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Database: UniProt
Entry: Q1E5R1
LinkDB: Q1E5R1
Original site: Q1E5R1 
ID   DHH1_COCIM              Reviewed;         512 AA.
AC   Q1E5R1; J3KL06;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   16-OCT-2019, entry version 73.
DE   RecName: Full=ATP-dependent RNA helicase DHH1;
DE            EC=3.6.4.13;
GN   Name=DHH1; ORFNames=CIMG_02102;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J.,
RA   Wortman J.R., Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E.,
RA   Zeng Q., Hung C.-Y., McMahan C., Muszewska A., Grynberg M.,
RA   Mandel M.A., Kellner E.M., Barker B.M., Galgiani J.N., Orbach M.J.,
RA   Kirkland T.N., Cole G.T., Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens
RT   Coccidioides and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in mRNA turnover,
CC       and more specifically in mRNA decapping. Is involved in G1/S DNA-
CC       damage 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).
CC       {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
CC       decapping and 5' to 3' exonucleotidic decay. {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC       subfamily. {ECO:0000305}.
DR   EMBL; GG704911; EAS36748.3; -; Genomic_DNA.
DR   RefSeq; XP_001248331.1; XM_001248330.2.
DR   SMR; Q1E5R1; -.
DR   EnsemblFungi; EAS36748; EAS36748; CIMG_02102.
DR   GeneID; 4566476; -.
DR   KEGG; cim:CIMG_02102; -.
DR   EuPathDB; FungiDB:CIMG_02102; -.
DR   eggNOG; KOG0326; Eukaryota.
DR   eggNOG; ENOG410XRAZ; LUCA.
DR   InParanoid; Q1E5R1; -.
DR   KO; K12614; -.
DR   OMA; DWNLMSS; -.
DR   OrthoDB; 583315at2759; -.
DR   Proteomes; UP000001261; 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: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   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; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   mRNA processing; mRNA transport; Nucleotide-binding;
KW   Reference proteome; RNA-binding; Translation regulation; Transport.
FT   CHAIN         1    512       ATP-dependent RNA helicase DHH1.
FT                                /FTId=PRO_0000255997.
FT   DOMAIN       78    248       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      258    418       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      91     98       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        47     75       Q motif.
FT   MOTIF       196    199       DEAD box.
SQ   SEQUENCE   512 AA;  57369 MW;  FA5D2DBAF9BE3A0A CRC64;
     MAEALASQLN KAKLGDNGAE TKWKEQLKLP PKDTRTQTED VTATKGLEFE DFYIKRELMM
     GIFEAGFEKP SPIQEETIPV ALTGRDILAR AKNGTGKTAA FVIPTLERTN PKISKTQALI
     LVPTRELALQ TSQVCKTLGK HLGINVMVTT GGTGLQDDII RLSDTVHIIV GTPGRILDLA
     SKGVADLSEC TTFVMDEADK LLSPEFTPVI EQLLSFHPKD RQVMLFSATF PMIVKSFKDK
     HMRNPYEINL MDELTLRGIT QYYAFVEERQ KVHCLNTLFS KLQINQSIIF CNSTNRVELL
     AKKITELGYS CFYSHARMLQ QNRNRVFHDF RNGVCRNLVC SDLLTRGIDI QAVNVVINFD
     FPKNAETYLH RIGRSGRFGH LGLAINLINW DDRYNLYKIE QELGTEIQPI PPSIDKKLYV
     YDTPETIPRP IANASTERNP PAQLAQSSDN QNHRQAHHIS GGHGQQTANR GHSLRGSYRG
     GRAQGHRGGH PENNRTNPMS SRSNMPTSTT AS
//
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