ID A0A0D2SXC4_GOSRA Unreviewed; 1533 AA.
AC A0A0D2SXC4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=B456_006G135500 {ECO:0000313|EMBL:KJB35980.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB35980.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB35980.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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; CM001745; KJB35980.1; -; Genomic_DNA.
DR EnsemblPlants; KJB35980; KJB35980; B456_006G135500.
DR Gramene; KJB35980; KJB35980; B456_006G135500.
DR Proteomes; UP000032304; Chromosome 6.
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 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:UP000032304}.
FT DOMAIN 348..473
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 594..765
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1205..1365
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 28..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1414..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 420..459
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 486..501
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1533 AA; 174519 MW; 4F3E8111FFFE0293 CRC64;
MEPRRQSKDS FSYSGLFNLE PLMNFKVPQP DDDFDYYGNS SQDESRGGAM SHHGNGTMSE
RELSLAKRKW RGALNSDEED DDYQGTHITE ERYRSMLGEH VQKYKRRFKD TSASPAPSRM
GIPAPKSNLG SSKNRKLLNE QRAGFYDMET TSEWMNDVSS QRFANYHEAD LVPKIMYEPA
YLDIGEGITF KIPPTYDKLA LSLNLPSFSD IRVEEFYLKG TLDLGSLATM MASDKRFGSR
SRAGMGEPHP QYESLQARLK ALAASNSSQK FSLKVSESAL NSSIPEGAAG NLQRSILSEG
GVLQVYYVKV LEKGDTYEII ERSLPKKPKV KKDPSVIERE EMEKIGKVWV TIVRRDIPKH
HRNFTNFHRK QLIDSKRFAE NCQREVKLKV SRSLKFMRGA ALRTRKLARD MLLFWKRVDK
EMAEVRKREE REAAEALRRE QELREAKRQQ QRLNFLIQQT ELYSHFMQNK ANSQPSEALP
AKDEESNDDE KEDDGGPGVE EDPEEAELKK EALRAAQDAV SKQKKLTSAF DTECIKLRQA
AETEVPLEDN SVAGSSNIDL HNPSTMPVTS TVQTPEMFKG SLKEYQLKGL QWLVNCYEQG
LNGILADEMG LGKTIQAMAF LAHLAEEKNI WGPFLVVAPA SVLNNWADEI SRFCPALKTL
PYWGGLQERM VLRKNINPKR LYRREAGFHI LITSYQLLVS DEKYFRRVKW QYMVLDEAQA
IKSSSSIRWK TLLSFNCRNR LLLTGTPIQN NMAELWALLH FIMPTLFDSH EQFNEWFSKG
IENHAEHGGT LNEHQLNRLH AILKPFMLRR VKKDVISELT RKTEIMVHCK LSSRQQAFYQ
AIKNKISLAE LFDSNRGHLN EKKILNLMNI VIQLRKVCNH PELFERNEGS TYFYFGEIPN
SLLPPPFGEL EDIHYAGSHN PITYKLPKLV QQEVLQNSET LCSAVARGVY QEMFYKYFNV
FSSGNVYQSI FQQESISNEC CVRSGTFGFS RLMDLSPAEV AFLGTGSFME RLLFSISRVD
NQFLDGTLDD LMEVLDDDFS PSYLEMGTVR VVTRMLLMPS RSKTNLLRRR IATGPGSDPF
EALVVSHQDR LLSNTKLLHS TYTFIPRTRA PPIGAQCSDR NFAYRMTEEL HNPWVKRLLI
GFARTSEYNG PRMPDGPHCL IQEIDSQLPV ALPALQLTYK IFGSCPPMQS FDHAKLLTDS
GKLQTLDILL KRLRAENHRV LLFAQMTKML NILEDYMNYR KYRYLRLDGS STIMDRRDMV
RDFQLRNDIF VFLLSTRAGG LGINLTAADT VIFYESDWNP TLDLQAMDRA HRLGQTKDVT
VYRLICKETV EEKILQRASQ KSTVQQLVMT GGHVQGDLLA PEDVVSLLLD DAQLEQKLRE
IPLQAKDRLK KKQPTKGIRL DAEGDASLED LANAGAQGTG VDPSPDPEKA KSSNKKRKSA
AERQTSAKQR ISQKTSEPSF VDNELDDALQ DDMQSQRPKR PKRPKKSVNE NLEPVITTAA
AASASGQVPG NEFGPGGFGT EMEHNMAQSN MST
//
