ID B6AIH2_CRYMR Unreviewed; 863 AA.
AC B6AIH2;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN ORFNames=CMU_031540 {ECO:0000313|EMBL:EEA08013.1};
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:EEA08013.1, ECO:0000313|Proteomes:UP000001460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN66 {ECO:0000313|EMBL:EEA08013.1,
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.
CC {ECO:0000256|RuleBase:RU365068}.
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DR EMBL; DS989736; EEA08013.1; -; Genomic_DNA.
DR RefSeq; XP_002142362.1; XM_002142326.1.
DR AlphaFoldDB; B6AIH2; -.
DR STRING; 441375.B6AIH2; -.
DR EnsemblProtists; EEA08013; EEA08013; CMU_031540.
DR GeneID; 6997496; -.
DR VEuPathDB; CryptoDB:CMU_031540; -.
DR eggNOG; KOG0348; Eukaryota.
DR OMA; VFLSNCH; -.
DR OrthoDB; 179108at2759; -.
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; 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; 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:UP000001460};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365068}.
FT DOMAIN 64..293
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 492..640
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 442..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 99117 MW; 50B11196707E0A10 CRC64;
MSKKEIPNII EFKDEVDDIE DIDGDNESIY TDNFNSYKDL DSRLLNQLEN LGFVKMTRTQ
KIVIPKVLTE KDILIRAPTG TGKTLSFLVP AIQLSLLKDN SNSIKRSNGT YILIITPTRE
LCIQTMRTAQ KLMQKMPWCV VGSICGGEKR KSEKARLRKG ITILGGTPGR LLDHIDSTSC
FNTANLKTLI LDEADRLLEE GFGSTFKRIY LHIMNNNSSL SEYQQLNTKK SKIDNEIEDY
SSMLLNIKHD KLKEFNNNEA NKKISRQVIL ISATLSKPVE DLARYCLKND PQWVILDQYK
EIKYENQLNE YPSDSSQSNK TFNSNVKGIF SVPINLSQEC VIIQDKYRIP ALISLLLSRT
IKKQRIVVFV SSTQVVEYYY AILQSIRWPS DILIKGGPKI KKFIQILENS KIENQNNGVN
CKSKFENLKY AVNKGRPFNK KRWRKNDTNI SDDSSDDSNE SYNDSLKYTS SLDDNLDLTS
KSRNKWLTTN TRLKELYESM FESYIFHNSI HDDEFNDEKI ILDRDNCASI YMLHGHMAKE
DRIGQLKSFE NNKKSSILIT SDVASRGLNF PKIDLVIQFD PPQSIEEYVH RIGRTARMGE
KGTGIIFLRP SEKEYIDILK TYGILSDNED IIMLSNTTIW EGFIVSNRNS GKIDDIPGFY
YSIINKILTL DPYDTHCELL NKARRAYMAF IRSYCSYDNE LSKVFCIKKL HLGHVASSFG
INEHPNKIIS HIKLLDGVSI SWNNKSKLML VKSKEKRNGI QLNSEISDDS TYKKKVVSLE
DVSNVKLSDK DRINKPKINR SNLEEKYNKK IKKKSTRDST LKGTNKVGTE RDPRVNPDNL
VAIDKVLSIM RSRNEIYNLN VNT
//
