位置:首页 > 蛋白库 > SPB4_EMENI
SPB4_EMENI
ID   SPB4_EMENI              Reviewed;         638 AA.
AC   Q5B8F4; C8VID7;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=AN3176;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000052; EAA62940.1; -; Genomic_DNA.
DR   EMBL; BN001306; CBF83255.1; -; Genomic_DNA.
DR   RefSeq; XP_660780.1; XM_655688.1.
DR   AlphaFoldDB; Q5B8F4; -.
DR   SMR; Q5B8F4; -.
DR   STRING; 162425.CADANIAP00009893; -.
DR   EnsemblFungi; CBF83255; CBF83255; ANIA_03176.
DR   EnsemblFungi; EAA62940; EAA62940; AN3176.2.
DR   GeneID; 2873958; -.
DR   KEGG; ani:AN3176.2; -.
DR   VEuPathDB; FungiDB:AN3176; -.
DR   eggNOG; KOG0345; Eukaryota.
DR   HOGENOM; CLU_003041_26_4_1; -.
DR   InParanoid; Q5B8F4; -.
DR   OMA; DRAIHDK; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0030686; C:90S preribosome; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
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; IEA:UniProtKB-EC.
DR   GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IEA:EnsemblFungi.
DR   GO; GO:0000470; P:maturation of LSU-rRNA; IEA:EnsemblFungi.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
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; IPR000629; RNA-helicase_DEAD-box_CS.
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; PS00039; DEAD_ATP_HELICASE; 1.
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..638
FT                   /note="ATP-dependent rRNA helicase spb4"
FT                   /id="PRO_0000232328"
FT   DOMAIN          45..249
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          283..437
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          538..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          521..629
FT                   /evidence="ECO:0000255"
FT   MOTIF           14..42
FT                   /note="Q motif"
FT                   /evidence="ECO:0000305"
FT   MOTIF           197..200
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        538..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..628
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         58..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   638 AA;  71063 MW;  2091AF2ED31C856F CRC64;
     MAPKPPSGTS SRAWDAVNPP LSEWVLDAVS SMGFTRMTPV QASAIPLFMA HKDVVVEAVT
     GSGKTLSFLI PVVEKLLRLE EPIKKHHVGA IIVSPTRELA SQIYNVLTSL LAFHPASAAV
     INTSETEDVP RPKHSSSVLR VVPQLLLGGS TSPAEDLSTF LKRSPNLLVA TPGRLLELLS
     SPHVYCPQSS FEMLVLDEAD RLLDLGFKET LQNILRRLPK QRRTGLFSAS VSEAVDQIVR
     VGLRNPVKVV VKVKGASGVD DKRTPASLQM TYLTQPPTGK FPALKHILNS VQPTPSKSIF
     FVSTCSGVDY LSVILPLILG NDFQLIPLHG KHPANVRQKN FNRFVNAHNP AILLTTDVAS
     RGLDIPSVDL VVQIDPPSDP KTFIHRCGRA GRAGRRGLSV VLLHPGREED YVSFLEVRKT
     PVAPFPHPIT VSDAEAAAAT ETARKVVKAD RAIHDRGQKA FVSWLRSYSK HQASSIFRVA
     DLDWEGLGKA WGLLKLPKMP ELKNFKGDKT LGVQMDWDTY AYKDKQREKR RLELLQEMAE
     SGQQQTTNKK RPNETVAWSN NAENRNKKAK RRDMKQVRQE RKRWEKMTEE EKKKALETEQ
     MLEQIRAKNE EQRRLKRAAA KADKDAEEGG DEEFTGFD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024