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Database: UniProt
Entry: K1XK90_MARBU
LinkDB: K1XK90_MARBU
Original site: K1XK90_MARBU 
ID   K1XK90_MARBU            Unreviewed;       366 AA.
AC   K1XK90;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Ribosomal RNA-processing protein 42 {ECO:0000256|ARBA:ARBA00042523};
GN   ORFNames=MBM_09093 {ECO:0000313|EMBL:EKD12864.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD12864.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD12864.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD12864.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
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   EMBL; JH921454; EKD12864.1; -; Genomic_DNA.
DR   RefSeq; XP_007296982.1; XM_007296920.1.
DR   AlphaFoldDB; K1XK90; -.
DR   STRING; 1072389.K1XK90; -.
DR   GeneID; 18765028; -.
DR   KEGG; mbe:MBM_09093; -.
DR   eggNOG; KOG1612; Eukaryota.
DR   HOGENOM; CLU_046570_0_0_1; -.
DR   InParanoid; K1XK90; -.
DR   OMA; INKRWHW; -.
DR   OrthoDB; 2070785at2759; -.
DR   Proteomes; UP000006753; 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; 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   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:UP000006753}.
FT   REGION          79..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   366 AA;  39655 MW;  F52B7D57C20875E1 CRC64;
     MAPSSTQQVL LSPAELSYLH TSLSLTPPIR PDSRSPSQFR PLVAESNILP GTNGSARICF
     ADGTEAIVGV KAEVEKSRPS WNVVEGEDED GESEGEGEGD GEKKKRALNE WVEIGVEIPG
     MRDDDSMPVF LAALLSEALL ADGGFTQRLW INARFHWKLY LDILLLSQPL SYPLPLLSLT
     THLALLSTRL PKLKSEGDED PLFDDDWDAS VYIYPREAQA AHARPPVTLL VMAVKENIIF
     DPSKEELAVA EVVLAVSVGE RAQGRGGMEI DGKTRDLRLL SVRTIDPPSR LTAPGLPNRS
     NTATGGTATT NEQAASQREP MEEEGVWQPP RGGAKRKVIA AMIQKVLEHG GVAEEVLDGL
     DGVELG
//
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