ID J4CCF8_THEOR Unreviewed; 650 AA.
AC J4CCF8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 03-MAY-2023, entry version 48.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=TOT_010000776 {ECO:0000313|EMBL:BAM39317.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM39317.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM39317.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM39317.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(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.
CC {ECO:0000256|RuleBase:RU000492}.
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DR EMBL; AP011946; BAM39317.1; -; Genomic_DNA.
DR RefSeq; XP_009689618.1; XM_009691323.1.
DR AlphaFoldDB; J4CCF8; -.
DR STRING; 869250.J4CCF8; -.
DR EnsemblProtists; BAM39317; BAM39317; TOT_010000776.
DR GeneID; 20713654; -.
DR KEGG; tot:TOT_010000776; -.
DR VEuPathDB; PiroplasmaDB:TOT_010000776; -.
DR eggNOG; KOG0348; Eukaryota.
DR OrthoDB; 179108at2759; -.
DR Proteomes; UP000003786; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase 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; IPR025313; DUF4217.
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:SF89; ATP-DEPENDENT RNA HELICASE DDX31-RELATED; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 103..291
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 321..517
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 598..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 73953 MW; BA55E68E7E74F3E8 CRC64;
MYLNRGRSSR FKLLKLVTLS HNLKRVNKCF IKHTHELETS FDPDDVEPVH NESYSPSDEI
TLEDSSTFVS NFSEFSGLLN SRLLKSLESN GFVKLTPIQK LSIPKVLKGS TVLIRSASGT
GKTLTFVIPA LQKLVSPPDN VKITRKDGTK VLIITPTREL SFQISKVTES LSKPFPWIVV
SCIKGISRKS EKARIRKGIT IVIGTPGRIL DHMESTSSFN LTNMDMLVLD EADRLLDMGF
ENKIRNIHSH LLDSKKSNAE NAGIQIVLTS ATITDRVTKL VDTCFVAKPL LIGVNEENHK
MPTKLNLEYA LVDCNNKFMC LVSMLLKFVG NHEKILIFVS NCDTVNYMER LLKMLSWPSL
KRKEGPQGSL MKNTNLNLSE LEKDRVLANK FAVNKDTERQ IFEVPIYKLH GDMESKERMP
LMDQFINSKS SIMVSTDVAS RGLNLSKVNR VVQYDPPQQL DEFIHRSGRT ARIGDSGTCL
LILMKHESEF VQVLNRKGMK LKEIGEGEVW NPIKNIHTPK YLKNFKGDLV GFMRNRFCTD
VKEDSQLLQL AKNAFKSSIR SYKTYAKELR KAFNFRRLHL GHYATSFCLN MKPTELMSRK
DQTSTEARKK RAPKMHSDRR AREPKLNLSA ESQSAAEMAL KYLKEKNMIL
//
