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Database: UniProt
Entry: Q58Z64
LinkDB: Q58Z64
Original site: Q58Z64 
ID   DHH1_CRYNH              Reviewed;         616 AA.
AC   Q58Z64; J9VTF9;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   31-JUL-2019, entry version 70.
DE   RecName: Full=ATP-dependent RNA helicase VAD1 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000305};
DE   AltName: Full=Virulence-associated DEAD box protein 1 {ECO:0000303|PubMed:15765146};
GN   Name=VAD1 {ECO:0000303|PubMed:15765146}; Synonyms=DHH1;
GN   ORFNames=CNAG_01537;
OS   Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC
OS   208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var.
OS   grubii).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=235443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=15765146; DOI=10.1172/JCI200523048;
RA   Panepinto J., Liu L., Ramos J., Zhu X., Valyi-Nagy T., Eksi S., Fu J.,
RA   Jaffe H.A., Wickes B.L., Williamson P.R.;
RT   "The DEAD-box RNA helicase Vad1 regulates multiple virulence-
RT   associated genes in Cryptococcus neoformans.";
RL   J. Clin. Invest. 115:632-641(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RA   Liu L., Panepinto J., Ramos J., Zhu X., Eksi S., Wickes B.L.,
RA   Williamson P.R.;
RT   "Multiple virulence-associated genes are dependent on VAD1 in the
RT   human fungal pathogen, Cryptococcus neoformans.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX   PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA   Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA   Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA   Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y.,
RA   Floyd-Averette A., Gaillardin C., Gerik K.J., Goldberg J.,
RA   Gonzalez-Hilarion S., Gujja S., Hamlin J.L., Hsueh Y.-P., Ianiri G.,
RA   Jones S., Kodira C.D., Kozubowski L., Lam W., Marra M., Mesner L.D.,
RA   Mieczkowski P.A., Moyrand F., Nielsen K., Proux C., Rossignol T.,
RA   Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA   Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA   Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA   Cuomo C.A., Dietrich F.S.;
RT   "Analysis of the genome and transcriptome of Cryptococcus neoformans
RT   var. grubii reveals complex RNA expression and microevolution leading
RT   to virulence attenuation.";
RL   PLoS Genet. 10:E1004261-E1004261(2014).
RN   [4]
RP   FUNCTION, RNA-BINDING, AND DISRUPTION PHENOTYPE.
RX   PubMed=26098573; DOI=10.1038/ncb3189;
RA   Hu G., McQuiston T., Bernard A., Park Y.D., Qiu J., Vural A.,
RA   Zhang N., Waterman S.R., Blewett N.H., Myers T.G., Maraia R.J.,
RA   Kehrl J.H., Uzel G., Klionsky D.J., Williamson P.R.;
RT   "A conserved mechanism of TOR-dependent RCK-mediated mRNA degradation
RT   regulates autophagy.";
RL   Nat. Cell Biol. 17:930-942(2015).
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). Blocks
CC       autophagy in nutrient-rich conditions by, at least partly, binding
CC       and repressing the expression of a set of ATG genes, including
CC       ATG3, ATG7, ATG8, ATG19, ATG20 and ATG22 (PubMed:26098573). VAD1-
CC       mediated repression of autophagy is regulated by TOR-dependent
CC       phosphorylation of the decapping enzyme DCP2 (PubMed:26098573).
CC       Regulates multiple virulence-associated genes (PubMed:15765146).
CC       Repression of autophagy by VAD1 also regulates the pathogenesis
CC       (PubMed:26098573). {ECO:0000250, ECO:0000269|PubMed:15765146,
CC       ECO:0000269|PubMed:26098573}.
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   -!- DISRUPTION PHENOTYPE: Leads to an accumulation of autophagic
CC       bodies and increases autophagic flux accompanied by increased
CC       accumulation of ATG8 mRNA and protein in nutrient-replete
CC       conditions (PubMed:26098573). {ECO:0000269|PubMed:26098573}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC       subfamily. {ECO:0000305}.
DR   EMBL; AY654620; AAV41010.1; -; Genomic_DNA.
DR   EMBL; AY661864; AAV69745.1; -; mRNA.
DR   EMBL; CP003830; AFR97742.1; -; Genomic_DNA.
DR   RefSeq; XP_012052585.1; XM_012197195.1.
DR   SMR; Q58Z64; -.
DR   SwissPalm; Q58Z64; -.
DR   EnsemblFungi; AFR97742; AFR97742; CNAG_01537.
DR   GeneID; 23885236; -.
DR   EuPathDB; FungiDB:CNAG_01537; -.
DR   Proteomes; UP000010091; Chromosome 11.
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   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Helicase; Hydrolase;
KW   mRNA processing; mRNA transport; Nucleotide-binding; RNA-binding;
KW   Translation regulation; Transport.
FT   CHAIN         1    616       ATP-dependent RNA helicase VAD1.
FT                                /FTId=PRO_0000232189.
FT   DOMAIN       67    238       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      248    408       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      80     87       ATP.
FT   MOTIF        36     64       Q motif.
FT   MOTIF       186    189       DEAD box.
FT   COMPBIAS    399    571       Gln/Pro-rich.
SQ   SEQUENCE   616 AA;  67652 MW;  C34A44058AA4A705 CRC64;
     MASSSTLAND DWKQGLAAPP KDLRPQTEDV TATQGSRFED FGLRRELLMG IYTAGFERPS
     PIQEQAIPMA LTGRDILARA KNGTGKTASF IIPTLNRINT SLSHIQALIL VPTRELALQT
     SQVCKTLGAH IPNLQVMITT GGTTLRDDIL RLQQPVHILV GTPGRILDLG SKGIAGLNKC
     GIFVMDEADK LLSEDFMPVI EQTLALCPQE RQVMLFSATF PWTVKEFKDQ HMVQPYEINL
     MDELTLKGVT QYYAYVEESQ KVHCLNTLFS KLQINQSIIF CNSTNRVELL AKKVTELGYS
     CFYSHAKMQQ AHRNRVFHDF RNGMTRNLVC SDLLTRGIDI QAVNVVINFD FPRTAESYLH
     RIGRSGRFGH LGLAISLLTL EDRHNLYRIE SELGTEIAPI PAVIDPVLYV APAMVEEERE
     SPPPKPAAIA APPAQQQPQQ RQRQHPPVPS HQVAHHSPAA APIQQQQQQQ QQQQQPQYQL
     AYGQGPPQPQ VPFQQANSSP APAPLPSYPQ QAPTQAQGPA QMQSPPSEPA TQPQASAQIP
     VQGQTPPIQP RAQQQGQQQP SQPGQAEGQS QPNRRPNTGG FRGNGRGQGH RGRGRGRGGQ
     PGHPGAGASQ SQQAQA
//
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