DHH1_YEAS7
ID DHH1_YEAS7 Reviewed; 506 AA.
AC A6ZXG9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=ATP-dependent RNA helicase DHH1;
DE EC=3.6.4.13;
DE AltName: Full=DExD/H-box helicase 1;
GN Name=DHH1; ORFNames=SCY_0757;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover, and
CC more specifically in mRNA decapping by activating the decapping enzyme
CC DCP1. Is involved in G1/S DNA-damage checkpoint recovery, probably
CC through the regulation of the translational status of a subset of
CC mRNAs. May also have a role in translation and mRNA nuclear export (By
CC similarity). {ECO:0000250}.
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 -!- SUBUNIT: Associated with the CCR4-NOT complex and possibly other big
CC complexes. Interacts with CDC39/NOT1 and POP2, components of the CCR4-
CC NOT complex, with the mRNA decapping proteins DCP1, LSM1, PAT1, and
CC with KEM1, the major 5'-3' exonuclease (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250}. Note=Is
CC concentrated in several cytoplasmic foci called P bodies (or
CC cytoplasmic processing bodies) which represent sites of mRNA decapping
CC and 5' to 3' exonucleotidic decay. {ECO:0000250}.
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. DDX6/DHH1
CC subfamily. {ECO:0000305}.
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DR EMBL; AAFW02000145; EDN60199.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZXG9; -.
DR SMR; A6ZXG9; -.
DR IntAct; A6ZXG9; 2.
DR MINT; A6ZXG9; -.
DR PRIDE; A6ZXG9; -.
DR EnsemblFungi; EDN60199; EDN60199; SCY_0757.
DR HOGENOM; CLU_003041_30_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
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; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW mRNA transport; Nucleotide-binding; RNA-binding; Translation regulation;
KW Transport.
FT CHAIN 1..506
FT /note="ATP-dependent RNA helicase DHH1"
FT /id="PRO_0000310198"
FT DOMAIN 77..247
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 257..417
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 46..74
FT /note="Q motif"
FT MOTIF 195..198
FT /note="DEAD box"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 506 AA; 57544 MW; 062CFA56DF6F2CEE CRC64;
MGSINNNFNT NNNSNTDLDR DWKTALNIPK KDTRPQTDDV LNTKGNTFED FYLKRELLMG
IFEAGFEKPS PIQEEAIPVA ITGRDILARA KNGTGKTAAF VIPTLEKVKP KLNKIQALIM
VPTRELALQT SQVVRTLGKH CGISCMVTTG GTNLRDDILR LNETVHILVG TPGRVLDLAS
RKVADLSDCS LFIMDEADKM LSRDFKTIIE QILSFLPPTH QSLLFSATFP LTVKEFMVKH
LHKPYEINLM EELTLKGITQ YYAFVEERQK LHCLNTLFSK LQINQAIIFC NSTNRVELLA
KKITDLGYSC YYSHARMKQQ ERNKVFHEFR QGKVRTLVCS DLLTRGIDIQ AVNVVINFDF
PKTAETYLHR IGRSGRFGHL GLAINLINWN DRFNLYKIEQ ELGTEIAAIP ATIDKSLYVA
ENDETVPVPF PIEQQSYHQQ AIPQQQLPSQ QQFAIPPQQH HPQFMVPPSH QQQQAYPPPQ
MPSQQGYPPQ QEHFMAMPPG QSQPQY
