NOB1_BOVIN
ID NOB1_BOVIN Reviewed; 413 AA.
AC Q3T042; Q7YRC5;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=RNA-binding protein NOB1;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q9FLL1};
GN Name=NOB1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou G., Li W., Yu L.;
RT "Cloning of Bos taurus nin one binding protein (Nob1p).";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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; AY336977; AAQ16153.1; -; mRNA.
DR EMBL; BC102577; AAI02578.1; -; mRNA.
DR RefSeq; NP_898906.1; NM_183083.1.
DR AlphaFoldDB; Q3T042; -.
DR SMR; Q3T042; -.
DR STRING; 9913.ENSBTAP00000027497; -.
DR PaxDb; Q3T042; -.
DR PRIDE; Q3T042; -.
DR GeneID; 360191; -.
DR KEGG; bta:360191; -.
DR CTD; 28987; -.
DR eggNOG; KOG2463; Eukaryota.
DR InParanoid; Q3T042; -.
DR OrthoDB; 765237at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
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:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
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..413
FT /note="RNA-binding protein NOB1"
FT /id="PRO_0000233264"
FT DOMAIN 5..108
FT /note="PINc"
FT /evidence="ECO:0000255"
FT ZN_FING 261..333
FT /note="NOB1"
FT /evidence="ECO:0000255"
FT REGION 116..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT CONFLICT 349
FT /note="Q -> S (in Ref. 1; AAQ16153)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="A -> G (in Ref. 1; AAQ16153)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="V -> G (in Ref. 1; AAQ16153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46563 MW; FC92B561873D708B CRC64;
MAPVEHVVAD AGAFLLDAAL QDIGKNIYTI RNVISEIRDK ATRRRLAVLP YELRFKEPFP
EYVRLVTEFS KKTGDYPSLS ATDIQVLALT YQLEAEFVGV SHLKQEPEKV KVSSSIQHPE
TPLHVSGFHL PSKPKPPRET VEHRHPASEP EDLEFSSFMF WRNPLPNIDC ELQELLMDGG
EDVPNEEEDE ENGLDERQDE DSDDDGGGWI TPSNIKQIQQ EMKQCAVPKD VRVGCVTTDF
AMQNVLLQMG LHVLAVNGML IREARSYILR CHGCFKTTSD MSRVFCAHCG NKTLKKVSVT
VSDDGTLHMH FSRNPKVLNP RGLRYSLPTP KGGKYAINPH LTEDQRFPQL RLSRKARQKT
DVFAPDYVAG VSPFAENDIS SRSATLQVRD STLGAGRRRL NPNASRKKFV KKR
