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Database: UniProt
Entry: G8B5C5_CANPC
LinkDB: G8B5C5_CANPC
Original site: G8B5C5_CANPC 
ID   G8B5C5_CANPC            Unreviewed;       573 AA.
AC   G8B5C5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   OrderedLocusNames=CPAR2_602350 {ECO:0000313|CGD:CAL0000150609,
GN   ECO:0000313|EMBL:CCE39817.1};
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:CCE39817.1, 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).
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DR   EMBL; HE605202; CCE39817.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8B5C5; -.
DR   STRING; 578454.G8B5C5; -.
DR   EnsemblFungi; CPAR2_602350-T; CPAR2_602350-T-p1; CPAR2_602350.
DR   CGD; CAL0000150609; CPAR2_602350.
DR   VEuPathDB; FungiDB:CPAR2_602350; -.
DR   eggNOG; KOG0346; Eukaryota.
DR   Proteomes; UP000005221; Chromosome 6.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0033677; F:DNA/RNA helicase activity; IEA:EnsemblFungi.
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:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   CDD; cd17961; DEADc_DDX56; 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; 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; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005221}.
FT   DOMAIN          16..44
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          48..229
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          258..454
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          332..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           16..44
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        550..573
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  65030 MW;  0FC7D837E04966D7 CRC64;
     MSTTTAASST YVDEDTTWKS LNLDPRLLQA IDKLGFENPT LIQSSAIPLA LEEKRDIIAK
     ASTGSGKTAA YALPIIQNLL LDNLGPGIKS VVLVPTRELS NQVFQFMEQL IKHSNKKIGI
     LNLSSSYSDQ VLNSLLANKP EIIISTPNKL IQVLEMNDEK KSPIDLSSVR NLTIDEVDLI
     LSFGYLEDLA KLESYLPVKK NLQTFLMSAT INDDINELKT KFCTRPAILK LDDEQSNNDK
     LVQFYAKTTE FDKFLLSYVI FKLNLIKGKT IVFVNNIDRG YRLKLFLEQF GIRCCILNSE
     LPINSRLHIV EEFNKNVYHL LIATDEISVE KDEGENDNED GKSSQKVVDN PKAKKSKKDK
     EYGVSRGVDF KNVACVLNFD LPTTSKAYVH RIGRTARAGK SGMALSFVVA SKEVGKHKTA
     TLSTAKRDEK ILSRIVKQQE KNGFEIKPYQ FDMKQVEGFR YRADDAFRAV TQTAIREARV
     KELKNELINS EKLKRFFQEN PQNLASLRHD KELHPARVQA HLKNLPEYLL PESARSDVKN
     IGFVPFHNKN KVNKYRKKGK PKRKQDPLKS FKK
//
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