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Database: UniProt
Entry: G3Q005_GASAC
LinkDB: G3Q005_GASAC
Original site: G3Q005_GASAC 
ID   G3Q005_GASAC            Unreviewed;       441 AA.
AC   G3Q005;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=RNA-binding protein NOB1 {ECO:0000256|PIRNR:PIRNR037125};
GN   Name=NOB1 {ECO:0000313|Ensembl:ENSGACP00000023195.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000023195.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000023195.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000023195.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May play a role in mRNA degradation.
CC       {ECO:0000256|PIRNR:PIRNR037125}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {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   AlphaFoldDB; G3Q005; -.
DR   STRING; 69293.ENSGACP00000023195; -.
DR   Ensembl; ENSGACT00000023240.1; ENSGACP00000023195.1; ENSGACG00000017552.1.
DR   eggNOG; KOG2463; Eukaryota.
DR   GeneTree; ENSGT00390000015857; -.
DR   InParanoid; G3Q005; -.
DR   OMA; GYELECE; -.
DR   TreeFam; TF105838; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000017552; Expressed in embryo and 13 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; 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   InterPro; IPR033461; WRNPLPNID.
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   Pfam; PF15017; WRNPLPNID; 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:UP000007635};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR037125}.
FT   DOMAIN          16..102
FT                   /note="Ribonuclease PIN"
FT                   /evidence="ECO:0000259|Pfam:PF17146"
FT   DOMAIN          172..240
FT                   /note="Putative WW-binding"
FT                   /evidence="ECO:0000259|Pfam:PF15017"
FT   DOMAIN          289..361
FT                   /note="Nin one binding (NOB1) Zn-ribbon-like"
FT                   /evidence="ECO:0000259|Pfam:PF08772"
FT   REGION          150..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..233
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         314
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037125-1"
SQ   SEQUENCE   441 AA;  49293 MW;  73886533B43A19AE CRC64;
     VSDIVSKMAP ALVSHVVADA GAFIKRAPLQ EIGSIIYTLR DVVNEIRDKP TRKSLSFLPY
     QLTFKEPQPE HVRLVTEFSK KTGDYPSLSA TDIKVLALTY QLELEHVGSQ HLRKEPAVKV
     DVHNTLRHPE TPVNVAGFHF PSKVVSHRNM EPVKDLNPNI KQNQTKTSDD DEFNSFQFWR
     EPLRSIEDCL LDVLTLDEVS TPDSRLDPSV QSEDQSDEDK ENEPEDDDEE DGGGGGWITP
     GNIKQVTMDS ADWTAPADVI VGCLTTDFAM QNVLIQIGLH VLSVNGMLIK QARNYILRCH
     ACFRSTSIMN KVFCPHCGNP TLKKLAVTVG EDGTTKMHFS KNPKVLNPRG LRHPLPRPQG
     GKHSNNPQLV EDQSFPQQRL SRKARQKTDV FDPDYAAGAS PFSQNDIYSR AANLQIRDGQ
     QGGGRRRRNP NAAHKKCVKK L
//
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