DHH1_ASPCL
ID DHH1_ASPCL Reviewed; 503 AA.
AC A1CJ18;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=ATP-dependent RNA helicase dhh1;
DE EC=3.6.4.13;
GN Name=dhh1; ORFNames=ACLA_033450;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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 RNA helicase involved in mRNA turnover, and
CC more specifically in mRNA decapping. Is involved in G1/S DNA-damage
CC checkpoint recovery, probably through the regulation of the
CC translational status of a subset of mRNAs. May also have a role in
CC translation and mRNA nuclear export (By 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; DS027056; EAW09142.1; -; Genomic_DNA.
DR RefSeq; XP_001270568.1; XM_001270567.1.
DR AlphaFoldDB; A1CJ18; -.
DR SMR; A1CJ18; -.
DR STRING; 5057.CADACLAP00003452; -.
DR EnsemblFungi; EAW09142; EAW09142; ACLA_033450.
DR GeneID; 4702815; -.
DR KEGG; act:ACLA_033450; -.
DR VEuPathDB; FungiDB:ACLA_033450; -.
DR eggNOG; KOG0326; Eukaryota.
DR HOGENOM; CLU_003041_30_1_1; -.
DR OMA; VCADEAP; -.
DR OrthoDB; 583315at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0098562; C:cytoplasmic side of membrane; IEA:EnsemblFungi.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IEA:EnsemblFungi.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0045900; P:negative regulation of translational elongation; IEA:EnsemblFungi.
DR GO; GO:0033962; P:P-body assembly; IEA:EnsemblFungi.
DR GO; GO:0045727; P:positive regulation of translation; IEA:EnsemblFungi.
DR GO; GO:0010603; P:regulation of cytoplasmic mRNA processing body assembly; IEA:EnsemblFungi.
DR GO; GO:0034063; P:stress granule assembly; IEA:EnsemblFungi.
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..503
FT /note="ATP-dependent RNA helicase dhh1"
FT /id="PRO_0000282461"
FT DOMAIN 78..248
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 258..418
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 47..75
FT /note="Q motif"
FT MOTIF 196..199
FT /note="DEAD box"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 503 AA; 56731 MW; 76F9009F0CAEA8B3 CRC64;
MADALASQLS NTTLGEANSE TKWKEQLNVP AKDARPQTED VTATKGLEFE DFYIKRELMM
GIFEAGFEKP SPIQEETIPV ALTGRDILAR AKNGTGKTAA FVIPTLERIN PKSTKTQALI
LVPTRELALQ TSQVCKTLGK HLGINVMVTT GGTGLMDDII RLNDAVHILV GTPGRVLDLA
SKGVADLSEC PTFVMDEADK LLSPEFTPVI EQLLSFHPKD RQVMLFSATF PLIVKSFKDK
HMRNPYEINL MDELTLRGIT QYYAFVEEKQ KVHCLNTLFS KLQINQSIIF CNSTNRVELL
AKKITELGYS CFYSHARMLQ QHRNRVFHDF RNGVCRNLVC SDLLTRGIDI QAVNVVINFD
FPKNAETYLH RIGRSGRFGH LGLAINLINW EDRFNLYKIE QELGTEIQPI PQNIDKKLYV
YDSPETIPRP ISNPPQLRQA TQSVTAERRH QNHANSGQYQ FNRGRGSYRG RGQGQRRSVQ
NESNKFNHPQ GQQSGKSQMA PVS
