ID W7JQY5_PLAFA Unreviewed; 922 AA.
AC W7JQY5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=C923_01893 {ECO:0000313|EMBL:EWC77433.1};
OS Plasmodium falciparum UGT5.1.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=1237627 {ECO:0000313|EMBL:EWC77433.1, ECO:0000313|Proteomes:UP000030697};
RN [1] {ECO:0000313|EMBL:EWC77433.1, ECO:0000313|Proteomes:UP000030697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGT5.1 {ECO:0000313|EMBL:EWC77433.1,
RC ECO:0000313|Proteomes:UP000030697};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum UGT5.1.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC {ECO:0000256|RuleBase:RU365068}.
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DR EMBL; KE124496; EWC77433.1; -; Genomic_DNA.
DR AlphaFoldDB; W7JQY5; -.
DR EnsemblProtists; EWC77433; EWC77433; C923_01893.
DR Proteomes; UP000030697; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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; IPR025313; DUF4217.
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 PANTHER; PTHR24031:SF89; ATP-DEPENDENT RNA HELICASE DDX31-RELATED; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00039; DEAD_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, ECO:0000256|RuleBase:RU365068};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW Reference proteome {ECO:0000313|Proteomes:UP000030697};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 223..452
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 616..805
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..142
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 107848 MW; 2D0C436072C23023 CRC64;
MGKFFKENKK SQKVFMHHKM NKHDQKKKRN KQHTDIVMGK KSKGFIKNKK NIGESGNEKK
RNNNFNNIWK KKKRSGNSEK DQVDILGLLK GDSENMNDDD DNNMNDDYNN NNIKGDYNNN
NIKDDDVDDD DYDDDDDDNF DENKNCNDNC SSKHKRNVPS KKEHDILELN NINFNETRKK
MINYKNIFDG KFCDLKYILS ESLINTLEKN EFIKMTSIQK MSIPLFFKPN DIFLKSMTGS
GKTLCYAIPS IEKILNMKEK VKITRDMGIF VLVLSPTREL AIQINNLFCI LTKPYPYIVA
SCITGGEKKK SEKNRLKKGI SILTCTPGRL LDHLENTKSL KLTFLKMVIL DEADKIIYLG
TQDKIKLIYD MIRKIKQEEF SKVHKKKKKE ENEVLDHIND TNMSDMNNIS NDHSNDYEQF
ILDKFQMIFI SATLNHAMKT LANYCLTNNT MWIEKEKKNG INGGNKNDET KQKSNDMISC
MNRENSPLNI HNNDDNDDND ENNGDNNNNN DDNNNNNDDN NNNNDDNNNK NNDDDNNNTY
ELPEQLKQYC ILIDMKQKFI CLIYMLLDCI EKKKKPVVFL SNHHSVEYLQ ILLKNIYWPT
DVNKKNIEVN KKLNEKITPV LEREDEKLLR KHLEQNILNN NYYNNNYNVG NISYKNINLE
EIQNEDELND EPGNLYNINA DKHKRIYLFN NVNIYILHGN LSKEDRLGNF MDFSKTNNSI
LLCTDIISRG IHFDSLSVVI QYDPPQILEE YIHKVGRTAR LNKQGSAYLF LLKSQKQFLN
ILKNKNIQLK IILGNTIINH FKKFCIPNFL KSVGKDILNF LHNHMQTIVK SNNTLMEKGT
SAFLCTITSF YSTSKNLRSI FNAKDIHLGH LAYTFLLEKT PKQISKYKKE QNYINIKKQT
VLSKKEKRLL KSKQFQKKQK RK
//
