ID F0VPQ7_NEOCL Unreviewed; 969 AA.
AC F0VPQ7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=BN1204_061290 {ECO:0000313|EMBL:CEL70446.1}, NCLIV_061290
GN {ECO:0000313|EMBL:CBZ55704.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ55704.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|EMBL:CBZ55704.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CBZ55704.1};
RA Aslett M.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBZ55704.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CBZ55704.1};
RA Reid A.J., Sohal A., Harris D., Quail M., Sanders M., Berriman M.,
RA Wastling J.M., Pain A.;
RT "Comparative genomics and transcriptomics of Neospora caninum and
RT Toxoplasma gondii.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000007494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA Wastling J.M.;
RT "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT Neospora caninum: Coccidia differing in host range and transmission
RT strategy.";
RL PLoS Pathog. 8:e1002567-e1002567(2012).
RN [4] {ECO:0000313|EMBL:CEL70446.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CEL70446.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
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. DDX27/DRS1
CC subfamily. {ECO:0000256|ARBA:ARBA00043999}.
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DR EMBL; FR823393; CBZ55704.1; -; Genomic_DNA.
DR EMBL; LN714487; CEL70446.1; -; Genomic_DNA.
DR RefSeq; XP_003885730.1; XM_003885681.1.
DR AlphaFoldDB; F0VPQ7; -.
DR GeneID; 13441135; -.
DR VEuPathDB; ToxoDB:NCLIV_061290; -.
DR eggNOG; KOG0338; Eukaryota.
DR InParanoid; F0VPQ7; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000007494; Chromosome XII.
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:InterPro.
DR CDD; cd17947; DEADc_DDX27; 1.
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; 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 PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF14; DEAD-BOX ATP-DEPENDENT RNA HELICASE 28; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 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.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:CBZ55704.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007494}.
FT DOMAIN 231..259
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 262..449
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 485..651
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 678..718
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 231..259
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 13..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..969
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 108196 MW; F6020E523BFD02D5 CRC64;
MGGRAALRYQ NAGGIRDKRK REERLELNRK KKAKKRQEEY AAARLPDMRT RGDKSAYGRS
VKHPVKKNGR LSDLQSSSDE DDEEADEEVE AEEEEEEKAE EEEEEEEGDE EEEDEEEEEE
GEDDEGEEED EDEEVELSDG CLDESFGEEE SDEAEDSEGD DGQGESGSRR GHARTTDPVD
GNPVAHERNQ GEDLAVASEG EKNKVQKNRE TAAQKRQCAY VKHNALLHTQ TAWGDLPLSR
PLLRAIQDLE YAHPTHIQAA CLRPALEGRD LLANAQTGSG KTAAFLLPTL ERLLHSPGVR
TRKMTPNGPA GGLRGTKALV LLPTRELAMQ CVQMLQCLSK YTPVTHALAC GGMTLKAHEN
ALRQQPDIVV ATPGRILDLL LNSPTVHLEL LEIIVLDEAD RLLELGFREE ILAILRHCHR
ARQTLLFSAT LTPSIASLAS LALNRPLHIS AEAAVGDSTA DREKSGFTVT SLQAATAALK
QVSSTLEQQF VMLQRDEHRA PALLHLCTTA YTKNVIVFFQ TKQLAHQTSL LFKFMGLQYA
ELHGNLTQQM RVEALERFHA GEADFLLASE LASRGLDIAG VEAVINFNVP ADIDRYIHSV
GRTARMGRSG VAVTLYHRDG PERLQVKKLL QALRGGLNQS GEKPGKSRNS KGKGDTAQDG
SSAGAPRVFQ RRIDADKLEA LEKKVKSLQG DISRELKREK LEREVRLAEL HLQKAENLQT
HADEIYSRPM RQWFMTAKEK QRLKDESKAL VGKDAEEREA LEKARGGSAK ERSGQAASED
EAEEDSEAET EDAEDNRSLS GSDEDMHGAD SDEELPDWIT ACSDDGQSVE DEVEEPAPKK
KKAKAVTVKE FKVAKPKAQP TGGHKEKKKQ ERLTPKQRER MKELQFMKAA GRSAKRSQMP
KRLRVTHTSP EDVHSGKARR QKNQKKKHRP CWRAEESKKP QGGRDEKKER KVKSVGKKAF
KSKGRYRRR
//
