ID B9WL64_CANDC Unreviewed; 1050 AA.
AC B9WL64;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN OrderedLocusNames=Cd36_27550 {ECO:0000313|CGD:CAL0000164718};
GN ORFNames=CD36_27550 {ECO:0000313|EMBL:CAX39769.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX39769.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX39769.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(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; FM992695; CAX39769.1; -; Genomic_DNA.
DR RefSeq; XP_002421825.1; XM_002421780.1.
DR AlphaFoldDB; B9WL64; -.
DR GeneID; 8049577; -.
DR KEGG; cdu:CD36_27550; -.
DR CGD; CAL0000164718; Cd36_27550.
DR VEuPathDB; FungiDB:CD36_27550; -.
DR eggNOG; KOG0924; Eukaryota.
DR HOGENOM; CLU_001832_6_3_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000002605; 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 Helicase {ECO:0000313|EMBL:CAX39769.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAX39769.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 345..516
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 538..724
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 68..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 119982 MW; 966AFC7EC421C6B7 CRC64;
MNILDDLDDE LDQLETNIKP KVKLLNQKKE NKLIDDDLDN DLDDEDDLNL PKIKPSTKFK
KMKKEHALRI KNETPSSPLL SQGVSSRISS TPATPSVSEP SIYKQNNEII NDINDINDIN
LDNFSNIEAD REWYNIDEES ALIRDEEIIE DPPPQNHRKR FRNTKHPKRP ATTTTTSSSS
SSLSSSFNET GATFNEFGEY IDYDHQQSLN ELNRIPIISH IFIPPFLENS KQYLQLQISG
SSIRGIGPTV NPIKDPTSEL ASMAKQGSFI VQNRRSKRER ALQAKEAAGI DNSNIGSIID
THNTKKEEEQ PKGKNLNNNE TTTTYQDIQQ QRKLLPAFAV RNDLLTTIRD NQVTIVIGET
GSGKTTQLTQ FLYEDGFGSN IDKNGEKKII ACTQPRRVAA MSVAKRVSEE MNCKLGEEVG
YSIRFEDKTN NKKTIIKYMT EGILLREILV DPLLINYSCI IMDEAHERSL NTDILLGLFK
NLLSKRKDLK LIITSATMNA NRFTKFFGAA PQFHIPGRTF PVEIFFNRDV NMDYVEMAVK
QILTIHLGRW NINATNGNGN DGDILVFMTG QEDIEITCDL IKEKLDLLED PPPLDIYPIY
STMPQDLQKK IFNKMNLQRR KVVVATNIAE TSLTVDGIKY VIDCGLVKVK VYNPKLGMDT
LQMVPISLAN ADQRSGRAGR TGAGIAYRLY TEKATDPNNM YIQPIPEIQR SNLSNIMLLL
KSLKINDINS FPFLDPPPKD LLNCSLHDLW AIGALDNLGQ LTKLGQSMIQ FPIEPTLAKL
ILLSTQSEFH CSEEIITIVA MLSVPNIYNR PKERSNEADM AREKFIISES DHLTLLNIFN
QWEINLNKFK GDYNKINNWC NKNFLQLKSL YRVKDIKYQL KLIMQKNKLT ILKSKNDNDI
RKCLCASFYQ QSAKLIKMNL NGQPEFINLR HSYMKMFLHP TSCLLDSNLS TNYVIYHELI
LTKKEYMNYV TTVDPIWLLE YGYKFFGIAD SYQSNKIGAD LISYKQEFEN QLLKDKKIYE
DIVKQQSKRR SNEISSTNKV SSLFKKRRGI
//
