ID   NOB1_PONAB              Reviewed;         411 AA.
AC   Q5RBB3; Q5RED4;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=RNA-binding protein NOB1;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q9FLL1};
GN   Name=NOB1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in mRNA degradation (By similarity).
CC       Endonuclease required for processing of 20S pre-rRNA precursor and
CC       biogenesis of 40S ribosomal subunits (By similarity).
CC       {ECO:0000250|UniProtKB:Q9FLL1, ECO:0000250|UniProtKB:Q9ULX3}.
CC   -!- SUBUNIT: May interact with UPF2 (By similarity). Component of the small
CC       ribosomal subunit, ribosomal RNA processing complex (SSU RRP complex)
CC       (By similarity). {ECO:0000250|UniProtKB:Q9FLL1,
CC       ECO:0000250|UniProtKB:Q9ULX3}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULX3}.
CC   -!- SIMILARITY: Belongs to the NOB1 family. {ECO:0000305}.
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DR   EMBL; CR857596; CAH89873.1; -; Transcribed_RNA.
DR   EMBL; CR858738; CAH90947.1; -; mRNA.
DR   RefSeq; NP_001127354.1; NM_001133882.1.
DR   AlphaFoldDB; Q5RBB3; -.
DR   SMR; Q5RBB3; -.
DR   STRING; 9601.ENSPPYP00000008479; -.
DR   Ensembl; ENSPPYT00000008825; ENSPPYP00000008479; ENSPPYG00000007509.
DR   GeneID; 100174418; -.
DR   KEGG; pon:100174418; -.
DR   CTD; 28987; -.
DR   eggNOG; KOG2463; Eukaryota.
DR   GeneTree; ENSGT00390000015857; -.
DR   HOGENOM; CLU_024666_0_0_1; -.
DR   InParanoid; Q5RBB3; -.
DR   OMA; GYELECE; -.
DR   OrthoDB; 765237at2759; -.
DR   TreeFam; TF105838; -.
DR   Proteomes; UP000001595; Chromosome 16.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000469; P:cleavage involved in rRNA processing; IEA:InterPro.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR   CDD; cd09876; PIN_Nob1-like; 1.
DR   Gene3D; 6.20.210.10; -; 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; IPR002716; PIN_dom.
DR   InterPro; IPR033411; Ribonuclease_PIN.
DR   InterPro; IPR033461; WRNPLPNID.
DR   PANTHER; PTHR12814; PTHR12814; 1.
DR   Pfam; PF08772; NOB1_Zn_bind; 1.
DR   Pfam; PF17146; PIN_6; 1.
DR   Pfam; PF15017; WRNPLPNID; 1.
DR   PIRSF; PIRSF037125; D-site_20S_pre-rRNA_nuclease; 1.
DR   SMART; SM00670; PINc; 1.
DR   SUPFAM; SSF144206; SSF144206; 1.
PE   2: Evidence at transcript level;
KW   Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..411
FT                   /note="RNA-binding protein NOB1"
FT                   /id="PRO_0000233268"
FT   DOMAIN          5..108
FT                   /note="PINc"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         259..331
FT                   /note="NOB1"
FT                   /evidence="ECO:0000255"
FT   REGION          120..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..197
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT   BINDING         284
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT   BINDING         287
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT   CONFLICT        20
FT                   /note="L -> LQ (in Ref. 1; CAH89873)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   411 AA;  46500 MW;  73601D5EBB91FEA9 CRC64;
     MAPVEHVVAD AGAFLRDAAL QDIGKNIYTI REVVTEIRDK ATRRRLAVLP YELRFKEPLP
     EYVRLVTEFS KKTGDYPSLS ATDIQVLALT YQLEAEFVGV SHLKQEPQKV KVSSSIQHPE
     TPLHISGFHL PSKPKPPQET EKGHPACEPE NLEFSSFMFW RNPLPNIDHE LQELLIDRGE
     DIPSDEEEEE NGFEDRRDDS DDDGGGWITP SNIKQIQQEL EQCDVPEDVR VGCVTTDFAM
     QNVLLQMGLH VLAVNGMLIR EARSYILRCH GCFKTTSDMS RVFCSHCGNK TLKKVSVTVS
     DDGTLHMHFS RNPKVLNPRG LRYSLPTPKG GKYAINPHLT EDQRFPQLRL SRKARQKTNV
     FAPDYVAGVS PFVENDISSR SATLQVRDSS LGAGRRRLNP NASRRKFVKK R