ID A0A0N5CP73_THECL Unreviewed; 501 AA.
AC A0A0N5CP73;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 08-NOV-2023, entry version 37.
DE RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
GN ORFNames=TCLT_LOCUS2007 {ECO:0000313|EMBL:VDM97738.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000200601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000200601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM97738.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 EMBL; UYYF01000332; VDM97738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N5CP73; -.
DR STRING; 103827.A0A0N5CP73; -.
DR WBParaSite; TCLT_0000200601-mRNA-1; TCLT_0000200601-mRNA-1; TCLT_0000200601.
DR OMA; VIYVEAN; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; Unassembled WGS sequence.
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:SF6; RUVB-LIKE 1; 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 Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW Transcription {ECO:0000256|RuleBase:RU363048};
KW Transcription regulation {ECO:0000256|RuleBase:RU363048}.
FT DOMAIN 76..392
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 469..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 54785 MW; D98CF4D6A245F595 CRC64;
MTIESATISS TKLVRIDEVK STARKQRVAA HSHVKGLGLD SETHVPKNSA CGFIGQLEAR
DAAGVIVDLI RTKRMAGRAV LLAGPPGTGK TAIALAMAQE LGDKMPFCPM VGSEVYSSEV
KKTEVLMENF RRSIGLRVRE KKEVYEGEVT ELTPVENENA IGGYGKTILH VLIGLKTAKG
SKQLKLDPSI YEAILKQKID VGDVIYIEAN SGAVKRLGRC DVYATEFDLE ADEFVPLPKG
DVHKSKEVIQ DVTLHDLDVA NARPHGTAGN VTSLVGQLLK PKKTEITERL RQEVNKVVND
YIEQGIAELM PGVLFIDEVH MLDIECFTYL HRALESTISP IVIFATNRGQ CKVRGTELIS
PHGVPSDLLD RMLIIITKPY KIEEILAIVK VRADAEAVKL DDEALSHLSK LGAETSLRYV
VQLLTPAKLL AQVNHREVVT KEDVQECSEL FIDAKTSAQM LRSVITDSPT HASVTPQTEV
APSCQPQTAA VDEVEMKAET S
//
