ID   A0A178DXB9_9PLEO        Unreviewed;       291 AA.
AC   A0A178DXB9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Exoribonuclease {ECO:0000313|EMBL:OAL48406.1};
GN   ORFNames=IQ07DRAFT_571059 {ECO:0000313|EMBL:OAL48406.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL48406.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL48406.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL48406.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; KV441649; OAL48406.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178DXB9; -.
DR   STRING; 765867.A0A178DXB9; -.
DR   InParanoid; A0A178DXB9; -.
DR   OrthoDB; 128403at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:UniProt.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
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:UP000077535};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT   DOMAIN          33..164
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF01138"
FT   DOMAIN          190..256
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF03725"
SQ   SEQUENCE   291 AA;  32388 MW;  7628094B61FBB127 CRC64;
     MPREAEISLN EREFIKQALQ EQVRLDGRAF DAFRPVELTF GEEYGVADVQ LGKTRVLARI
     SVDVTTPLPE RKFDGIFQIV TEFSPMASPT FEVGRPTDAE VILSRILEKA IRRSNAFDTE
     SLCIIAGLKC FALRADVHII DHDGGLIDAS CIAVMAALQH FRRPDVLVEG EKATILSVRE
     REPVPLSILH QPLCVTFSYF EEEVFLVDAN LAEEQVRQGE VIVTMNKHGE VCQIAKYGGA
     TVDALSLLNC TKIALEKVKE MTVFIQKRLN EDAKIRDAGG LMAELSAENA R
//