ID   RUVB1_XENLA             Reviewed;         456 AA.
AC   Q9DE26;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=RuvB-like 1;
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9Y265};
DE   AltName: Full=Pontin;
GN   Name=ruvbl1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10842076; DOI=10.1016/s0925-4773(00)00305-1;
RA   Etard C., Wedlich D., Bauer A., Huber O., Kuehl M.;
RT   "Expression of Xenopus homologs of the beta-catenin binding protein
RT   pontin52.";
RL   Mech. Dev. 94:219-222(2000).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30561330; DOI=10.7554/elife.38497;
RA   Huizar R.L., Lee C., Boulgakov A.A., Horani A., Tu F., Marcotte E.M.,
RA   Brody S.L., Wallingford J.B.;
RT   "A liquid-like organelle at the root of motile ciliopathy.";
RL   Elife 7:0-0(2018).
CC   -!- FUNCTION: Has single-stranded DNA-stimulated ATPase and ATP-dependent
CC       DNA helicase (3' to 5') activity suggesting a role in nuclear processes
CC       such as recombination and transcription (By similarity). Proposed core
CC       component of the chromatin remodeling INO80 complex which exhibits
CC       DNA- and nucleosome-activated ATPase activity and catalyzes ATP-
CC       dependent nucleosome sliding (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y265}.
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:0000250|UniProtKB:Q9Y265};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y265};
CC   -!- SUBUNIT: Forms homohexameric rings (By similarity). Can form a
CC       dodecamer with ruvbl2 made of two stacked hexameric rings (By
CC       similarity). Is a component of the RNA polymerase II holoenzyme
CC       complex. Component of the chromatin-remodeling Ino80 complex (By
CC       similarity). Component of some MLL1/MLL complex (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y265}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Dynein axonemal particle
CC       {ECO:0000269|PubMed:30561330}.
CC   -!- DEVELOPMENTAL STAGE: Strong expression in neural crest cells and in
CC       later stages in different gastrointestinal organs.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR   EMBL; AF218072; AAG44127.1; -; mRNA.
DR   AlphaFoldDB; Q9DE26; -.
DR   SMR; Q9DE26; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0120293; C:dynein axonemal particle; IDA:UniProtKB.
DR   GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:InterPro.
DR   GO; GO:0097255; C:R2TP complex; IEA:InterPro.
DR   GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
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:0006310; P:DNA recombination; 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; 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; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..456
FT                   /note="RuvB-like 1"
FT                   /id="PRO_0000165643"
FT   BINDING         70..77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   456 AA;  50358 MW;  AFD3696AA9289FC8 CRC64;
     MKIEEVKSTT KTQRIATHSH VKGLGLDENG IAKQAAAGLV GQENAREACG VIVELIKSKK
     MAGRAVLLAG PPGTGKTALA LAIAQELGNK VPFCPMVGSE VYSTEIKKTE VLMENFRRAI
     GLRIRETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL KLDPSIYESL
     QKERVEVGDV IYIEANSGAV KRQGRSDTYA TEFDLEAEEY VPLPKGDVHQ KKEVIQDVTL
     HDLDVANARP QGGQDILSMM GQLMKPKKTE ITDKLRGQIN KVVNKYIDQG IAELVPGVLF
     IDEVHMLDIE CFTYLHRALE SSLAPIVIFA TNRGNCIIRG TEDVASPHGI PLDLLDRVMI
     IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK TTLRYSVQLL TPANLLAKIN
     GKDSIEKEHV EEINELFYDA KSSAKILAEQ QEKFMK