ID A7RIX4_NEMVE Unreviewed; 1429 AA.
AC A7RIX4;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000256|ARBA:ARBA00019805, ECO:0000256|RuleBase:RU368001};
DE EC=3.6.4.- {ECO:0000256|RuleBase:RU368001};
GN ORFNames=NEMVEDRAFT_v1g238634 {ECO:0000313|EMBL:EDO48474.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO48474.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO48474.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- FUNCTION: ATPase component of the INO80 complex which remodels
CC chromatin by shifting nucleosomes and is involved in DNA repair.
CC {ECO:0000256|RuleBase:RU368001}.
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;
CC Evidence={ECO:0000256|RuleBase:RU368001};
CC -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex.
CC {ECO:0000256|RuleBase:RU368001}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368001}.
CC -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC {ECO:0000256|RuleBase:RU368001}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025, ECO:0000256|RuleBase:RU368001}.
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DR EMBL; DS469513; EDO48474.1; -; Genomic_DNA.
DR RefSeq; XP_001640537.1; XM_001640487.1.
DR STRING; 45351.A7RIX4; -.
DR EnsemblMetazoa; EDO48474; EDO48474; NEMVEDRAFT_v1g238634.
DR eggNOG; KOG0388; Eukaryota.
DR HOGENOM; CLU_000315_19_1_1; -.
DR InParanoid; A7RIX4; -.
DR OMA; DHRIMRS; -.
DR PhylomeDB; A7RIX4; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45685:SF2; CHROMATIN-REMODELING ATPASE INO80; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF13892; DBINO; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51413; DBINO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368001};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU368001};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU368001};
KW DNA-binding {ECO:0000256|RuleBase:RU368001};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368001};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT DOMAIN 263..388
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 515..689
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 991..1146
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 185..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 344..374
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 193..222
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1429 AA; 161431 MW; 4C7283FAF6FABF65 CRC64;
MAAAPLRRGM MVMGRIARIL PTRLSKSAIT DSQPKHEGSW LYTLENPPNL SWLRPRQPGD
TDDSEVGDLG KTLPEGIRLS LVNGDVSDSG SLINGCLRPE ELHVDKSRLY NFTKVKKDRR
WLKEMLLSDS SSSSDEEQPM TDEDLHEMLW LHKQQKLARQ RFLRGGELSQ YQHYSASLLY
TQDKYHDSQK QRGNAKKLKK KKMKDGSLKI VKVKKEKMRI KKKRKKSEDQ SDGDRRESGT
IDERLMKRTL IRRKEADAKR RKLWALICRK EIPRTQRQKS SARNNTLSNA KKLAQLCQKE
RRREAQRSQK IAQQTVPRAR RLVREMMVYW KKYEKVEKEH RKRVEKEAME QRKLDDELRE
ARRQQRKLNF LITQTELYAH FMGKKLKGNK MSASSDVHHI LSKLDEPSDK SKIKSVSGGV
LIDMENSDNY DARAMKMEAL ANAENAFRLQ EAKRQAFDVN SQESGGSKKI ALSQESFDVN
FSLANPNISG EDHPQPNLFQ GKLKTYQLKG MNWLISLYEQ GISGILADEM GLGKTVQSIA
FLSYLAETHN IWGPFLVVAP ASTLHNWQQE VSRFIPQFKV LPYWGNQGDR KSLRKFWSQK
QTHISDRNHA PFHLLITSYQ LVVQDVRYFQ RIKWQYIVLD EAQAIKSSSS VRWKILLGYQ
CRNRLLLTGT PIQNSMAELW ALLHFIMPTL FDNHEEFNEW FSKDIESHAE NKSLIDQNQL
SRLHMILKPF MLRRIKKDVE NELSEKIEIK LVCGLTTRQK WLYQAVKQKI SIDDLVYTSA
SSSATSATTS SLMNLVMQFR KVCNHPELFE RRDVTSPVTV QLPPYVIPKL IYRKVPESEC
FSFLRFAGIS LEEASMMMLG SPSHRLLLLL ILLRKVMLLH HKRSWSPSKS SSSVLVPNLM
EKKVVAVCEL SYCSDRSAAY EHQELARGGP DESRNLLLYG SPEAVDMKEY RAHLFPPPLG
GLEATQPSKG WSFVQMPNRN SVISDSGKLT VLDGLLTKLK LQGHRVLIYS QMTRMIDILE
EYMTFRKHKY MRLDGSSKIS DRRDMVADFQ NNKDIFVFLL STRAGGLGIN LTAADTVIFY
DSDWNPTVDE QAMDRAHRLG QTKQVTVYRL VTKNTIEERI LQRAREKSEI QKMVISGGNF
KPDALKPKEV VSLLLDDEEL ENKFLQRQAE KKADEQRKRR ERKRKKGGTD EGTSSPSIEI
SETSTPPPKA KKGRKSKTSL FPPAPEGVPT ASVPPSEASS VNGDASARLE GADADDISVM
SLDEISMVSG DGSLYSMDAP PSSSATPFNE DSLLGDAEPK SETASPSTAE GKRGRGRGRA
RGRGRTRGRG TAPIRTSRGR GRGRGGTGVM AASAAASAAA AAASAAAYAA YGFTFQGTPT
PPPPAARSSP VAFGSGGSTV PGSAVTHPVP RYDNSSANSS PARHRDVEN
//
