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BYR3_SCHPO
ID   BYR3_SCHPO              Reviewed;         179 AA.
AC   P36627;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Cellular nucleic acid-binding protein homolog;
GN   Name=byr3; ORFNames=SPAC13D6.02c;
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 [GENOMIC DNA].
RC   STRAIN=SP870;
RX   PubMed=1515675; DOI=10.1091/mbc.3.7.721;
RA   Xu H.-P., Rajavashisth T., Grewal N., Jung V., Riggs M., Rodgers L.,
RA   Wigler M.;
RT   "A gene encoding a protein with seven zinc finger domains acts on the
RT   sexual differentiation pathways of Schizosaccharomyces pombe.";
RL   Mol. Biol. Cell 3:721-734(1992).
RN   [2]
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: Acts in the sexual differentiation pathway. Is required for
CC       efficient conjugation. Double-stranded DNA-binding protein.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: To human CNBP and to retroviral nucleic acid binding
CC       proteins (NBP). {ECO:0000305}.
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DR   EMBL; S45038; AAB23116.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA93542.1; -; Genomic_DNA.
DR   PIR; T37622; T37622.
DR   RefSeq; NP_593680.1; NM_001019112.2.
DR   AlphaFoldDB; P36627; -.
DR   BioGRID; 279276; 33.
DR   STRING; 4896.SPAC13D6.02c.1; -.
DR   iPTMnet; P36627; -.
DR   MaxQB; P36627; -.
DR   PaxDb; P36627; -.
DR   PRIDE; P36627; -.
DR   EnsemblFungi; SPAC13D6.02c.1; SPAC13D6.02c.1:pep; SPAC13D6.02c.
DR   GeneID; 2542829; -.
DR   KEGG; spo:SPAC13D6.02c; -.
DR   PomBase; SPAC13D6.02c; byr3.
DR   VEuPathDB; FungiDB:SPAC13D6.02c; -.
DR   eggNOG; KOG4400; Eukaryota.
DR   HOGENOM; CLU_058879_2_0_1; -.
DR   InParanoid; P36627; -.
DR   OMA; SHQARDC; -.
DR   PhylomeDB; P36627; -.
DR   PRO; PR:P36627; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; ISO:PomBase.
DR   GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR   GO; GO:0008494; F:translation activator activity; ISO:PomBase.
DR   GO; GO:0045182; F:translation regulator activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISO:PomBase.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF00098; zf-CCHC; 7.
DR   SMART; SM00343; ZnF_C2HC; 7.
DR   SUPFAM; SSF57756; SSF57756; 4.
DR   PROSITE; PS50158; ZF_CCHC; 7.
PE   4: Predicted;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..179
FT                   /note="Cellular nucleic acid-binding protein homolog"
FT                   /id="PRO_0000065031"
FT   ZN_FING         17..34
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         36..53
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         58..75
FT                   /note="CCHC-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         83..100
FT                   /note="CCHC-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         116..133
FT                   /note="CCHC-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         135..152
FT                   /note="CCHC-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         157..174
FT                   /note="CCHC-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
SQ   SEQUENCE   179 AA;  19343 MW;  749B93904E645D60 CRC64;
     MESESVPTVP QTTRPGPRCY NCGENGHQAR ECTKGSICYN CNQTGHKASE CTEPQQEKTC
     YACGTAGHLV RDCPSSPNPR QGAECYKCGR VGHIARDCRT NGQQSGGRFG GHRSNMNCYA
     CGSYGHQARD CTMGVKCYSC GKIGHRSFEC QQASDGQLCY KCNQPGHIAV NCTSPVIEA
 
 
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