ID A0A226N0P6_CALSU Unreviewed; 1550 AA.
AC A0A226N0P6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=ASZ78_008440 {ECO:0000313|EMBL:OXB61156.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB61156.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB61156.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB61156.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB61156.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXB61156.1}.
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DR EMBL; MCFN01000294; OXB61156.1; -; Genomic_DNA.
DR STRING; 9009.A0A226N0P6; -.
DR Proteomes; UP000198323; Unassembled WGS sequence.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd18002; DEXQc_INO80; 1.
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; IPR031047; DEXQc_INO80.
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; 3.
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:UP000198323}.
FT DOMAIN 281..406
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 539..710
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1058..1254
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 47..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1361..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1494..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 362..392
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 136..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..229
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1550 AA; 175915 MW; 03F3D302C62E17F3 CRC64;
MASELGARED GSCSELAKPL YLQYLEKALR LDQFLRQTSA IFNRNISSDE SEDGLDDNPL
LPQSGDPLMQ VKEEPPNALL GESSGVGNSG VLNAHSLNGV LQPEMKSEKG SLYNFSKLKK
SRKWLKSILL SDDSSDTDSP SDEDGEDEEE FSLSREELHN MLRLHKYKKL HQSKYSKDKE
LQQYQYYSAG LLSTYDPYYE QQRHLLGPKK KKFKEEKKLK GKLKKVKKKR RRDEDLSSEE
SPEHHHHQTK VFAKFSHDTP PPGSKKKHMS IEQLNARRRK VWLSIVKKEL PKAYKQKASA
RNLFLTNSKK LAHQCMREVR RAALQAQKNC KETLPRARRL TKEMLLYWKK YEKVEKEHRK
RAEKEALEQR KLDEEMREAK RQQRKLNFLI TQTELYAHFM SRKRDIGHDG IQEEILRKLE
DSSTQRQIDI GGGVVVNITQ EDYDSNYYKA QALKNAEDAY QIHQARVCMF RIHETRSFDE
DAKESRAAAL RAANKSGTGF GESYSLANPS IRAGEDIPQP TIFNGKLKGY QLKGMNWLAN
LYEQGINGIL ADEMGLGKTV QSIALLAHLA ERENIWGPFL IISPASTLNN WHQEFARFVP
KFKVLPYWGN PHDRKVIRKF WSQKTLYTQD APFHVVITSY QLVVQDVKYF QRVKWQYMVL
DEAQALKSSS SVRWKILLQF QCRNRLLLTG TPIQNTMAEL WALLHFIMPT LFDSHEEFNE
WFSKDIESHA ENKSAIDENQ LSRLHMILKP FMLRRIKKDV ENELSDKIEV LMYCQQTSRQ
KLLYQALKNK ISIDDLLQSS MGTTQQAQTT TSSLMNLVMQ FRKVKLYFCD IGINEESCFS
FLRFIDVSPA EMANLMNQGH LARWLALFLS LKASYRLHHL RFWMEPEREK QQGSRCLENK
DFLLDVNFPL SFPNLHSCTL LQNLVFSSHC RAVTGYSDHV ILRRRSATSR ARCCQVTELP
SFLCIASPRV TAVPLEFYCN DRSAEYERRA LREGGSLEAK QCVVNGAPEL AADWQKQSSQ
FFPEYPGGLL GIRPQNGWSF IRIPDKESLI TDSGKLHALD LLLTRLKSQG HRVLIYSQMT
RMIDLLEEYM VYRKHTYMRL DGSSKISERR DMVADFQNRN DIFVFLLSTR AGGLGINLTA
ADTVEILMYV TRRKDILERS WIAGLTVGAN AIFIQCIVEL VFLLVIFYDS DWNPTVDQQA
MDRAHRLGQT KQVTVYRLIC KGTIEERILQ RAKEKSEIQR MVISGGNFKP DTLKPKEVVS
LLLDDEELEK KLRQRQEEKR QQEETNRVKE RKRKREKYAE KKKKEDELDG KRKKEGMNLV
IPFVPSADNS NLSADGDDSF VSVDSAMPSP FSEISISSEL HMGSIPPDES SSDMLVIVDD
PASSAPQSRA TNSPASITGS VSDTINGVSM QDAPLTGRGQ SNRSRGRPKG GSAGAKGTGK
GRSRKSIAGS AAAMAGAKAG AAAASAAAYA AYGYNVSKGM SSSSPLQTAI IRPSGLADFG
PSSASSPLSS PLSKGNSVCG TPKSLNLTSS LASETAIRKQ SKGAHTSGGR
//
