ID   NOB1_MACFA              Reviewed;         412 AA.
AC   Q4R537;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=RNA-binding protein NOB1;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q9FLL1};
GN   Name=NOB1; ORFNames=QccE-20755;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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; AB169707; BAE01788.1; -; mRNA.
DR   RefSeq; NP_001270471.1; NM_001283542.1.
DR   AlphaFoldDB; Q4R537; -.
DR   SMR; Q4R537; -.
DR   STRING; 9541.XP_005592453.1; -.
DR   PRIDE; Q4R537; -.
DR   GeneID; 101866049; -.
DR   CTD; 28987; -.
DR   eggNOG; KOG2463; Eukaryota.
DR   OrthoDB; 765237at2759; -.
DR   Proteomes; UP000233100; Unplaced.
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   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..412
FT                   /note="RNA-binding protein NOB1"
FT                   /id="PRO_0000233266"
FT   DOMAIN          5..108
FT                   /note="PINc"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         260..332
FT                   /note="NOB1"
FT                   /evidence="ECO:0000255"
FT   REGION          121..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT   BINDING         285
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT   BINDING         288
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         201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT   MOD_RES         325
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULX3"
SQ   SEQUENCE   412 AA;  46456 MW;  4D242217417F0870 CRC64;
     MAPVEHVVAD AGAFLRDAAL QDIGKNIYTI REVVTEIRDK ATRRRLAVLP YELRFKEPLP
     QYVRLVTEFS KKTGDYPSLS ATDIQVLALT YQLEAEFVGV SHLKQEPQKV KVSSSIQHPE
     TPLHISGFHL PSKPKSPQEA EKGHPACEPE NLEFSSFMFW RNPLPSIDHE LQELLIDRSE
     DVPSKEEEEA ENGFEDRKDD SDDDGGGWIT PNNIKQIQQE LEQCDVPKDV RVGCVTTDFA
     MQNVLLQMGL HVLAVNGMLI REARSYILRC HGCFKTTSDM SRVFCAHCGN KTLKKVSVTV
     SDDGALHMHF SRNPKVLNPR GLRYSLPTPK GGKYAVNPHL TEDQRFPQLR LSRKARQKTN
     VFAPDYIAGV SPFVENDVSS RSATLQVRDS TLGAGRRRLN PNASRKKFVK KR