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NAF1_SCHPO
ID   NAF1_SCHPO              Reviewed;         516 AA.
AC   O14360;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=H/ACA ribonucleoprotein complex non-core subunit NAF1;
DE   AltName: Full=Nuclear assembly factor 1;
GN   Name=naf1; ORFNames=SPBC30D10.15;
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).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND SER-366, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: RNA-binding protein required for the maturation of box H/ACA
CC       snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA
CC       snoRNPs complex, it associates with the complex and disappears during
CC       maturation of the complex and is replaced by GAR1 to yield mature H/ACA
CC       snoRNPs complex (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: During assembly of the complex, component of the small
CC       nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs
CC       (H/ACA snoRNPs) which contains cbf5, naf1, nhp2 and nop10 proteins.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Absent from the
CC       nucleolus. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NAF1 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB10810.1; -; Genomic_DNA.
DR   PIR; T40181; T40181.
DR   RefSeq; NP_596270.1; NM_001022191.2.
DR   AlphaFoldDB; O14360; -.
DR   SMR; O14360; -.
DR   BioGRID; 276878; 1.
DR   STRING; 4896.SPBC30D10.15.1; -.
DR   iPTMnet; O14360; -.
DR   MaxQB; O14360; -.
DR   PaxDb; O14360; -.
DR   PRIDE; O14360; -.
DR   EnsemblFungi; SPBC30D10.15.1; SPBC30D10.15.1:pep; SPBC30D10.15.
DR   GeneID; 2540349; -.
DR   KEGG; spo:SPBC30D10.15; -.
DR   PomBase; SPBC30D10.15; -.
DR   VEuPathDB; FungiDB:SPBC30D10.15; -.
DR   eggNOG; KOG2236; Eukaryota.
DR   HOGENOM; CLU_528026_0_0_1; -.
DR   InParanoid; O14360; -.
DR   OMA; EQPCKIP; -.
DR   PRO; PR:O14360; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR   GO; GO:0005654; C:nucleoplasm; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0030515; F:snoRNA binding; ISM:PomBase.
DR   GO; GO:0000493; P:box H/ACA snoRNP assembly; ISO:PomBase.
DR   GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IC:PomBase.
DR   Gene3D; 2.40.10.230; -; 1.
DR   InterPro; IPR038664; Gar1/Naf1_Cbf5-bd_sf.
DR   InterPro; IPR007504; H/ACA_rnp_Gar1/Naf1.
DR   InterPro; IPR040309; Naf1.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR31633; PTHR31633; 1.
DR   Pfam; PF04410; Gar1; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..516
FT                   /note="H/ACA ribonucleoprotein complex non-core subunit
FT                   NAF1"
FT                   /id="PRO_0000116502"
FT   REGION          174..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          489..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         366
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   516 AA;  57639 MW;  22597CE8E5AF9B5F CRC64;
     MYPHLPCKIP GLSLIYDDES KVEKSKQLST NASSSNFVKE DQIPSNLSID NINTPQGDPI
     DKNNLNTNTE NNLPNIVNFQ NISSANSGEI KQKDNEILFS STEDINQHKE NYQDENKIDL
     LDVALANPKD CVVPSSGLLM PKEEFISNEE VGIPATNSSE KSNVKIADEI AEVTHSNSSI
     GKSSADLSSD SSSDSESNTS FSETDVEEEK AEEKSDAESM APSTPPKTVN ELPEQIYEKP
     EIVLQPNSLI EPLGKIIQVL KREVVVKSDI DDEKIVFDEK TVLCFEDRSI IGYIHETFGP
     VSSPYYIVRF STEEECSAIN ACMGRPVFYV PTMANKIDPE PLKYIKGSDA SNVYDEEINP
     SEQEFSDDEA EVAAKQLKKK RKRKAKSMVS GNQALPGEAN FQSLNQNNVR NYPFYQTNQG
     SNPPAKRFTQ EPPSSSLYSL SESSINYSTQ SPMYYNYNYP QPSFPPFHPI YNDSIGYYSQ
     ANPQMYYANQ VSAPPPQGSF DPNSKFYRNS SDSYRK
 
 
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