ID U6LMF9_9EIME Unreviewed; 359 AA.
AC U6LMF9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Exosome complex exonuclease, putative {ECO:0000313|EMBL:CDJ49769.1};
GN ORFNames=EBH_0028400 {ECO:0000313|EMBL:CDJ49769.1};
OS Eimeria brunetti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ49769.1};
RN [1] {ECO:0000313|EMBL:CDJ49769.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ49769.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ49769.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ49769.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RNase PH family.
CC {ECO:0000256|ARBA:ARBA00006678}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG711843; CDJ49769.1; -; Genomic_DNA.
DR AlphaFoldDB; U6LMF9; -.
DR EnsemblProtists; CDJ49769; CDJ49769; EBH_0028400.
DR VEuPathDB; ToxoDB:EBH_0028400; -.
DR OrthoDB; 202892at2759; -.
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; IPR015847; ExoRNase_PH_dom2.
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 Pfam; PF03725; RNase_PH_C; 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:CDJ49769.1};
KW Exosome {ECO:0000256|ARBA:ARBA00022835};
KW Hydrolase {ECO:0000313|EMBL:CDJ49769.1};
KW Nuclease {ECO:0000313|EMBL:CDJ49769.1}.
FT DOMAIN 59..219
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF01138"
FT DOMAIN 249..296
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF03725"
FT REGION 86..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 37640 MW; F16A7632F313DF1C CRC64;
MYKGEVVSPC GFRADGRLVH ECRQLNCRTS VPAAAATAAA AAAAAHADGA SIAAAGASGC
LTSCDGRAVV SLGCTKVMAL VYGPQPTSTS SSSSSSGGGS SSSNSSSSCW SVNATEQTSA
AMQMMHEGRQ SSTRGELAAA VSVVVSVGLL DSCVRSRCMY TPDAAEVAAA VRTAAEGIII
RRLYTQTRIT ISILVLADDG CVLSASLIAA SLALADAGIA MRDLLPACTV LLLPQHQQQQ
QQQQQEPLLL LDPTSEETRS GGSSLTLGIT AQTNNVVALQ LRGRVDRATY EKMFELCLKG
CIATAECMRG LLIHRLTNIF PHLHAVAAAA VHQQQQQQQQ QQQQQQQQQQ QQPILFGVR
//
