DHH1_CRYNH
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 03-AUG-2022, entry version 81.
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 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC 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-associated
RT 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 human
RT 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., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., 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 var.
RT grubii reveals complex RNA expression and microevolution leading to
RT 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., Zhang N.,
RA Waterman S.R., Blewett N.H., Myers T.G., Maraia R.J., Kehrl J.H., Uzel G.,
RA 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, 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). Blocks autophagy
CC in nutrient-rich conditions by, at least partly, binding and repressing
CC the expression of a set of ATG genes, including ATG3, ATG7, ATG8,
CC ATG19, ATG20 and ATG22 (PubMed:26098573). VAD1-mediated repression of
CC autophagy is regulated by TOR-dependent phosphorylation of the
CC decapping enzyme DCP2 (PubMed:26098573). Regulates multiple virulence-
CC associated genes (PubMed:15765146). Repression of autophagy by VAD1
CC also regulates the pathogenesis (PubMed:26098573). {ECO:0000250,
CC ECO:0000269|PubMed:15765146, 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 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 -!- DISRUPTION PHENOTYPE: Leads to an accumulation of autophagic bodies and
CC increases autophagic flux accompanied by increased accumulation of ATG8
CC mRNA and protein in nutrient-replete conditions (PubMed:26098573).
CC {ECO:0000269|PubMed:26098573}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC subfamily. {ECO:0000305}.
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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 AlphaFoldDB; Q58Z64; -.
DR SMR; Q58Z64; -.
DR SwissPalm; Q58Z64; -.
DR EnsemblFungi; AFR97742; AFR97742; CNAG_01537.
DR GeneID; 23885236; -.
DR VEuPathDB; FungiDB:CNAG_01537; -.
DR HOGENOM; CLU_003041_30_2_1; -.
DR PHI-base; PHI:423; -.
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: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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW mRNA transport; Nucleotide-binding; RNA-binding; Translation regulation;
KW Transport.
FT CHAIN 1..616
FT /note="ATP-dependent RNA helicase VAD1"
FT /id="PRO_0000232189"
FT DOMAIN 67..238
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 248..408
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 36..64
FT /note="Q motif"
FT MOTIF 186..189
FT /note="DEAD box"
FT COMPBIAS 433..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
