DHH1_PICST
ID DHH1_PICST Reviewed; 509 AA.
AC A3LWX3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=ATP-dependent RNA helicase DHH1;
DE EC=3.6.4.13;
GN Name=DHH1; ORFNames=PICST_90571;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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 -!- 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; CP000500; ABN67709.1; -; Genomic_DNA.
DR RefSeq; XP_001385738.1; XM_001385701.1.
DR AlphaFoldDB; A3LWX3; -.
DR SMR; A3LWX3; -.
DR STRING; 4924.XP_001385738.1; -.
DR EnsemblFungi; ABN67709; ABN67709; PICST_90571.
DR GeneID; 4840004; -.
DR KEGG; pic:PICST_90571; -.
DR eggNOG; KOG0326; Eukaryota.
DR HOGENOM; CLU_003041_30_0_1; -.
DR InParanoid; A3LWX3; -.
DR OMA; VCADEAP; -.
DR OrthoDB; 583315at2759; -.
DR Proteomes; UP000002258; Chromosome 6.
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; Reference proteome; RNA-binding;
KW Translation regulation; Transport.
FT CHAIN 1..509
FT /note="ATP-dependent RNA helicase DHH1"
FT /id="PRO_0000285140"
FT DOMAIN 61..231
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 241..401
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 30..58
FT /note="Q motif"
FT MOTIF 179..182
FT /note="DEAD box"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..495
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 74..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 509 AA; 57624 MW; 2999316EF88A4BAD CRC64;
MSEQNWKQNL NLPQRDTRPQ TEDVLNTKGK SFEDFNLKRE LLMGIFEAGF EKPSPIQEES
IPMALAGRDV LARAKNGTGK TASFIIPSLQ QIKPKLNKIQ ALILVPTREL ALQTSQVVRT
LGKHLGIQCM VTTGGTSLKD DILRLNDPVH VLVGTPGRVL DLAARSVADL SECPLFVMDE
ADKMLSREFK GIIEQILEFF PKNRQSLLFS ATFPLAVKSF MDKHLNKPYE INLMDELTLR
GITQYYAFVE EKQKLHCLNT LFSKLQINQS IIFCNSTNRV ELLAKKITEL GYSCYYSHAK
MPQQARNKVF HEFRQGKVRN LVCSDLLTRG IDIQAVNVVI NFDFPKTAET YLHRIGRSGR
FGHLGLAINL MSWNDRYSLY KIEQELGTEI KPIPATIDRK LYVADNEDAI PKPFKIEQLP
KGNEKVHTRA GYEYKGQPEV QSGQQHAQQQ LQPSQQPQQQ LQQPQQPQAA PQGYPPAFNG
YPPYQQYPPQ AGGYPPPQFN GYQAAPGQQ
