ID A8PWL8_MALGO Unreviewed; 291 AA.
AC A8PWL8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Ribosomal RNA-processing protein 42 {ECO:0000256|ARBA:ARBA00042523};
GN ORFNames=MGL_1145 {ECO:0000313|EMBL:EDP44663.1};
OS Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP44663.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP44663.1, ECO:0000313|Proteomes:UP000008837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT virulence traits shared with plant and human fungal pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EDP44663.1}.
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DR EMBL; AAYY01000003; EDP44663.1; -; Genomic_DNA.
DR RefSeq; XP_001731877.1; XM_001731825.1.
DR AlphaFoldDB; A8PWL8; -.
DR STRING; 425265.A8PWL8; -.
DR GeneID; 5856182; -.
DR KEGG; mgl:MGL_1145; -.
DR VEuPathDB; FungiDB:MGL_1145; -.
DR InParanoid; A8PWL8; -.
DR OMA; LMSAENC; -.
DR OrthoDB; 197480at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:UniProt.
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; PTHR11097:SF8; EXOSOME COMPLEX COMPONENT RRP42; 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 Exosome {ECO:0000256|ARBA:ARBA00022835};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837}.
FT DOMAIN 3..147
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF01138"
FT DOMAIN 211..276
FT /note="Exoribonuclease phosphorolytic"
FT /evidence="ECO:0000259|Pfam:PF03725"
SQ SEQUENCE 291 AA; 32099 MW; B9CB0D313809B2BD CRC64;
MSEQADGCAR VTLGSTEVMC GVKLEMDSQE APTVTVSQGE RKIDFTPWLP SKPCIQVQVD
YTPSLLREHN ASELSMLTST MQDMLQACYA FSGDSYGPLP ARQFVVVPYA KYWVLHVDVY
VMSWSGGNVL DTVFAAVFCA LWNTRIPETR VMAMDRTNQG EQDAMNEDHD DPAGIKFITR
GRKNTSQNTN AVDYALVNEW EHGRALEGRE DVPVCVSVYP FQGTFLLDPT LEEECALSCC
VAVLASPQGR LYGVRQRGEG ELTLDSIHKA TEVGLQYAKL LAQSLPASLP A
//