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Database: UniProt
Entry: C4YL82_CANAW
LinkDB: C4YL82_CANAW
Original site: C4YL82_CANAW 
ID   C4YL82_CANAW            Unreviewed;      1070 AA.
AC   C4YL82;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=CAWG_01599 {ECO:0000313|EMBL:EEQ43363.1};
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ43363.1, ECO:0000313|Proteomes:UP000001429};
RN   [1] {ECO:0000313|EMBL:EEQ43363.1, ECO:0000313|Proteomes:UP000001429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1 {ECO:0000313|EMBL:EEQ43363.1,
RC   ECO:0000313|Proteomes:UP000001429};
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).
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         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR   EMBL; CM000309; EEQ43363.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4YL82; -.
DR   PaxDb; 5476-C4YL82; -.
DR   VEuPathDB; FungiDB:CAWG_01599; -.
DR   HOGENOM; CLU_001832_6_3_1; -.
DR   OMA; LYDLWAI; -.
DR   Proteomes; UP000001429; Chromosome R.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0022613; P:ribonucleoprotein complex biogenesis; IEA:UniProt.
DR   GO; GO:0006396; P:RNA processing; IEA:UniProt.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          368..539
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          561..745
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          110..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          327..354
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        114..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1070 AA;  122003 MW;  5D233E971951DF96 CRC64;
     MRIFFFVGDV SIFTTITISF LEFNIDNNTF PSPRINNIST MNILDDLDDE LDELETTTKP
     KVKILNKKKE HKPIVDDDLD LDLDDDDFNL PKIKPPTKFK KMKREDALRI KKETPSSLSP
     SSSVPSKPQG VSSNLPFRPA TPPVSEPSTY EEEDLGDINL DNFSNIEADR EWYNIDEESA
     LARDNEIDED LPQRQRKRIR NTRHPKRTPK TSFNESGATF NEFGEYIDYD HQQSLNELNR
     IPITSHVFIP PFLENSKQYL QLQISGSSIR GIGPTVNPVK DPTSELASMA KQGSFVVQNR
     RSKRERALQA KEAAGVENSN IGSIIDAANT TEEIKQEEKN ADVNETKHQD IQQQRKSLPA
     FAVRNDLLTT IRDNQVTIVI GETGSGKTTQ LTQFLYEDGF GANIDKNGEK RIIACTQPRR
     VAAMSVAKRV SEEMNCKLGE EVGYSIRFED KTDNKKTVIK YMTEGILLRE ILADPMLANY
     SCIIMDEAHE RSLNTDILLG LFKNLLAKRK DLKLIVTSAT MNANRFTKFF GAAPQFHIPG
     RTFPVEVFFN RDVNMDYVEM AVKQVLTIHL GRWNADNNNA NDGDILVFMT GQEDIEITCD
     LIKEKLNLLE DPPPLNIFPI YSTMPQDLQK KIFNKTNLQR RKVVVATNIA ETSLTVDGIK
     YVIDCGLVKV KVYNPKLGMD TLQVVPISLA NADQRSGRAG RTGAGIAYRL YTEKATEPDS
     MYVQPIPEIQ RSNLSNIMLL LKSLKVNDIN SFPFLDPPPK DLLNCSLYDL WAIGALDNLG
     ELTKLGHSMT QFPIEPTLAK LILLSTQPEF HCSEEVVTIV AMLSVPNIFN RPKERANEAD
     MAREKFIISE SDHLTLLNVF NQWNINLNKF KGNYTKINNW CDKNFLQLKS LYRAKDIKHQ
     LMLIMKKNKL AILKSKTDDD IRKCLCASFY QQSAKLTKMN LNGQPEFVNL RHSYMKMFLH
     PTSSLLDSNL STNYVIYHEL VLTKKEYMNC VTTVDPIWLL EYGYKFFGVA DSHRNKIDSE
     AILNKQKFEK QLLKDKEIYE DIIKQQSKRR SNEISTSNRV SSLFKKQRGI
//
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