ID A0A1D3D126_9EIME Unreviewed; 1115 AA.
AC A0A1D3D126;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=cyc_05761 {ECO:0000313|EMBL:OEH77133.1};
OS Cyclospora cayetanensis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Cyclospora.
OX NCBI_TaxID=88456 {ECO:0000313|EMBL:OEH77133.1, ECO:0000313|Proteomes:UP000095192};
RN [1] {ECO:0000313|EMBL:OEH77133.1, ECO:0000313|Proteomes:UP000095192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHN_HEN01 {ECO:0000313|EMBL:OEH77133.1,
RC ECO:0000313|Proteomes:UP000095192};
RX PubMed=27129308; DOI=10.1186/s12864-016-2632-3;
RA Liu S., Wang L., Zheng H., Xu Z., Roellig D.M., Li N., Frace M.A., Tang K.,
RA Arrowood M.J., Moss D.M., Zhang L., Feng Y., Xiao L.;
RT "Comparative genomics reveals Cyclospora cayetanensis possesses coccidia-
RT like metabolism and invasion components but unique surface antigens.";
RL BMC Genomics 17:316-316(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEH77133.1}.
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DR EMBL; JROU02001199; OEH77133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D3D126; -.
DR VEuPathDB; ToxoDB:cyc_05761; -.
DR VEuPathDB; ToxoDB:LOC34622067; -.
DR InParanoid; A0A1D3D126; -.
DR Proteomes; UP000095192; Unassembled WGS sequence.
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 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000095192}.
FT DOMAIN 303..500
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 539..712
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1115 AA; 122771 MW; 6DE4CF0144F0BC1D CRC64;
MLSFVDEEEA EEAAASPSLL LQPHMQQQPQ RRRAPKRRRR TGWSVVEEEE DSQKLPSGGP
SGGPSGGPSG SGWGPPIDPR VREERVKAIE LAVERDKKKI SGGFKGMTEE EKAETALQRM
WYDRDDSSGL QLGDYEDEDP RNAAREEKLK RLKGGAPRGA PSRSLAEQQR HRDNELWENL
LMHRGGAGGP KEVAFDGEDE EETEKEHVVC RNITPPFLKG FKPSEKPLTV VKDITSDMAM
LARKGSAVLR HTKDAEDRAA VRQRFWEVAG STLGSLLQEF SRTKTKQEQR EALPVFQVRQ
AFLDVCREHR IVVVVGETGS GKTTQLTQYL LEDGYARAPA EAAKAATLTA SVHPSSIAEA
ATAAALAGVS SVGIIGCTQP RRVAAVSVAK RVADEMGVEL GSIVGYSIRF EDCTSAQTAI
KYMTDGVLLR ESLNDADLDK YSCIIMDEAH ERSLNTDILF GVLKGVVARR QDFRLIVTSA
TMDSDRFSAF FGGAVVFNIP GRTFPVEVEF ARCLPDDYVD AAVQKCLTIH CSTPCGGRDP
DGKDTETSEE TGDILVFMTG QDDIEVTCLL LASRLEQLGS RAPPLTILPI YSQLPADLQA
KIFEPSAFRK VIVATNIAET SLTVDGVRYV VDCGFCKLKV FNPSIGMDSL QVTPISQANA
NQRKGRAGRT GPGKCFRLYT ETAFIREMLP NTVPEVQRTN LSNVVLLLKS IGVDDLLDFD
LIDPPPQDTL IDAMHQLWVL GALDNLGALT PIGRKMASFP LDPPLSKMLL TAAELGGARE
IVSIVSLLSV PAVFFVPKEK QDEAESLKEK FFVPESDHLT LLNVYQQWKR AQYNAQWCLK
HFVQPKAMVK AREVREQLMD TMQQQGIPDT SCGTDWDILR KAICAGYFHH AAKLRGIGEY
VNLRTSVPCH VHPTSALYSA GYTPDYVVYH ELLLTTKEYM RNVTAVDARW LADLGPMFFA
LRRMGDGAAN LLAEDQADAA AFEAQMERDL QQQRMQQLSA AKKGQRTFVE ATAGRRKRAT
GLSCVPVPPT SSLSELPSVA ISKGIEETVD AGNDKMEQAH GEKHPQEDIE AEAALHKLKL
LRRATVRQLP KVKSEREAIM QPLDSGGATK SPKDE
//
