位置:首页 > 蛋白库 > SPB4_SCHPO
SPB4_SCHPO
ID   SPB4_SCHPO              Reviewed;         606 AA.
AC   O74764;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=ATP-dependent rRNA helicase spb4 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:P25808};
GN   Name=spb4 {ECO:0000250|UniProtKB:P25808}; ORFNames=SPBC24C6.02;
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: ATP-binding RNA helicase involved in the biogenesis of 60S
CC       ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates
CC       from pre-60S ribosomal particles after processing of 27SB pre-rRNA.
CC       Required for the normal formation of 18S rRNA through the processing of
CC       pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and
CC       5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2.
CC       {ECO:0000250|UniProtKB:P25808}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC         Evidence={ECO:0000250|UniProtKB:P25808};
CC   -!- SUBUNIT: Component of pre-60S ribosomal complexes.
CC       {ECO:0000250|UniProtKB:P25808}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:P25808}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329671; CAA21146.1; -; Genomic_DNA.
DR   PIR; T39966; T39966.
DR   RefSeq; NP_595956.1; NM_001021865.2.
DR   AlphaFoldDB; O74764; -.
DR   SMR; O74764; -.
DR   BioGRID; 277124; 1.
DR   STRING; 4896.SPBC24C6.02.1; -.
DR   iPTMnet; O74764; -.
DR   MaxQB; O74764; -.
DR   PaxDb; O74764; -.
DR   PRIDE; O74764; -.
DR   EnsemblFungi; SPBC24C6.02.1; SPBC24C6.02.1:pep; SPBC24C6.02.
DR   GeneID; 2540598; -.
DR   KEGG; spo:SPBC24C6.02; -.
DR   PomBase; SPBC24C6.02; spb4.
DR   VEuPathDB; FungiDB:SPBC24C6.02; -.
DR   eggNOG; KOG0345; Eukaryota.
DR   HOGENOM; CLU_003041_26_4_1; -.
DR   InParanoid; O74764; -.
DR   OMA; DRAIHDK; -.
DR   PhylomeDB; O74764; -.
DR   PRO; PR:O74764; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR   GO; GO:0006364; P:rRNA processing; ISO:PomBase.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..606
FT                   /note="ATP-dependent rRNA helicase spb4"
FT                   /id="PRO_0000232332"
FT   DOMAIN          32..213
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          246..400
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          521..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          521..601
FT                   /evidence="ECO:0000255"
FT   MOTIF           1..29
FT                   /note="Q motif"
FT                   /evidence="ECO:0000305"
FT   MOTIF           161..164
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        547..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   606 AA;  68742 MW;  471BDD5BA576893B CRC64;
     MSFQSINIDK WLKNAVAAQG FKKMTPVQAN AIPLFLKNKD LVVEAVTGSG KTLAYLLPCF
     DKVTRRDTDE TGLGALIVAP TRELATQIFN VTKELLAYQP DSLDGGKKLV ADMYIGGKGT
     LTNDLASFRE KNPSVVIGTP GRLNEMLSHI SSKHLEILIL DEADTLIDMG FQRTLQSIIS
     QLPKQRRTGL FSATMNDTVS SFLKIAGLRN SVRVSVTVTS KKIDTRTPSS LAIQSLVIPP
     IYKVQCMIHL LCTIEYEKAI VFFSSCASVE YFNSLFLTYK LPFEIVALHG QQVQSNRSRN
     FEKFKKSNKK TVLFTTDIAS RGLDIPNVDF VLQLDPPLDP KSFSHRCGRA GRAGRAGVAI
     VLLNDGREEE YEELLRVRKV PITRIDTPIE ALDLSRLKVL THELRKIVSK DRDLYDKGLR
     AFVSHVRAYT KHHASFIFRI KDLDLGQLAT AYALLHLPKM PELKDTEISE NIFKKFDIDY
     ATIPYRDQVR EQARRRRLEV EKTEPKKLAR PAKIKNEAWS KQKEVKEKRN TRREKRKSKK
     EFLKAQKNEA SNNLKQEIVS KAGAQETEND DLIDEESDAL SELEEDYRQL KKSKKRKNQA
     SFGFSM
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024