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NOB1_SCHPO
ID   NOB1_SCHPO              Reviewed;         388 AA.
AC   Q9UTK0;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=20S-pre-rRNA D-site endonuclease nob1;
DE            EC=3.1.-.-;
DE   AltName: Full=Pre-rRNA-processing endonuclease nob1;
GN   Name=nob1; ORFNames=SPAC1486.09;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Required for the synthesis of 40S ribosome subunits. Has a
CC       role in processing 20S pre-rRNA into the mature 18S rRNA, where it is
CC       required for cleavage at the 3' end of the mature 18S rRNA (D-site).
CC       Accompanies the 20S pre-rRNA from the nucleus to the cytoplasm (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit, ribosomal RNA
CC       processing complex (SSU RRP complex). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
CC   -!- SIMILARITY: Belongs to the NOB1 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB62419.1; -; Genomic_DNA.
DR   PIR; T50078; T50078.
DR   RefSeq; NP_594097.1; NM_001019521.2.
DR   AlphaFoldDB; Q9UTK0; -.
DR   SMR; Q9UTK0; -.
DR   BioGRID; 277953; 1.
DR   STRING; 4896.SPAC1486.09.1; -.
DR   iPTMnet; Q9UTK0; -.
DR   MaxQB; Q9UTK0; -.
DR   PaxDb; Q9UTK0; -.
DR   PRIDE; Q9UTK0; -.
DR   EnsemblFungi; SPAC1486.09.1; SPAC1486.09.1:pep; SPAC1486.09.
DR   GeneID; 2541448; -.
DR   KEGG; spo:SPAC1486.09; -.
DR   PomBase; SPAC1486.09; nob1.
DR   VEuPathDB; FungiDB:SPAC1486.09; -.
DR   eggNOG; KOG2463; Eukaryota.
DR   HOGENOM; CLU_024666_2_0_1; -.
DR   InParanoid; Q9UTK0; -.
DR   OMA; DYAMQNT; -.
DR   PhylomeDB; Q9UTK0; -.
DR   Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   PRO; PR:Q9UTK0; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0030688; C:preribosome, small subunit precursor; ISO:PomBase.
DR   GO; GO:0004521; F:endoribonuclease activity; ISO:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; ISO:PomBase.
DR   GO; GO:0000478; P:endonucleolytic cleavage involved in rRNA processing; ISO:PomBase.
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   PANTHER; PTHR12814; PTHR12814; 1.
DR   Pfam; PF08772; NOB1_Zn_bind; 1.
DR   Pfam; PF17146; PIN_6; 1.
DR   PIRSF; PIRSF037125; D-site_20S_pre-rRNA_nuclease; 1.
DR   SMART; SM00670; PINc; 1.
DR   SUPFAM; SSF144206; SSF144206; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW   Reference proteome; Ribosome biogenesis; Zinc; Zinc-finger.
FT   CHAIN           1..388
FT                   /note="20S-pre-rRNA D-site endonuclease nob1"
FT                   /id="PRO_0000374003"
FT   DOMAIN          6..108
FT                   /note="PINc"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         246..317
FT                   /note="NOB1"
FT                   /evidence="ECO:0000255"
FT   REGION          110..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          311..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BW10"
FT   BINDING         259
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         274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BW10"
SQ   SEQUENCE   388 AA;  43874 MW;  4DEF30DD19E75394 CRC64;
     MSKSITHLVL DTGGIICSST LLRNSAESFY TIPRVIAEIR DETSRKNFEL WGDQVIQRVP
     KPEFIKKVSE FAKQTGDYSS LSVTDIQILA LTYELEVEFN GGDWRLRKYP GQKHINGKPP
     SNSNSTEDAS KPTSSDTASV KETENSDPKS AENEVLEGET TQHSNNKEAH PNTEENKEQE
     DNEEDDEDDG WITPSNIRKK KAEDGVGESL VQPKHLKVAC ATTDFSMQNV LLQIGLNLVS
     SDGFKIQNVK RFVLRCHGCY TVVKDMEKKF CPSCGGNTLI KTTCSINSKG EFQVHLKKNF
     EWKTRGTKYS LPKPVHGTSN GKGKKNPVLR EDQPEYQRAV RRMQRKKEID LMDEDYLPSL
     LTGVTKDRMY VQIGAGRKNP NEVRRKKR
 
 
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