DBP7_YEAST
ID DBP7_YEAST Reviewed; 742 AA.
AC P36120; D6VX89;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=ATP-dependent RNA helicase DBP7;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 7;
GN Name=DBP7; OrderedLocusNames=YKR024C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9582098; DOI=10.1017/s1355838298980190;
RA Daugeron M.-C., Linder P.;
RT "Dbp7p, a putative ATP-dependent RNA helicase from Saccharomyces
RT cerevisiae, is required for 60S ribosomal subunit assembly.";
RL RNA 4:566-581(1998).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {ECO:0000269|PubMed:9582098}.
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 -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:9582098}.
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 -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {ECO:0000305}.
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DR EMBL; Z28249; CAA82096.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09179.1; -; Genomic_DNA.
DR PIR; S38093; S38093.
DR RefSeq; NP_012949.1; NM_001179814.1.
DR AlphaFoldDB; P36120; -.
DR SMR; P36120; -.
DR BioGRID; 34156; 469.
DR DIP; DIP-1833N; -.
DR IntAct; P36120; 10.
DR MINT; P36120; -.
DR STRING; 4932.YKR024C; -.
DR iPTMnet; P36120; -.
DR MaxQB; P36120; -.
DR PaxDb; P36120; -.
DR PRIDE; P36120; -.
DR EnsemblFungi; YKR024C_mRNA; YKR024C; YKR024C.
DR GeneID; 853894; -.
DR KEGG; sce:YKR024C; -.
DR SGD; S000001732; DBP7.
DR VEuPathDB; FungiDB:YKR024C; -.
DR eggNOG; KOG0348; Eukaryota.
DR GeneTree; ENSGT00550000075041; -.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; P36120; -.
DR OMA; AVHIKAD; -.
DR BioCyc; YEAST:G3O-32000-MON; -.
DR PRO; PR:P36120; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36120; protein.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..742
FT /note="ATP-dependent RNA helicase DBP7"
FT /id="PRO_0000055037"
FT DOMAIN 178..372
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 405..605
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 45..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 143..172
FT /note="Q motif"
FT MOTIF 307..310
FT /note="DEGD box"
FT COMPBIAS 69..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 742 AA; 83308 MW; A7E25BC16AE09A0B CRC64;
MSDEDSMLLN FTTNEDTAGS SYKQAAKVTG GRWKDRRRMK MKLEGKTVSR KRKANTTGDE
GIIPGRGENS IKKLHKESSY SSEEQEKYKG RNAHNTQGRT LPADSQFVSS LFTSNREITT
AVNTNIHDEN VAINPSNAPL KGDQFASLGV SSLLVSHLEQ KMRIKKPTSI QKQAIPQIIG
NAGKNDFFIH AQTGSGKTLS YLLPIISTIL NMDTHVDRTS GAFALVIAPT RELASQIYHV
CSTLVSCCHY LVPCLLIGGE RKKSEKARLR KGCNFIIGTP GRVLDHLQNT KVIKEQLSQS
LRYIVLDEGD KLMELGFDET ISEIIKIVHD IPINSEKFPK LPHKLVHMLC SATLTDGVNR
LRNVALKDYK LISNGTKKDS DIVTVAPDQL LQRITIVPPK LRLVTLAATL NNITKDFIAS
GQQSKTLRTI VFVSCSDSVE FHYDAFSGSD GHHKNLTGDS VRLLTKGNTM FPCFSDSRDP
DVVIYKLHGS LSQQMRTSTL QHFARDNEAT KGKHLIMFCT DVASRGLDLP HVGSVIELDP
PFAVEDHLHR VGRTARAGEK GESLLFLLPG EEEKYMDYIQ PYHPMGWELL KFDKEILMPA
FKDVNVNRND KFIRKDEKSS KNKDVGDKEY EWDTNATTWH LNIERRVVGD SAFKNLAVKG
FISHVRAYAT HISQEKKFFN VKFLHLGHLA KSFGLRERPK AMGLQSSKDG NSEKKPTKEN
SKNKMFRMAR MAEKQIASEF NY
