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Database: UniProt
Entry: A0A150V683_9PEZI
LinkDB: A0A150V683_9PEZI
Original site: A0A150V683_9PEZI 
ID   A0A150V683_9PEZI        Unreviewed;       336 AA.
AC   A0A150V683;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Exoribonuclease phosphorolytic domain-containing protein {ECO:0000259|Pfam:PF01138};
GN   ORFNames=M433DRAFT_66017 {ECO:0000313|EMBL:KYG46039.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG46039.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG46039.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG46039.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- SIMILARITY: Belongs to the RNase PH family.
CC       {ECO:0000256|ARBA:ARBA00006678}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYG46039.1}.
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DR   EMBL; JPDO01000133; KYG46039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150V683; -.
DR   STRING; 766039.A0A150V683; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:UniProt.
DR   CDD; cd11371; RNase_PH_MTR3; 1.
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   Exosome {ECO:0000256|ARBA:ARBA00022835};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT   DOMAIN          40..205
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF01138"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   336 AA;  36179 MW;  7A7750992134DFB1 CRC64;
     MQAADRRRIN APAGGTTPPV FNAPKDVQLQ RPSRTRTANE HRKIFLRTGI VPSASGSAYF
     ELPPQRQSDE REIFAPSSSN LKISCTVHGP RPLPRNAQFS PNLLLSANIK FAPFATRNRR
     GYVRDGTERD LSVHLETALR GVVIGERFPK SACDVVITVL EGEEDSWWVD SSEDSGGGNR
     SGWGAMTVLA GCITAASAAL VDAGIDCLDL VSGGVAAITS DAFTTVEQSK EVLILDPSPA
     EHETISAACV VAYLQSRDEI TEMWLKGDPG SREQMEKLVD EAVKAATLSR TVLEDAVKDG
     VDMKMKMKNQ ANDSSGASKQ NTSKGENESG DIIMTD
//
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