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RRP3_NEOFI
ID   RRP3_NEOFI              Reviewed;         472 AA.
AC   A1D405;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=ATP-dependent rRNA helicase rrp3 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:P38712};
GN   Name=rrp3 {ECO:0000250|UniProtKB:P38712}; ORFNames=NFIA_018490;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: ATP-dependent rRNA helicase required for pre-ribosomal RNA
CC       processing. Involved in the maturation of the 35S-pre-rRNA and to its
CC       cleavage to mature 18S rRNA. {ECO:0000250|UniProtKB:P38712}.
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:P38712};
CC   -!- SUBUNIT: Interacts with the SSU processome.
CC       {ECO:0000250|UniProtKB:P38712}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DS027688; EAW23148.1; -; Genomic_DNA.
DR   RefSeq; XP_001265045.1; XM_001265044.1.
DR   AlphaFoldDB; A1D405; -.
DR   SMR; A1D405; -.
DR   STRING; 36630.CADNFIAP00001764; -.
DR   EnsemblFungi; EAW23148; EAW23148; NFIA_018490.
DR   GeneID; 4591870; -.
DR   KEGG; nfi:NFIA_018490; -.
DR   VEuPathDB; FungiDB:NFIA_018490; -.
DR   eggNOG; KOG0330; Eukaryota.
DR   HOGENOM; CLU_003041_1_1_1; -.
DR   OMA; YDIELYQ; -.
DR   OrthoDB; 744428at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0032040; C:small-subunit processome; 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:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   CDD; cd17954; DEADc_DDX47; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR044765; DDX47/Rrp3_DEADc.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..472
FT                   /note="ATP-dependent rRNA helicase rrp3"
FT                   /id="PRO_0000282697"
FT   DOMAIN          83..254
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          282..426
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           52..80
FT                   /note="Q motif"
FT                   /evidence="ECO:0000305"
FT   MOTIF           202..205
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         96..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   472 AA;  52138 MW;  811F0CAF987397AF CRC64;
     MPDVKKRKIA HEAPEHGSDA ESTSSHESVA QQDDTAETQD EAAATETRPA PKSFKDLGII
     DQLCEACETM GYKAPTPIQA ESIPLALQGR DLIGLAETGS GKTAAFALPI LQALMEKPQS
     FFGLILAPTR ELAFQISKSF ESLGSTINVR CAVIVGGMDM VSQSIALGKK PHIIVATPGR
     LLDHLENTKG FSLRTLKYLV MDEADRLLDM DFGPLLDKIL KVLPRERRTF LFSATMSSKV
     ESLQRASLSN PLRVSVSSNK YQTVSTLLQS YLFLPHKHKD IYLVYLLNEF VGQSAIIFTR
     TVHETQRISF LLRSLGFGAI PLHGQLSQSA RLGALGKFRS RSRDILVATD VAARGLDIPS
     VDVVLNFDLP TDSKTYVHRV GRTARAGKSG VAISFVTQYD VEIWLRIEGA LGKKLKEYEL
     EKDEVMVLAE RVGEAQRQAI VEMKNFDEKR GTKAKKFGKG KRSRDEMDQE EG
 
 
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