eggNOG; KOG1068; Eukaryota.
DR   OrthoDB; 231151at2759; -.
DR   Proteomes; UP000003786; Chromosome 1.
DR   GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11953; EXOSOME COMPLEX COMPONENT; 1.
DR   PANTHER; PTHR11953:SF2; EXOSOME COMPLEX COMPONENT MTR3; 1.
DR   Pfam; PF01138; RNase_PH; 1.
DR   SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   Exonuclease {ECO:0000313|EMBL:BAM39539.1};
KW   Exosome {ECO:0000256|ARBA:ARBA00022835};
KW   Hydrolase {ECO:0000313|EMBL:BAM39539.1};
KW   Nuclease {ECO:0000313|EMBL:BAM39539.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003786}.
FT   DOMAIN          17..136
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF01138"
SQ   SEQUENCE   258 AA;  28711 MW;  0C37A1399936227B CRC64;
     MEDSIEEDTE MTDRFTQLRP LDVKLSTSST FHGSCIINLG NTIVKCLVNL PKVSAKKAAS
     DFGQFTLEVT SNDSFHTQKD LETLKTQILE TFEKHIIMDN YPCQIIEAYV IISNDDGGLL
     PTVLMGMCLA LIDCGIHVYD VIAACSVCVF KDRNQQLTVA LDLTREEEEY YKSLDPDLTV
     VNLGLCSQLK TIALLYSKGC YIGESLKDAL DVAKEACSLL SGELFKVLRS SHIWKAESSN
     FVLQTDYIQP SVDVNPIM
//