ID A0A096MHQ1_POEFO Unreviewed; 456 AA.
AC A0A096MHQ1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000030942.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000030942.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling Ino80
CC complex which exhibits DNA- and nucleosome-activated ATPase activity
CC and catalyzes ATP-dependent nucleosome sliding.
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:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC -!- SUBCELLULAR LOCATION: Dynein axonemal particle
CC {ECO:0000256|ARBA:ARBA00024190}. Nucleus
CC {ECO:0000256|RuleBase:RU363048}.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|ARBA:ARBA00007519,
CC ECO:0000256|RuleBase:RU363048}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYCK01007866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007559732.1; XM_007559670.2.
DR AlphaFoldDB; A0A096MHQ1; -.
DR STRING; 48698.ENSPFOP00000030942; -.
DR Ensembl; ENSPFOT00000024460.1; ENSPFOP00000030942.1; ENSPFOG00000003640.2.
DR GeneID; 103143219; -.
DR KEGG; pfor:103143219; -.
DR CTD; 8607; -.
DR eggNOG; KOG1942; Eukaryota.
DR GeneTree; ENSGT00940000153556; -.
DR OrthoDB; 5479950at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0120293; C:dynein axonemal particle; IEA:UniProtKB-SubCell.
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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; 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 DNA damage {ECO:0000256|RuleBase:RU363048};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU363048}; DNA repair {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:UP000028760};
KW Transcription {ECO:0000256|RuleBase:RU363048};
KW Transcription regulation {ECO:0000256|RuleBase:RU363048}.
FT DOMAIN 62..365
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 456 AA; 50433 MW; 49DB7E381417C210 CRC64;
MKIEEVKSTT KTQRIASHSH VKGLGLDEAG NAKQTACGLV GQETAREACG IIVEMIRSKK
MAGRAVLLAG PPGTGKTALA LAMAQELGNK VPFCPMVGSE VYSSEIKKTE VLMENFRRAI
GLRIKETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL KLDPSIYESL
QKERVEVGDV IYIEANSGAV KRQGRCDTFA TEFDLEAEEY VPLPKGDVHK KKEIVQDVTL
HDLDVANARP QGGQDILSMM GQLMKPKKTE ITDKLRAEIN KVVNRYIDQG VAELVPGVLF
VDEVHMLDIE CFTYLHRALE SSIAPIVVFA SNRGKCLIRG TEDISSPHGI PLDLLDRVMI
IRTMLYTPQE MKQIVKIRAQ TEGISISEEA LTHLAEIGTK TTLRYAVQLL TPASLLGRVQ
GKETVEREQV EEINELFYDA KSSAKILQDQ QHKFMK
//