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Database: UniProt
Entry: G3T3V2_LOXAF
LinkDB: G3T3V2_LOXAF
Original site: G3T3V2_LOXAF 
ID   G3T3V2_LOXAF            Unreviewed;       441 AA.
AC   G3T3V2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Exosome complex component RRP45 {ECO:0000256|ARBA:ARBA00019572};
DE   AltName: Full=Exosome component 9 {ECO:0000256|ARBA:ARBA00032660};
GN   Name=EXOSC9 {ECO:0000313|Ensembl:ENSLAFP00000007979.2};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000007979.2, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000007979.2, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007979.2,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000007979.2}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007979.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the RNase PH family.
CC       {ECO:0000256|ARBA:ARBA00006678}.
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DR   AlphaFoldDB; G3T3V2; -.
DR   STRING; 9785.ENSLAFP00000007979; -.
DR   Ensembl; ENSLAFT00000009513.2; ENSLAFP00000007979.2; ENSLAFG00000009514.2.
DR   eggNOG; KOG1614; Eukaryota.
DR   GeneTree; ENSGT00950000183130; -.
DR   HOGENOM; CLU_038194_7_0_1; -.
DR   InParanoid; G3T3V2; -.
DR   OMA; GPQFENG; -.
DR   TreeFam; TF300092; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0000228; C:nuclear chromosome; IEA:Ensembl.
DR   GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IEA:Ensembl.
DR   GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IEA:Ensembl.
DR   GO; GO:0071028; P:nuclear mRNA surveillance; IEA:Ensembl.
DR   GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IEA:Ensembl.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0006396; P:RNA processing; IEA:Ensembl.
DR   CDD; cd11368; RNase_PH_RRP45; 1.
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   InterPro; IPR033100; Rrp45.
DR   PANTHER; PTHR11097:SF14; EXOSOME COMPLEX COMPONENT RRP45; 1.
DR   PANTHER; PTHR11097; EXOSOME COMPLEX EXONUCLEASE RIBOSOMAL RNA PROCESSING PROTEIN; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT   DOMAIN          32..163
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF01138"
FT   DOMAIN          189..254
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF03725"
FT   REGION          341..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..367
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..441
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  49228 MW;  E5259F445013F972 CRC64;
     MKETPLSNCE RRFLLRAIEE KKRLDGRQTY DYRNIKISFG TDYGCCIVEL GKTRVLGQVS
     CELVSPKLNR ATEGILFFNL ELSQMAAPAF EPGRQSDLLV KLNRLLERCL RNSKCIDTES
     LCVVAGEKVW QIRVDLHLLN HDGNIIDAAS IAAIVALCHF RRPDVSVQGD EVTLYTPEER
     DPVPLSIHHM PICVSFAFFQ QGTYLLVDPN EREERVMDGL LVIAMNKHRE ICTIQSSGGI
     MLLKDQVLRC SKIAGVKVAE ITELIQKALE NDQKVRHRKE GGKFGFAESI ANQRITAFKM
     EKAPIDTSDV GEKAEEIIAE AEPPSEVVSN PVLWTPGTAQ IGEGIENSWG DLEDSEKEDE
     DEGGSEEAVI LDSVKMDAGV ISNIGSQDAP IVLSDSEEEE MIILEPDKNP KKIRTQTISV
     KQEKAASKKP MKKRKKKRAV N
//
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