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Database: UniProt
Entry: Q4MZ82_THEPA
LinkDB: Q4MZ82_THEPA
Original site: Q4MZ82_THEPA 
ID   Q4MZ82_THEPA            Unreviewed;       476 AA.
AC   Q4MZ82;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   OrderedLocusNames=TP03_0216 {ECO:0000313|EMBL:EAN30951.1};
OS   Theileria parva (East coast fever infection agent).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5875 {ECO:0000313|EMBL:EAN30951.1, ECO:0000313|Proteomes:UP000001949};
RN   [1] {ECO:0000313|EMBL:EAN30951.1, ECO:0000313|Proteomes:UP000001949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Muguga {ECO:0000313|EMBL:EAN30951.1,
RC   ECO:0000313|Proteomes:UP000001949};
RX   PubMed=15994558; DOI=10.1126/science.1110439;
RA   Gardner M.J., Bishop R., Shah T., de Villiers E.P., Carlton J.M., Hall N.,
RA   Ren Q., Paulsen I.T., Pain A., Berriman M., Wilson R.J.M., Sato S.,
RA   Ralph S.A., Mann D.J., Xiong Z., Shallom S.J., Weidman J., Jiang L.,
RA   Lynn J., Weaver B., Shoaibi A., Domingo A.R., Wasawo D., Crabtree J.,
RA   Wortman J.R., Haas B., Angiuoli S.V., Creasy T.H., Lu C., Suh B.,
RA   Silva J.C., Utterback T.R., Feldblyum T.V., Pertea M., Allen J.,
RA   Nierman W.C., Taracha E.L.N., Salzberg S.L., White O.R., Fitzhugh H.A.,
RA   Morzaria S., Venter J.C., Fraser C.M., Nene V.;
RT   "Genome sequence of Theileria parva, a bovine pathogen that transforms
RT   lymphocytes.";
RL   Science 309:134-137(2005).
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. DDX52/ROK1
CC       subfamily. {ECO:0000256|ARBA:ARBA00024355}.
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:EAN30951.1}.
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DR   EMBL; AAGK01000005; EAN30951.1; -; Genomic_DNA.
DR   RefSeq; XP_763234.1; XM_758141.1.
DR   AlphaFoldDB; Q4MZ82; -.
DR   STRING; 5875.Q4MZ82; -.
DR   EnsemblProtists; EAN30951; EAN30951; TP03_0216.
DR   GeneID; 3500147; -.
DR   KEGG; tpv:TP03_0216; -.
DR   VEuPathDB; PiroplasmaDB:TpMuguga_03g00216; -.
DR   eggNOG; KOG0344; Eukaryota.
DR   InParanoid; Q4MZ82; -.
DR   OMA; DRALMAC; -.
DR   Proteomes; UP000001949; Unassembled WGS sequence.
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; cd00268; DEADc; 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   PANTHER; PTHR24031:SF594; ATP-DEPENDENT RNA HELICASE DDX52-RELATED; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000256|RuleBase:RU365068, ECO:0000313|EMBL:EAN30951.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU365068};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001949};
KW   RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          100..265
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          293..438
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   COILED          317..344
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   476 AA;  53919 MW;  20B22A81305070F6 CRC64;
     MDKIFKKLVR GTNFKNGPSS GIFVFRDGDK ESDSGVFDED FSVVNSSGED FNDYSPLDTF
     SALDSLTTDD KISERAKVIS KSINSKLNFD KTTPIQRYVI PIMMKGNDVV AVAPTGSGKT
     LSYLTPILLK NLEDSLSVII IVPTVELVQQ VKSEFIYLTG GEIFSIKALE KNMTEFNFSI
     AITTPLTLYT LLHNNALKTD LMRGLKCLVL DECDKLLEEG YGENIEYIMN LIKDFKGIQK
     ASFSSTLQSE VLLLSKSHFN NPIHITIGKE NVCCCNVEQE LICVTNDKGK LLILKQLIND
     GKLLPPILVF LQSINRVNDL YNELSQLNLN VQKFTKQLTL KQRQNIIQKF RIGQIWILLC
     TDILCRGINF KGVHSIVNYD LPLTPQVYIN RVGRAGRGTK RGKSVTFFTI NDFKILNHII
     QIMKLSKSNI PQYLLSLKPI HIQQKRKNST NPNQQILNTQ PLTHEFKLWK VDPKNF
//
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