ID H8WVM6_CANO9 Unreviewed; 1035 AA.
AC H8WVM6;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=CORT_0A01070 {ECO:0000313|EMBL:CCG20499.1};
OS Candida orthopsilosis (strain 90-125) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG20499.1, ECO:0000313|Proteomes:UP000005018};
RN [1] {ECO:0000313|EMBL:CCG20499.1, ECO:0000313|Proteomes:UP000005018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT "Sequence and analysis of the genome of the pathogenic yeast Candida
RT orthopsilosis.";
RL PLoS ONE 7:e35750-e35750(2012).
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; HE681719; CCG20499.1; -; Genomic_DNA.
DR RefSeq; XP_003865940.1; XM_003865892.1.
DR AlphaFoldDB; H8WVM6; -.
DR GeneID; 14536789; -.
DR KEGG; cot:CORT_0A01070; -.
DR eggNOG; KOG0924; Eukaryota.
DR HOGENOM; CLU_001832_6_3_1; -.
DR OrthoDB; 3682876at2759; -.
DR Proteomes; UP000005018; Chromosome 1.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 334..502
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 524..709
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 129..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1035 AA; 118059 MW; FB6E906E4E3A1772 CRC64;
MDDGDITSSI KHKLAVYLNK PENNSLTQTV IIQARGKNFD DFSKFIQIIG LKNDEHAKDI
YDSVQASKPD ATEIMPKKAT IIRRADKSTL KLSFEEDDDE IDDIVSPNIK IRTKEGTPSQ
PRFKRLKKED AERLKEALPP LANERRESPK LEADRVSLRP KIQNDTRPRQ DVKQSWDTRA
VKRDIPKSTS NEGTGGYFNS LGEYIDHDHA PSNDFNRIPI TSHVLIPPFL EKVKEHLTLQ
ITGSSIKGAG PTVDPVKDFT SELASMAKQG SLVVQTKKSK QERAKQAKEK TGVTTSGNRD
DVELDEDTEQ SSDYTIIQKQ RQSLPAYAVK EDVVSAIRDN QVTIIIGETG SGKTTQLAQF
LYEQGLATTK GERKIIGCTQ PRRVAAMSVA KRVSEEMQVE LGEEVGYSVR FDDKTNPEKT
VIKYMTEGIL LREILADNTL SEYSCIIIDE AHERSLNTDI LLGLFKGLLA KRRDLKLVVT
SATMNADRFT RFFGAAPQFT IPGRTFPVDI YFNKNVTMDY VETAVKQILS IHLSKGRDTR
GEFVNDGDIL VFMTGQEDIE ITCDLLREKL EMLENPPPLE ILPIYSTMPQ ELQKRIFNKT
STKKRKVVIA TNIAETSLTV DGIKYVIDCG LVKVKVYNPK LGMDTLQVVP ISFANAEQRS
GRAGRTSAGV AYRLYTERAT DPQNMYQQPI PEIQRTNLSN TMLLLKSLNV HDINSFPFLD
SPPKDLLNCS LYDLWAMGAL DNFGELTKLG RDMIQFPIEP TLSKLILLST ERYFHCSEDI
LTIVAMLSVS NIFQRSKERA KEADSARERF VVAESDHLTL LNVYTQWEAN MNKFSNNWNR
INEWCGRNYI QHKSLYRARE IRKQLAYIMQ KRKLPFCRAK NDDDIRRCLC AAFYHQSAKL
VKMGLNGTPE FVNLRHNYMK MYLHPTSSLL NSNLSSNFVI YHDLILTSKE YMNYVTCVDP
MWLLKFGYVF YSIPESSRDK LVEGLGTNAR VEFEHQLEND RTLYEQQNSK LQKSDQKESS
ITNRKSLLFR KRKRM
//
