ID   RUVB1_ENCCU             Reviewed;         426 AA.
AC   Q8STP2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=RuvB-like protein 1;
DE            Short=RUVBL1;
DE            EC=3.6.4.12;
DE   AltName: Full=TIP49-homology protein 1;
DE   AltName: Full=TIP49a homolog;
GN   Name=RVB1; OrderedLocusNames=ECU09_1390;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16691553; DOI=10.1002/pmic.200500796;
RA   Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT   "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT   (microsporidia): a reference map for proteins expressed in late sporogonial
RT   stages.";
RL   Proteomics 6:3625-3635(2006).
CC   -!- FUNCTION: DNA helicase which participates in several chromatin
CC       remodeling complexes, including the SWR1 and the INO80 complexes. The
CC       SWR1 complex mediates the ATP-dependent exchange of histone H2A for the
CC       H2A variant HZT1 leading to transcriptional regulation of selected
CC       genes by chromatin remodeling. The INO80 complex remodels chromatin by
CC       shifting nucleosomes and is involved in DNA repair. Also involved in
CC       pre-rRNA processing (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Component of the SWR1 chromatin remodeling complex, the INO80
CC       chromatin remodeling complex, and of the R2TP complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC       {ECO:0000269|PubMed:16691553}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR   EMBL; AL590451; CAD27111.1; -; Genomic_DNA.
DR   RefSeq; XP_955692.1; XM_950599.1.
DR   AlphaFoldDB; Q8STP2; -.
DR   SMR; Q8STP2; -.
DR   STRING; 284813.Q8STP2; -.
DR   GeneID; 860477; -.
DR   KEGG; ecu:ECU09_1390; -.
DR   VEuPathDB; MicrosporidiaDB:ECU09_1390; -.
DR   HOGENOM; CLU_028311_1_1_1; -.
DR   InParanoid; Q8STP2; -.
DR   OMA; VYSKEYD; -.
DR   OrthoDB; 752343at2759; -.
DR   Proteomes; UP000000819; Chromosome IX.
DR   GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:InterPro.
DR   GO; GO:0097255; C:R2TP complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.360; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; IPR041048; RuvB-like_C.
DR   InterPro; IPR037938; RUVBL1.
DR   InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR   InterPro; IPR010339; TIP49_P-loop.
DR   PANTHER; PTHR11093; PTHR11093; 1.
DR   PANTHER; PTHR11093:SF6; PTHR11093:SF6; 1.
DR   Pfam; PF06068; TIP49; 1.
DR   Pfam; PF17856; TIP49_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   Activator; ATP-binding; Chromatin regulator; DNA damage; DNA repair;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..426
FT                   /note="RuvB-like protein 1"
FT                   /id="PRO_0000381758"
FT   BINDING         62..69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   426 AA;  47308 MW;  76C11B0B46057B1E CRC64;
     MVKSSNIAIH SHVRSLGLDD CGNPVEKPDA VIGQENAREA AGLIVEMVRT KRMSGRAVLI
     SGPVGSGKTA LAVGISEELG AGTPFTSMSG SEVYSNEVKK TEVLEEALRR SILVRMRELK
     DVYEGEVVEL RIVDEENPLS SYPKRIKEMF VILKTSKESK KLKLAPSLYE QIDKQRIVNG
     DVVYIEVNSG VIKKLGRSEA HMNDFDLEAD TYVPIPKGEV LKRKEVMQSV TLHDLDMANA
     RPSGQDMLSL VFRILSPRKT EITERLRGDV NRMVNGYLEN GNAEIVPGVL FIDEVHMLDV
     ECFTFLHKVI ESPLSPTIIF ASNKGMAPIK GSDGLLGPFG ITKDLLDRIV IISVKRNPDE
     ANREIIRRRM KEEGLEMDDD AFGFFVGLST SRSLRYCISL IPLLKTYGGC VSVRNVEEVA
     ELFHDS