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Database: UniProt
Entry: A5DGL1_PICGU
LinkDB: A5DGL1_PICGU
Original site: A5DGL1_PICGU 
ID   A5DGL1_PICGU            Unreviewed;       242 AA.
AC   A5DGL1;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 2.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDK38314.2};
GN   ORFNames=PGUG_02412 {ECO:0000313|EMBL:EDK38314.2};
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK38314.2, ECO:0000313|Proteomes:UP000001997};
RN   [1] {ECO:0000313|EMBL:EDK38314.2, ECO:0000313|Proteomes:UP000001997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC   Y-324 {ECO:0000313|Proteomes:UP000001997};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- SIMILARITY: Belongs to the RNase PH family.
CC       {ECO:0000256|ARBA:ARBA00006678}.
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DR   EMBL; CH408157; EDK38314.2; -; Genomic_DNA.
DR   RefSeq; XP_001484683.1; XM_001484633.1.
DR   AlphaFoldDB; A5DGL1; -.
DR   STRING; 294746.A5DGL1; -.
DR   GeneID; 5126715; -.
DR   KEGG; pgu:PGUG_02412; -.
DR   VEuPathDB; FungiDB:PGUG_02412; -.
DR   eggNOG; KOG1068; Eukaryota.
DR   HOGENOM; CLU_063514_0_1_1; -.
DR   InParanoid; A5DGL1; -.
DR   OMA; ECRINTH; -.
DR   OrthoDB; 202892at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0000177; C:cytoplasmic exosome (RNase complex); IEA:UniProt.
DR   GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:UniProt.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProt.
DR   GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IEA:UniProt.
DR   GO; GO:0016075; P:rRNA catabolic process; 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:UP000001997};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT   DOMAIN          21..151
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF01138"
FT   DOMAIN          155..218
FT                   /note="Exoribonuclease phosphorolytic"
FT                   /evidence="ECO:0000259|Pfam:PF03725"
SQ   SEQUENCE   242 AA;  27260 MW;  C63C9E0124478063 CRC64;
     MSRLELYSPE GLRVDGRRWN ELRRFECKIN THPNSSTGSS YVEQGNTKVI CMVEGPSEPE
     TRSQVDVSRA TIEVNIAVAS FSTIERKKRL KNEKRIIELK ATMERTFEQS VICKLYPRTV
     IKVNLHVLAQ DGGMLATMIN ATTLALIDAG IAMYDYVAAV AAGLHNETPL LDLNTLEEND
     MSHLTLGVIG KSEKLAVLML EDKMPMDRLE PVLAIGIAGS HRIRELMDQE TRRHGERRVK
     RK
//
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