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Database: UniProt
Entry: J8ZYV3_EDHAE
LinkDB: J8ZYV3_EDHAE
Original site: J8ZYV3_EDHAE 
ID   J8ZYV3_EDHAE            Unreviewed;       417 AA.
AC   J8ZYV3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
GN   ORFNames=EDEG_00951 {ECO:0000313|EMBL:EJW04858.1};
OS   Edhazardia aedis (strain USNM 41457) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Edhazardia.
OX   NCBI_TaxID=1003232 {ECO:0000313|EMBL:EJW04858.1, ECO:0000313|Proteomes:UP000003163};
RN   [1] {ECO:0000313|EMBL:EJW04858.1, ECO:0000313|Proteomes:UP000003163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USNM 41457 {ECO:0000313|EMBL:EJW04858.1,
RC   ECO:0000313|Proteomes:UP000003163};
RA   Liu Z.J., Shi F.L., Lu J.Q., Li M., Wang Z.L.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000003163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USNM 41457 {ECO:0000313|Proteomes:UP000003163};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cuomo C.A., Sanscrainte N.D., Goldberg J.M., Heiman D., Young S., Zeng Q.,
RA   Becnel J.J., Birren B.W.;
RT   "Contrasting host-pathogen interactions and genome evolution in two
RT   generalist and specialist microsporidian pathogens of mosquitoes.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA helicase participates in several chromatin remodeling
CC       complexes, including the SWR1 and the INO80 complexes.
CC       {ECO:0000256|RuleBase:RU363048}.
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|ARBA:ARBA00001665,
CC         ECO:0000256|RuleBase:RU363048};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU363048}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|ARBA:ARBA00007519,
CC       ECO:0000256|RuleBase:RU363048}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJW04858.1}.
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DR   EMBL; AFBI03000012; EJW04858.1; -; Genomic_DNA.
DR   AlphaFoldDB; J8ZYV3; -.
DR   STRING; 1003232.J8ZYV3; -.
DR   VEuPathDB; MicrosporidiaDB:EDEG_00951; -.
DR   HOGENOM; CLU_028311_1_1_1; -.
DR   InParanoid; J8ZYV3; -.
DR   OMA; VYSKEYD; -.
DR   OrthoDB; 5479950at2759; -.
DR   Proteomes; UP000003163; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR027238; RuvB-like.
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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU363048};
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU363048};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU363048};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU363048};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363048};
KW   Hydrolase {ECO:0000256|RuleBase:RU363048};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363048};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU363048};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003163};
KW   Transcription {ECO:0000256|RuleBase:RU363048};
KW   Transcription regulation {ECO:0000256|RuleBase:RU363048}.
FT   DOMAIN          53..342
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   417 AA;  47175 MW;  DB85DD9D5B41765C CRC64;
     MSRKLPLLYS HIKGLGIDEK HQPQSSLNTI IGQENARKAA SIIVEMVRQN RFSGHGIFIV
     GPSGCGKTAL AYAMSQEIGC EIPFNIISST EITSSEINKS EALMQYARMS TKIIIKEIKD
     IYEGEVVSIS IVEDDTVVNK GEGRILFAKL ELRTSKECLE VKISPLLYEM YENENIDIGD
     IIYIESNSGV LKKIGRCEQF LNETEIEAEN YVPLPKTEVM RRRELWREVT LHEMDESNSR
     PTGSDPISSF NRMLNSKKPE ISDFIRNNIN DVVNEYVKNG NCNVIKGVLF IEDADLLDAH
     CISSINKILD GILSPIIILS MNKVDENNVP IFTVPKELLN RFLIIQMCKN TKENQKTILK
     AHLIAEKMEI DDETFEYLST ISLRQVIGLI PLLKTIPEDL SKHNVQKLFS SFCLSDQ
//
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