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Database: UniProt
Entry: Q8I3P6_PLAF7
LinkDB: Q8I3P6_PLAF7
Original site: Q8I3P6_PLAF7 
ID   Q8I3P6_PLAF7            Unreviewed;       841 AA.
AC   Q8I3P6;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   ORFNames=PF3D7_0521700 {ECO:0000313|EMBL:CAD51581.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CAD51581.1, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA   Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [2] {ECO:0000313|EMBL:CAD51581.1, ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C., Harris B., Harris D.,
RA   Mungall K., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA   Christodoulou Z., Clark L., Clark R., Corto C., Cronin A., Davies R.,
RA   Davies P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA   Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA   Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James D.,
RA   Johnson D., Kerhornou A., Knight A., Kontfortov B., Keyes S., Larke N.,
RA   Lawson D., Lennard N., Line A., Maddison M., McLean J., Mooney P.,
RA   Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rajandream M-A., Rutter S., Rutherford K.M., Sanders M.,
RA   Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA   Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
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; AL844504; CAD51581.1; -; Genomic_DNA.
DR   RefSeq; XP_001351774.1; XM_001351738.1.
DR   AlphaFoldDB; Q8I3P6; -.
DR   SMR; Q8I3P6; -.
DR   STRING; 36329.Q8I3P6; -.
DR   PaxDb; 5833-PFE1085w; -.
DR   EnsemblProtists; CAD51581; CAD51581; PF3D7_0521700.
DR   GeneID; 813032; -.
DR   KEGG; pfa:PF3D7_0521700; -.
DR   VEuPathDB; PlasmoDB:PF3D7_0521700; -.
DR   HOGENOM; CLU_016321_0_0_1; -.
DR   InParanoid; Q8I3P6; -.
DR   OMA; EYCIRAI; -.
DR   OrthoDB; 102545at2759; -.
DR   PhylomeDB; Q8I3P6; -.
DR   Proteomes; UP000001450; Chromosome 5.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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:UniProtKB-EC.
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   Reference proteome {ECO:0000313|Proteomes:UP000001450};
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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