ID A0A0M3HU92_ASCLU Unreviewed; 453 AA.
AC A0A0M3HU92;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 2.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
OS Ascaris lumbricoides (Giant roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0000633501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ALUE_0000633501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (MAY-2016) to UniProtKB.
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=3.6.4.12;
CC Evidence={ECO:0000256|RuleBase:RU363048};
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|ARBA:ARBA00007519,
CC ECO:0000256|RuleBase:RU363048}.
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DR AlphaFoldDB; A0A0M3HU92; -.
DR WBParaSite; ALUE_0000633501-mRNA-1; ALUE_0000633501-mRNA-1; ALUE_0000633501.
DR Proteomes; UP000036681; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.50.360; RuvB-like helicase, domain II; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR027238; RuvB-like.
DR InterPro; IPR041048; RuvB-like_C.
DR InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR InterPro; IPR010339; TIP49_P-loop.
DR PANTHER; PTHR11093:SF2; RUVB-LIKE 2; 1.
DR PANTHER; PTHR11093; RUVB-RELATED REPTIN AND PONTIN; 1.
DR Pfam; PF06068; TIP49; 1.
DR Pfam; PF17856; TIP49_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363048};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363048};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363048};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363048};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU363048};
KW Transcription {ECO:0000256|RuleBase:RU363048};
KW Transcription regulation {ECO:0000256|RuleBase:RU363048}.
FT DOMAIN 65..361
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 453 AA; 50105 MW; F6BD03EA05D7C101 CRC64;
MTTIDGVEVR DVLKMERIGA HSHIRGLGLD EHLHAARIAE GMVGQMEARR AAGLIVKMIK
DGKIAGRAVL FAGEPGTGKT AIAMGMARTL GDDAPFVSMS ASEIFSVDMS KTEALMQAIR
KAIGVRIKEE NEVPLIVLEG EVVTIEIDRP AAGGGAKVGR LTMKTTDMET VYDLGTKMIE
TCIKQKIAAG DVVQIDKASG RITKIGRSFS RSHDYDAMGP QTKFVKCPEG EIQKRKETVH
TVALHEIDVI NSRSQGFLAL FSGDTGEIKN EVREQINKKV VEWREENKAD VVPGVLFIDE
AHMLDLECFS FLNRAIEADL SPILVMATNR GHEVIRGTQL NSPHGIPIDL LDRSLIVRTR
PYSEKDIEDI LRIRATEESV NLEADAIAIL TKLAGQTSLR YAMQLISTGN VLRERRRGDQ
VSPADLKRAY TLFIDQKRSE KFLTDYQKHF ISE
//
