ID A0A1A8W1E0_PLAMA Unreviewed; 1199 AA.
AC A0A1A8W1E0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN Name=PRP16 {ECO:0000313|EMBL:SCO92968.1};
GN ORFNames=PMALA_017030 {ECO:0000313|EMBL:SBS86704.1}, PMUG01_11021900
GN {ECO:0000313|EMBL:SCO92968.1};
OS Plasmodium malariae.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5858 {ECO:0000313|EMBL:SBS86704.1, ECO:0000313|Proteomes:UP000078597};
RN [1] {ECO:0000313|Proteomes:UP000078597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Naeem Raeece;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SBS86704.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SCO92968.1, ECO:0000313|Proteomes:UP000219813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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; FLQW01000912; SBS86704.1; -; Genomic_DNA.
DR EMBL; LT594632; SCO92968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8W1E0; -.
DR VEuPathDB; PlasmoDB:PmUG01_11021900; -.
DR OMA; VDVMFHR; -.
DR OrthoDB; 5488182at2759; -.
DR Proteomes; UP000078597; Unassembled WGS sequence.
DR Proteomes; UP000219813; Chromosome 11.
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 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:SBS86704.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SCO92968.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000219813}.
FT DOMAIN 497..660
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 744..946
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 138456 MW; 11BC4C75CE20F2C7 CRC64;
MIAKTSFNNT SSSDEEKKTE NKIIESSNKN ITFKRRKINR INKNNATNNS QKNVFKNVDI
LEKGNIIFKK NKYMKSDNWK KGIRKEVRNS KGVYKNERFA SSKLRISKLD EFSSEALEGN
DDDRSSYEEI NLTKKKESRH NNSNCNSDIN SNNSSNDNSY YSSSQEKGSN QFESNCISSR
YETYNKSDRR KSSYQKKHDN NKKGKEYYSN NNDRILDEIW YTKEDEFIDS FYNIDKDITY
EKEKKMINNF KTRLNSEGKK VNQKNLDNNL WELNKLKQGG VNSTYNKLQL DRINEANNTN
EVKKFVLTRH VTPSFIDKLK SSNEEWAAEV GEGTATAAVI KEVETGGNVS KNVVNECNNG
SYDRKSNSTS YSIVVKDETC DFVKAAKKGS EFLKYFKNEN EKSKARDRYW EIERSKLGEL
LKLYKNNLND STKDGSNTNL DIEEEENSEV FDYKKDKMYG TIFNMESKKK KSTLQDKEDL
LRLKESLPIY KSKKELLDAV YNNNIIIIVG ETGSGKTTQI VQYLYEEGYH KNGIICCTQP
RRVAAVSVAY RVSYEMNVEI GSLVGYTIRF EDNTTKDTKI RYVTDGILLR ETLTDKELDK
YSVIIMDEAH ERSINTDVLL GILKNICLKR NDLKLLVTSA TIDSKKFSQF FGNAPIYNIH
GRTFKVHLEY LRTPCNDYIE CAVQKAIEIH ISDNNYDNNF GDILIFMTGQ EDINATCYLL
SERFYEVYES YKEAKSNKKV TINKIRNIIN RKKSSSEMAQ KGGDHKVVVE YSGEHDNEDR
NADRGEDRSA NSGKDSVEER GNDYYNKGIN DGMHHIYPFY VFPIYSQLSS EQQSKIFQKY
DLRKIIVSTN IAETSLTLDG IKYVIDTGYC KLKVYNQKIG MDVLQVTPIS QANANQRSGR
AGRTGAGICY RLYTENTFLC DLYPNNIPEI QRSNLSNVVL LLKSLNVQNI FEFDFIDTPS
KESIINSLHE LWVLGAINNE GNLTDIGKKM ILFPLDPPLS KIVIYSEKFA CTKETLIIVS
MLSSPAIFLE AKESNEAIES KKEKFTVPES DHLTLLNIYL QWRAHNYSYS WCTNNFIQYK
SLNKAKEVYS QLSDIIKTVN IKNVSCNNKW ECVRKTICSG YFHNAAKLKS FSEYINLRTN
VSCHVHPNCS LYNIGYTPDY VIYQEIVFTT KEFMRNVTTV EPEWLCELGP LFFYMKNLY
//
