ID A0A165CJ56_9APHY Unreviewed; 312 AA.
AC A0A165CJ56;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KZT02904.1};
GN ORFNames=LAESUDRAFT_762333 {ECO:0000313|EMBL:KZT02904.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT02904.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT02904.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT02904.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV427648; KZT02904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165CJ56; -.
DR STRING; 1314785.A0A165CJ56; -.
DR InParanoid; A0A165CJ56; -.
DR OrthoDB; 202892at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:UniProt.
DR CDD; cd11370; RNase_PH_RRP41; 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 PANTHER; PTHR11953; EXOSOME COMPLEX COMPONENT; 1.
DR PANTHER; PTHR11953:SF0; EXOSOME COMPLEX COMPONENT RRP41; 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 Exosome {ECO:0000256|ARBA:ARBA00022835};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT DOMAIN 65..195
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF01138"
FT DOMAIN 198..262
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF03725"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 34658 MW; 27EE5B4C5B91AB3F CRC64;
MRRQSRGRVS PRAQRRRSGY RNHWTLPASC EPSPFTLHPD NIQMSSRVEI LNDGGYRSDG
RRQYELRDII IDLSPQGTAD GSATVTHGLT QALVTVFGPR EAKMRSQTLH DRAVINVEMN
VLPFSTGERR RRARVDRRTL ELAAMIKSTF EPVIQTNLYP RSQIDIFVQV LQQDGGLLQT
CINATTLALA AAGIPLLDFV CAITGGVHTT SPVLDLTMLE ENDLPHLTVA VMPRTKKITL
VTLETRLHVD RFAEIFELAC EAGQTIHKEM KRAVKDRMST LVAAMGAGLT QGASGETAEQ
DAIMDGVVMY EY
//
