ID A0A1U8BDI8_NELNU Unreviewed; 1396 AA.
AC A0A1U8BDI8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 Name=LOC104613449 {ECO:0000313|RefSeq:XP_010279574.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010279574.1};
RN [1] {ECO:0000313|RefSeq:XP_010279574.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_010279574.1; XM_010281272.2.
DR GeneID; 104613449; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR GO; GO:0031011; C:Ino80 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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 Helicase {ECO:0000313|RefSeq:XP_010279574.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368001};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703}.
FT DOMAIN 351..476
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 600..771
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1212..1362
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 423..453
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1396 AA; 159898 MW; 16CBCB038E17CC22 CRC64;
MNFQFPQQDD DFDNYGNSSQ KETRGSQGRG TMRDHMNGSL LKRSSELGRR KKNRRAIEAE
AGSNSSSRRG ADRSDDEEED REYGRHISEE WYRSMLGEHI QKYRRGRFKD SSRPASIQMG
MPVLKRNLGF KGQKLGAEDR VPHGMETPSD YLNDINPRKT GSYYELTSEY GTDRFSSSAD
SAYLDLGEGI AYRIPPTYDI LAASLNLPSF SDIQVEEYYL KGTLDLGSLA VIVASDGRFG
PQRRAGIGEL QPQYESLQAR LKALPASNSV QKFNLQVSNI GLDSSSIPEG AVGGIQRSIM
SEAGTLQVYY VKVLEKGDTY EIIERSLPKK QTMKKDPTMI VKEEFEKIGK VWVNIVRRDI
PKYHKIFSNF HRKQLADAKR CSETCQREVK LKVSRSFKLM RGATNRTRKL ARDMMVFWKR
VDKEQAELRK KEEREAAEAL KREEELREAK RQQQRFNFLL SQTELYSHFM QNKSISHPSE
ALPMGDGELN DQEAALGSAE IKLGEEEDPE EAELKKEALR AAQQAVFQQR KITSAFDSEC
LKLRQAADIE GPPKDTSISG SSNIDLLHPS TMPVMSLVQT PEMFKGCLKE YQLKGLQWLV
NCYEQGLNGI LADEMGLGKT IQAMAFLGHL AEEKNIWGPF LVVAPASVLN NWADEISRFC
PDLKALPYWG GINERVILRK NINPKHLYRR ESTFHVLITS YQLLVSDEKY FRRVKWQYMV
LDEAQAIKSS NSIRWKTLLS FNCRNRLLLT GTPIQNNMAE LWSLLHFIMP TLFDSHEQFN
EWFSKGIENH AEHGGTLNEH QLNRLHAVLK PFMLRRVKKD VITEMTGKTE ITVHCKLSSR
QQAFYQAIKN KISLAELFDG SRGHLNEKKI LNLMNIVIQL RKVCNHPELF ERNEGTTYLY
FGMIPNSLLP PPFGELEDIH YAGGWNPITY KVPKLVHQET IESSEMPCSI FGHGVQQELF
QKLFNIFSPE NVYQSVLPQD KISDESYPLK SGTFGFTHLM GLSPGEVVFL AKGSFMERLL
YSIMVWNRQF LDEILDFMES EADDSEYGHL ERGTVRAVTR MLLMPSRCKS SLLRRKIATG
PGHAPYEALI VCHQDRLVFN TGLLHSTYVF IPRVRAPPIN VHCSNRNFAY KMVEELHHPW
VKRLFFGFAR TSECNGPRMP NGPPHHLIQV IDSEVPVEQP ILQLTYKIFG SSPPMRSFDS
AKMLTDSGKL QTLDILLKRL RAENHRVLLF AQMTKMLNIL EDYMNYRKYR YLRLDGSSTI
MDRRDMVRDF QHRSDIFVFL LSTRAGGLGI NLTAADTVIF YESDWNPTLD LQAMDRAHRL
GQTKEVTVYR LICKETVEEK ILQRASQKNA VQQLVMTGGH VQGDLLTPED VVSLLLDDAQ
LERKLREAPA QLCLFH
//
