RUVB1_DANRE
ID RUVB1_DANRE Reviewed; 456 AA.
AC Q8AWW7;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=RuvB-like 1;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9Y265};
DE AltName: Full=Pontin;
DE AltName: Full=zPontin;
GN Name=ruvbl1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|EMBL:AAM18788.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12464178; DOI=10.1016/s0092-8674(02)01112-1;
RA Rottbauer W., Saurin A.J., Lickert H., Shen X., Burns C.G., Wo Z.G.,
RA Kemler R., Kingston R., Wu C., Fishman M.;
RT "Reptin and pontin antagonistically regulate heart growth in zebrafish
RT embryos.";
RL Cell 111:661-672(2002).
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). May act as a negative
CC regulator of embryonic heart growth (PubMed:12464178).
CC {ECO:0000250|UniProtKB:Q9Y265, ECO:0000269|PubMed:12464178}.
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 complex
CC (By similarity). Component of the chromatin-remodeling Ino80 complex
CC (By 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:0000250|UniProtKB:Q9DE26}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR EMBL; AY092764; AAM18788.1; -; mRNA.
DR AlphaFoldDB; Q8AWW7; -.
DR SMR; Q8AWW7; -.
DR STRING; 7955.ENSDARP00000012488; -.
DR PaxDb; Q8AWW7; -.
DR ZFIN; ZDB-GENE-030109-2; ruvbl1.
DR eggNOG; KOG1942; Eukaryota.
DR InParanoid; Q8AWW7; -.
DR PhylomeDB; Q8AWW7; -.
DR Reactome; R-DRE-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-DRE-5689603; UCH proteinases.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR Reactome; R-DRE-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DRE-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR PRO; PR:Q8AWW7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:ZFIN.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0097255; C:R2TP complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0070286; P:axonemal dynein complex assembly; IMP:ZFIN.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0060420; P:regulation of heart growth; IMP:ZFIN.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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_0000165642"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 456 AA; 50367 MW; 32C1E5C8F24D08C7 CRC64;
MKIEEVKSTT KTQRIASHSH VKGLGLDEAG NAKQSASGLV GQESAREACG IITELIRSKK
MAGRAILLAG PPGTGKTALA LAMAQELGNK VPFCPMVGSE VYSSEIKKTE VLMENFRRAI
GLRIKETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL KLDPSIYESL
QKERVEVGDV IYIEANSGAV KRQGRCDTFA TEFDLEAEEY VPLPKGDVHE KKEIIQDVTL
HDLDVANARP QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG VAELVPGVLF
IDEVHMLDIE CFTYLHRALE SSIAPIVVFA SNRGNCLIRG TEDISSPHGI PLDLLDRVMI
IRTMLYTPQE MKQIIKIRAQ TEGLNISEEA LSHLGEIGTK TTLRYAVQLL TPASLLARVQ
GREVVEKEHV EEINELFYDA KSSAKILQDQ HTKFMK
