NOB1_RAT
ID NOB1_RAT Reviewed; 410 AA.
AC Q6VEU1; A0JN09;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=RNA-binding protein NOB1;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q9FLL1};
GN Name=Nob1; Synonyms=Nob1p;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Zhou G., Zhang Y., Ni J.;
RT "Mammalian NOB1 interact with Nob1p.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; AY341886; AAQ24170.1; -; mRNA.
DR EMBL; BC126076; AAI26077.1; -; mRNA.
DR RefSeq; NP_954517.1; NM_199086.1.
DR AlphaFoldDB; Q6VEU1; -.
DR SMR; Q6VEU1; -.
DR STRING; 10116.ENSRNOP00000031905; -.
DR PhosphoSitePlus; Q6VEU1; -.
DR jPOST; Q6VEU1; -.
DR PaxDb; Q6VEU1; -.
DR GeneID; 291996; -.
DR KEGG; rno:291996; -.
DR UCSC; RGD:735222; rat.
DR CTD; 28987; -.
DR RGD; 735222; Nob1.
DR VEuPathDB; HostDB:ENSRNOG00000021890; -.
DR eggNOG; KOG2463; Eukaryota.
DR HOGENOM; CLU_024666_0_0_1; -.
DR InParanoid; Q6VEU1; -.
DR OMA; GYELECE; -.
DR OrthoDB; 765237at2759; -.
DR PhylomeDB; Q6VEU1; -.
DR TreeFam; TF105838; -.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q6VEU1; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000021890; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q6VEU1; RN.
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; ISO:RGD.
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 GO; GO:0007601; P:visual perception; ISO:RGD.
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..410
FT /note="RNA-binding protein NOB1"
FT /id="PRO_0000233269"
FT DOMAIN 5..108
FT /note="PINc"
FT /evidence="ECO:0000255"
FT ZN_FING 258..330
FT /note="NOB1"
FT /evidence="ECO:0000255"
FT REGION 180..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..202
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT BINDING 283
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 MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX3"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX3"
SQ SEQUENCE 410 AA; 46425 MW; 9F7F843A52310F4C CRC64;
MAPVEHVVAD AGAFLRDAPL QDIGKNIYTI REVVREIRDK ATRRRLAVLP YELRFKEPFP
EYVRLVTEFS KKTGDYPSLS ATDIQVLALT YQLEAEFVGV SHLKKEPEKV KVSSSIQHPE
TPLHISGFHL PSKSKALQET VDHGPPADGS ENLEFSSFMF WRNPLPNIDH ELQQLLIDGR
EEEEEEEEEE EEEDELEDSD DDGGGWITPS NIKQIQHESE QCDIPKDVQV GCVTTDFAMQ
NVLLQMGLHV LAVNGMLVRE ARSYILRCHG CFKTTSDMNR VFCGHCGNKT LKKVSVTIND
DGTLHMHFSR NPKVLNPRGL RYSLPTPKGG KYAVNPHLTE DQRFPQLRLS HKARQKTNVF
APDYIAGVSP FAENDISSRS AILQVRDSML GAGRRRLNPN ASRKKFVKKR
