ID G8BDM5_CANPC Unreviewed; 800 AA.
AC G8BDM5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN OrderedLocusNames=CPAR2_210170 {ECO:0000313|CGD:CAL0000146601,
GN ECO:0000313|EMBL:CCE43372.1};
OS Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS parapsilosis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE43372.1, ECO:0000313|Proteomes:UP000005221};
RN [1] {ECO:0000313|Proteomes:UP000005221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000313|Proteomes:UP000005221}
RP GENOME REANNOTATION.
RC STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA Berriman M., Butler G.;
RT "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT response of the pathogenic yeast Candida parapsilosis.";
RL BMC Genomics 12:628-628(2011).
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU000492}.
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DR EMBL; HE605206; CCE43372.1; -; Genomic_DNA.
DR AlphaFoldDB; G8BDM5; -.
DR STRING; 578454.G8BDM5; -.
DR EnsemblFungi; CPAR2_210170-T; CPAR2_210170-T-p1; CPAR2_210170.
DR CGD; CAL0000146601; CPAR2_210170.
DR VEuPathDB; FungiDB:CPAR2_210170; -.
DR eggNOG; KOG0347; Eukaryota.
DR Proteomes; UP000005221; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0022613; P:ribonucleoprotein complex biogenesis; IEA:UniProt.
DR CDD; cd17946; DEADc_DDX24; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005221}.
FT DOMAIN 179..207
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 210..408
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 469..625
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 179..207
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 9..26
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 90330 MW; A585BA82A93AFE8B CRC64;
MANNKPSKKQ QKKPGKIFKP RKPPTLKQKL KKESKVVKIN DLAWKPVEIP DNLGDYTGFF
GLEEIDGVDV EVVDGKPQFV IKDDKAEDKK ADKVDEIKTP SHDEQSDDDE VIDEEDFTGF
DNDNQEEEPD VSKTDILATE EPSNANDNDE LSELKHNVFA NLDLPMPDDN DIDLPQWSAN
EIGVSLSPYT LNGLANLNFT KPTPIQKRTI PIAIEGKDVV GKATTGSGKT LAYGIPILEK
YLQSLDLVKQ NVKDQKINRP NGIIFTPTRE LAHQVVDHLN KLAQYSPLSV RGIVSVTGGL
AIQKQQRLLK MGPGIIVATP GRFLELCEND SELMKRMSLT DIIVLDEADR LLQDGHFEEF
EKILELLGKT RPKNKNVDWK WQTLVFSATF SRDLFGKLDK QQKPKAKNQK QQIDGNSLVQ
NDEIIELLNE KLHFKDKKPV LIDANPKEIV SGQITEALVE CGATERDLYL YYFLLMYKGS
TLVFANSIDS VKRLVPLLEN LKIPAFAIHS SMEQKQRLRS LERFKAALEK NETAVLVASD
VAARGLDIPK IDHVAHYHLP RSADVYIHRS GRTARAGREG VSVMFCSPQE ASGPLRKLRK
IVASNASNKK LSTHNDVKLL PIEMDLVGQL RPRVELAGKL ADARISSTAT RKEDSWVKQA
AEDLGVEDLH DLDEFEDDII KKQRKRQEGK KLTKNEQNRY KFELRELLAK PIRKQNRRSY
LTSGLHNLAH QMVTGKHHED VVGHEKVNAL NDLQKNGSKI KPVSNDQKLN KIVKLKEAKQ
TKKDQKKEAK QKRQQLRGGK
//
