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Database: UniProt
Entry: A0A0D2JK39_9EURO
LinkDB: A0A0D2JK39_9EURO
Original site: A0A0D2JK39_9EURO 
ID   A0A0D2JK39_9EURO        Unreviewed;       424 AA.
AC   A0A0D2JK39;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 36.
DE   RecName: Full=20S-pre-rRNA D-site endonuclease NOB1 {ECO:0000256|PIRNR:PIRNR037125};
GN   ORFNames=Z518_00931 {ECO:0000313|EMBL:KIX09850.1};
OS   Rhinocladiella mackenziei CBS 650.93.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Rhinocladiella.
OX   NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX09850.1, ECO:0000313|Proteomes:UP000053617};
RN   [1] {ECO:0000313|EMBL:KIX09850.1, ECO:0000313|Proteomes:UP000053617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX09850.1,
RC   ECO:0000313|Proteomes:UP000053617};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the synthesis of 40S ribosome subunits. Has a
CC       role in processing 20S pre-rRNA into the mature 18S rRNA, where it is
CC       required for cleavage at the 3' end of the mature 18S rRNA (D-site).
CC       Accompanies the 20S pre-rRNA from the nucleus to the cytoplasm.
CC       {ECO:0000256|PIRNR:PIRNR037125}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|PIRNR:PIRNR037125}.
CC   -!- SIMILARITY: Belongs to the NOB1 family. {ECO:0000256|ARBA:ARBA00005858,
CC       ECO:0000256|PIRNR:PIRNR037125}.
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DR   EMBL; KN847475; KIX09850.1; -; Genomic_DNA.
DR   RefSeq; XP_013276986.1; XM_013421532.1.
DR   AlphaFoldDB; A0A0D2JK39; -.
DR   STRING; 1442369.A0A0D2JK39; -.
DR   GeneID; 25289002; -.
DR   VEuPathDB; FungiDB:Z518_00931; -.
DR   HOGENOM; CLU_024666_2_0_1; -.
DR   OrthoDB; 5473723at2759; -.
DR   Proteomes; UP000053617; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:InterPro.
DR   CDD; cd09876; PIN_Nob1-like; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 6.20.210.10; Nin one binding (NOB1), Zn-ribbon-like; 1.
DR   InterPro; IPR039907; NOB1.
DR   InterPro; IPR017117; Nob1_euk.
DR   InterPro; IPR036283; NOB1_Zf-like_sf.
DR   InterPro; IPR014881; NOB1_Zn-bd.
DR   InterPro; IPR033411; Ribonuclease_PIN.
DR   PANTHER; PTHR12814; RNA-BINDING PROTEIN NOB1; 1.
DR   PANTHER; PTHR12814:SF2; RNA-BINDING PROTEIN NOB1; 1.
DR   Pfam; PF08772; NOB1_Zn_bind; 1.
DR   Pfam; PF17146; PIN_6; 1.
DR   PIRSF; PIRSF037125; D-site_20S_pre-rRNA_nuclease; 1.
DR   SUPFAM; SSF144206; NOB1 zinc finger-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR037125}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR037125}.
FT   DOMAIN          16..107
FT                   /note="Ribonuclease PIN"
FT                   /evidence="ECO:0000259|Pfam:PF17146"
FT   DOMAIN          273..344
FT                   /note="Nin one binding (NOB1) Zn-ribbon-like"
FT                   /evidence="ECO:0000259|Pfam:PF08772"
FT   REGION          120..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          177..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         283
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
SQ   SEQUENCE   424 AA;  46372 MW;  F3FDC8EC7E24C935 CRC64;
     MSHTPQETET KPVHTIILDS SPLLLNTPGI STLLANGHVL VTTSSVLAEI RGEEARTRIE
     TLYKPFLTVR SPRPESVKRV KDFARKSGDA AVLSQTDFEI LALAYDIECE RNGGDWRLRA
     VPGQKRLNGT PPSKTKEEDD QSTPTDIDLS GTNDGNEVES LAGNIEKEIE SMTLGDTAHQ
     GQISSEQPPD PAPSSLEESE GTQTKEETSD SDDGWITPSN IKRRQAKDGA ASSKSQTETK
     HVQVATMTGD FAVQNVLLQM NLNLLSTKSC QRISQIKQFI LRCHGCFSTT KDTTKQFCPR
     CGKPTLTRVS CTINDKGEVK LHLKANMQWN TKGNVYAIPK PVSGSSNQKW KGPRSGGGQG
     GWGNDLILAE DQKEYIRAMA AMKRTKEKDL MDEDTLPSIL TGNRGHTSGR PRVGAGKSVN
     SQKR
//
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