GenomeNet

Database: UniProt
Entry: F0VAK2_NEOCL
LinkDB: F0VAK2_NEOCL
Original site: F0VAK2_NEOCL 
ID   F0VAK2_NEOCL            Unreviewed;      1014 AA.
AC   F0VAK2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   ORFNames=NCLIV_011580 {ECO:0000313|EMBL:CBZ50691.1};
OS   Neospora caninum (strain Liverpool).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX   NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ50691.1, ECO:0000313|Proteomes:UP000007494};
RN   [1] {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).
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 Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6
CC       subfamily. {ECO:0000256|ARBA:ARBA00038200}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FR823384; CBZ50691.1; -; Genomic_DNA.
DR   RefSeq; XP_003880724.1; XM_003880675.1.
DR   AlphaFoldDB; F0VAK2; -.
DR   GeneID; 13441720; -.
DR   VEuPathDB; ToxoDB:NCLIV_011580; -.
DR   eggNOG; KOG0338; Eukaryota.
DR   eggNOG; KOG0350; Eukaryota.
DR   InParanoid; F0VAK2; -.
DR   OrthoDB; 214799at2759; -.
DR   Proteomes; UP000007494; Chromosome IV.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR24031:SF68; ATP-DEPENDENT RNA HELICASE DDX51; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365068};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU365068};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU365068};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007494};
KW   RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          332..699
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          856..1014
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          751..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          910..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..68
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..766
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        773..852
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1014 AA;  111117 MW;  B11834B5E41DC9D5 CRC64;
     MASEIAPADR GGEEENAQTG KRKKTRDSEY RKLRQEARRL AREGGEKAVE GGACKSKHER
     EKTHGTERAA ASGTKGDHVG EARTEKRDDE ANGAREGEER KRKRERGREA EKEGEKREEP
     VEGDDGDAGT RLGRKRKRRR RRKNLTEDED TLAHEENGDE AEDEKADRER QEALPNEEGK
     RHRKRHMKRK GTRNTEEQSR DEEGQDGEDA NGDSEETDAA QKDSKETPDS QDPSSPSSAS
     SSSASSSASS SSSSSSSSPS CAGKERTPRP EFTSRYCVVT QHSAGEEEDE KQAQSLRALH
     PCVVDALRRR NIQSLFPVQR TVVHFLTRCI DRPYDAQNCD LCVSAPTGEG KTFCYVLPIV
     SFLLGSVVRT TRCVVLVPTR ELAMQVAEEF RRFRHFHPSP FVSRPGSCRT SSSSVRHADA
     EENERSDAAD EHAGKRGRKK PESDTGLDGV NTTPLDSTGI CDSKTTLGNQ VVFCRDISVV
     CLVGELPVHR NKRGNGSAGG SNSSGTRFAS PLNSDFLASF LGSSHAPEAT SGVSIAGSAS
     PDSAAPPDVV VCTPGKFSEM VWNATRRNGG AFSFDAVRGE DGLSLQDEDA LQAGDMRLSL
     DDVQWLVIDE ADRLVRQPHH DWMKAVEALQ RLRFEACRTR GRSFASRSPG KVAIPCVSAF
     ASPFVASASL PLQKLTFSAT MTKNPKSLAL LNLTRPFFVL STPSGHYSMP QSLAQRYVVC
     DSEDKPLCLL LLLLRLARHL ANGGSELGRN RAAVQAASND SNASGDEAKG QEAGGSEDEE
     EEKEEKAEEE NAEEEKAEEE NAEEENAEEE NEEEEKAEEG EEKEESDDGE EGGEEAEGGE
     SREGEGECGE EPEEGGVSEK RKKMKVLVFC SSRDATHRLA RLLQLYFEHA DSSQIRPTSI
     SRFAAFSSSE GQSVPAPSRP DAANGAWRPG DACKEEEEEV ERPLCLRVRE LSSNLSQRDR
     MKLINGFKNG TVEVLVCSDL ASRGLDVEGV DAVFHYDAPQ HVQAYVHRSG RSAR
//
DBGET integrated database retrieval system