ID A0A3Q3AS52_KRYMA Unreviewed; 438 AA.
AC A0A3Q3AS52;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000019240.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000019240.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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DR AlphaFoldDB; A0A3Q3AS52; -.
DR Ensembl; ENSKMAT00000019503.1; ENSKMAP00000019240.1; ENSKMAG00000014273.1.
DR GeneTree; ENSGT00940000153556; -.
DR Proteomes; UP000264800; Unplaced.
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; IPR012340; NA-bd_OB-fold.
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:SF2; RUVB-LIKE 2; 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; 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|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:UP000264800};
KW Transcription {ECO:0000256|RuleBase:RU363048};
KW Transcription regulation {ECO:0000256|RuleBase:RU363048}.
FT DOMAIN 68..360
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 438 AA; 48436 MW; 4B03CA03AD7139C9 CRC64;
LIQMATTKVP EVRDITRIER IGAHSHIRGL GLDDALEPRQ VSQGMVGQLA SRRAAGVILE
MIKDGHIAGR AVLIAGQPGT GKTAIAMGIA QSLGLDTPFT ALAGSEIFSL EMSKTEALSQ
AFRKAIGVRI KEETEIIEGE VVEIQIDRPA TGTGSKVGKL TLKTTEMETI YDLGNKMIDS
LSKEKVQAGD VITIDKATGK ISKLGRSFTR ARDYDAMGAQ TQFVQCPEGE LQKRKEVVHT
VSLHEIDVIN SRTQGFLALF SGDTGEIKSE VREQINAKVC EWREEGKAEI IPGVLFIDEV
HMLDMECFSF LNRALESDLS PVLIMATNRG ITRIRGTNYQ SPHGIPIDLL DHSAFWPLSV
YKLCFFLTRI GMETSLRYAI QLISTAGLVC RKRKGTEVQV EDIKRVYSLF LDEARSSQYM
KEYQDSFLFN ETPAMDTS
//
