ID A7U5W9_PLAFA Unreviewed; 841 AA.
AC A7U5W9;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
OS Plasmodium falciparum (malaria parasite P. falciparum).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833 {ECO:0000313|EMBL:ABU45415.1};
RN [1] {ECO:0000313|EMBL:ABU45415.1}
RP NUCLEOTIDE SEQUENCE.
RA Tuteja R., Shankar J.;
RL Submitted (JUN-2007) 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 helicase domain is involved in the stimulation of RELA
CC transcriptional activity. {ECO:0000256|RuleBase:RU365068}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX1 subfamily.
CC {ECO:0000256|ARBA:ARBA00008765}.
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DR EMBL; EF690550; ABU45415.1; -; Genomic_DNA.
DR AlphaFoldDB; A7U5W9; -.
DR SMR; A7U5W9; -.
DR VEuPathDB; PlasmoDB:PF3D7_0521700; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000140900; -.
DR VEuPathDB; PlasmoDB:Pf7G8_050026900; -.
DR VEuPathDB; PlasmoDB:PfCD01_050028000; -.
DR VEuPathDB; PlasmoDB:PfDd2_050026600; -.
DR VEuPathDB; PlasmoDB:PfGA01_050026100; -.
DR VEuPathDB; PlasmoDB:PfGB4_050027600; -.
DR VEuPathDB; PlasmoDB:PfGN01_050026600; -.
DR VEuPathDB; PlasmoDB:PfHB3_050026700; -.
DR VEuPathDB; PlasmoDB:PfIT_050026900; -.
DR VEuPathDB; PlasmoDB:PfKE01_050026100; -.
DR VEuPathDB; PlasmoDB:PfKH01_050027000; -.
DR VEuPathDB; PlasmoDB:PfKH02_050027200; -.
DR VEuPathDB; PlasmoDB:PfML01_050026600; -.
DR VEuPathDB; PlasmoDB:PfNF135_050027200; -.
DR VEuPathDB; PlasmoDB:PfNF166_050026800; -.
DR VEuPathDB; PlasmoDB:PfNF54_050025900; -.
DR VEuPathDB; PlasmoDB:PfSD01_050026600; -.
DR VEuPathDB; PlasmoDB:PfSN01_050026800; -.
DR VEuPathDB; PlasmoDB:PfTG01_050026800; -.
DR OMA; EYCIRAI; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR003877; SPRY_dom.
DR PANTHER; PTHR24031:SF307; ATP-DEPENDENT RNA HELICASE DDX1; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365068};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365068};
KW RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 2..30
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 64..265
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 336..482
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 579..751
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 2..30
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
SQ SEQUENCE 841 AA; 97338 MW; 78E342F5C7E0F4B3 CRC64;
MSAFEELGLH SDLCAVLEKN GIDLPTAIQQ ESIPLTLGGG DLCACAETGT GKTLSFIFSS
LQIVHELVRN IGNYEDVSIR KNNNNMENNN DSNISNIIDD NDKNKKSSYI KTINKNSKVI
IKDNECICNN NNNNNSNNFL FEEVKVDCEI TNGLYAYEIE ILSKSYVNVG FCPSIKETLK
YNYTYCSNGN KYNNNRQEHY GEYFSNNDII TCLINKNNNT ISFKKNGKFL GNAFKIFYKY
NDVAFFPYIW GKYFHIKLHF ENLKYGDRSL HFNELCILLT SNCNDNDTLS DRKIFFSSEN
IRDEKNFKLE KANMQTHNYQ NNNSIINEYT HNYNQQNFNN KKKLYCIVLC PTRDLAQQTY
NNYLTYSECF NNPSINIGIL VGGEQRNKGH HMNDDGSYNI VVGTCFKLIE CIRKNSIKVN
DIRLLILDEA DELINNDEKT VLEIKDSCMK YGHRVQTLFF SATLQDKNVK DCINKITNKP
IFVDLKYGKN SIPSHIYVCL YYVNDENSNL SYIIKENDNN NHNKEIYNIL YNEKLYHMNT
RELYEYTDKV HILNNSNSNL KKNDKEQISL NIKMNKLKKL VQIINVFNMQ NGIIFCRTNL
DCDNVYNFLN AVGDGKAYKG TVESLKENKY SCVILKGKMS NDERKNNLQA FKKGEVRFLI
CTDVAARGID IQNLRYLIIM TLSDNINTFF HKIGRVGRDG KNSLCIVLSA DNEQEEKVWF
HTCPSRGINC YNRNLKENKG CTVYIKESDY IKTINDMLEV PIHVLDSKYY YAENVVDPLN
YFKKHPVSNK SRRNKNQNAN SIFQESSHID VLSSFASNIN SIKKLQSAIS YKHYELLNFQ
I
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