ID B6AAL0_CRYMR Unreviewed; 776 AA.
AC B6AAL0;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=CMU_043250 {ECO:0000313|EMBL:EEA05251.1};
OS Cryptosporidium muris (strain RN66).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=441375 {ECO:0000313|Proteomes:UP000001460};
RN [1] {ECO:0000313|EMBL:EEA05251.1, ECO:0000313|Proteomes:UP000001460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN66 {ECO:0000313|EMBL:EEA05251.1,
RC ECO:0000313|Proteomes:UP000001460};
RA Lorenzi H., Inman J., Miller J., Schobel S., Amedeo P., Caler E.V.,
RA da Silva J.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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. DDX55/SPB4
CC subfamily. {ECO:0000256|ARBA:ARBA00038002}.
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DR EMBL; DS989726; EEA05251.1; -; Genomic_DNA.
DR RefSeq; XP_002139600.1; XM_002139564.1.
DR AlphaFoldDB; B6AAL0; -.
DR STRING; 441375.B6AAL0; -.
DR EnsemblProtists; EEA05251; EEA05251; CMU_043250.
DR GeneID; 6994578; -.
DR VEuPathDB; CryptoDB:CMU_043250; -.
DR eggNOG; KOG0345; Eukaryota.
DR OMA; CIQINDE; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000001460; Unassembled WGS sequence.
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; cd17960; DEADc_DDX55; 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; 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:SF2; ATP-DEPENDENT RNA HELICASE DDX55; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001460};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 56..263
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 308..492
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 684..718
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 776 AA; 89433 MW; E7A78A9750E8C571 CRC64;
MEKRNSNNKN KDNTKCIRKP KSFRDLNKPA LSIGTLDFIE NGLKFKYMAP IQEVSIPEIL
TNKDVAVEAC TGSGKTLCYL IPVVEILLRS SITNLSIQFI VGSIIVAPTR ELALQINEIL
DHFLSFIEKY EGNKLKNMLC IGGKDISATM KYIDTVNNIE VDNKDVYRTN NSQLVYHILV
GTPGRLFHMF NILNDGKDWC IKSSLEIFIL DEADRLLDLG FEKHINVILR ALPKQRRTGL
FSATLTSQVC NLIKTGLRNP KFIKVSMGLS DFNGNDDNKK KNEYIQHSRD VNIPSGLGCH
YVELSMTEKN EFLLWFINEY LFPNKCLGKN KGTKSIIFFL TCSSVEFYYK YLSSIYHEHD
NKEKIAEFNT LGNSTYITNT KIGVLCKLHG QMYQKSRETS YNNFKKSNCG ILLATDVAAR
GIDIPDIEWI IQFDAPQDPS FYIHRIGRTA RAGKSGKSII LLQKHEDSFI PYIEKQTCQA
LTKFNFELNK LDESYKSNIV SLCKCIQIND EILSKDEFLR NYEGLNLYRA QTLMRKLVIS
DPATYILAKK AFVAFVRAYK EHQLKFIFPF NILSLGNLAS SFSLLRIPRV KEILGKSCIK
DDFITYSENI HPNDILKGNH YSNEDLEDKK QIKLKDNTKD INSSNNNFKS KTALNIENKV
RTRTEKRNAK RRMEMNEWED LQYEEKLTKK LRQGKITLEN YNKQLKSYRK SNMNNEDSYT
DDDLGYSSNS CNELSDEEII YSNNGKSNLN IKVYPNVLTK KIPKWVYSKS KSKKKR
//
