GenomeNet

Database: UniProt
Entry: A7TJI3
LinkDB: A7TJI3
Original site: A7TJI3 
ID   INO80_VANPO             Reviewed;        1556 AA.
AC   A7TJI3;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   13-NOV-2019, entry version 77.
DE   RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
GN   Name=INO80; ORFNames=Kpol_534p5;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294)
OS   (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
OC   Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M.,
RA   Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two
RT   yeast species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- FUNCTION: ATPase component of the INO80 complex which remodels
CC       chromatin by shifting nucleosomes and is involved in DNA repair.
CC       {ECO:0000255|PROSITE-ProRule:PRU00746}.
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:0000250|UniProtKB:P53115};
CC   -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex.
CC       {ECO:0000255|PROSITE-ProRule:PRU00746}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00746}.
CC   -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC       {ECO:0000250|UniProtKB:Q9ULG1}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
DR   EMBL; DS480402; EDO17526.1; -; Genomic_DNA.
DR   RefSeq; XP_001645384.1; XM_001645334.1.
DR   SMR; A7TJI3; -.
DR   STRING; 36033.XP_001645384.1; -.
DR   PRIDE; A7TJI3; -.
DR   EnsemblFungi; EDO17526; EDO17526; Kpol_534p5.
DR   GeneID; 5545748; -.
DR   KEGG; vpo:Kpol_534p5; -.
DR   eggNOG; KOG0388; Eukaryota.
DR   eggNOG; ENOG410XP0A; LUCA.
DR   InParanoid; A7TJI3; -.
DR   KO; K11665; -.
DR   OMA; GCQREVK; -.
DR   OrthoDB; 188211at2759; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0031011; C:Ino80 complex; IEA:EnsemblFungi.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IEA:EnsemblFungi.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043486; P:histone exchange; IEA:EnsemblFungi.
DR   GO; GO:0042766; P:nucleosome mobilization; IEA:EnsemblFungi.
DR   GO; GO:0016584; P:nucleosome positioning; IEA:EnsemblFungi.
DR   GO; GO:0080040; P:positive regulation of cellular response to phosphate starvation; IEA:EnsemblFungi.
DR   GO; GO:0090053; P:positive regulation of chromatin silencing at centromere; IEA:EnsemblFungi.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0051983; P:regulation of chromosome segregation; IEA:EnsemblFungi.
DR   GO; GO:0060303; P:regulation of nucleosome density; IEA:EnsemblFungi.
DR   GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:EnsemblFungi.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IEA:EnsemblFungi.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR020838; DBINO.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR031047; Ino80.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45685:SF2; PTHR45685:SF2; 1.
DR   Pfam; PF13892; DBINO; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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   Activator; ATP-binding; Complete proteome; DNA damage; DNA repair;
KW   DNA-binding; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN         1   1556       Chromatin-remodeling ATPase INO80.
FT                                /FTId=PRO_0000350965.
FT   DOMAIN      572    697       DBINO. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00746}.
FT   DOMAIN      812    984       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1381   1535       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     825    832       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       935    938       DEAQ box.
FT   COMPBIAS      8    104       Asn-rich.
FT   COMPBIAS    149    301       Lys-rich.
FT   COMPBIAS    322    391       Glu-rich.
FT   COMPBIAS    518    521       Poly-Lys.
FT   COMPBIAS   1545   1549       Poly-Ala.
FT   MOD_RES     156    156       Phosphothreonine. {ECO:0000250}.
SQ   SEQUENCE   1556 AA;  180155 MW;  A6B916E7B577D449 CRC64;
     MSLAKLLNND DDDNNINLPN INVNNTNTND TSSSIVTNTH TTNTTTNLQK EKFLNKLNND
     FNLLNKRDNL ELNYQDWKFL NYQEFELLNE WNQQSKEWNN SIKNFEYLYS LMKKYKSEWE
     NYLTLKSSDK YLKNVVNDCL INSNTNNLKS KSKLKTDTKT KAKSKSKSKL KLKSNSDAKV
     KSKSSNAKAK AKTKSVSTQQ KRKRTTSIKN LLEKEDSALT SLDDMDEIDD VNEILNNDNN
     DEITQNSKDL STTTATEKKL NTKTSPSKKR KDEVRVAMKK PMTSTPNVKT ENKSKQKSNK
     KNIDADDNTY DDNNLINGKD TEELDDIEKA KDLEDNTDIE IEGTNENEDE DEDEDEDEDE
     DEEDEEEGEE EEEEEEDEEG VINMIENEDD EDYFAPGKKS GRQNASKVAG EPAAPVPKTP
     TTIHSDRERI VRELIKMCNK NKNKKSRKRR FTNSIVTDYN PEENKLIVKV TLKQYHVRKL
     KKLINDAKKL REEEEMKLKK SLMKEAENAE ELEGPSSKKK KLNSGTAQNE NGGEQNSEFI
     QNTHDLPTYG MQMTLKEAKA IKRHYDNTFF TILKDLARKD SAKMARLVQQ IQSIRATNFK
     KNSSVCAREA RKWQQRNFKQ VKDFQTRARR GIREMLNYWK KNEREERDLK KKAEKVAMEQ
     ARKEEEDREN VRQAKKLNFL LTQTELYSHF IGSKIKTNEL EGNMKDDEFD ENEDNLMNNI
     DLDSTSSVKT DFKTIDFDNE DDDELRRKAA QNASNVLQKS REKTKKFDND TSNGEELNFQ
     NPTSLGEVVI EQPSILACTL KEYQLKGLNW LANLYDQGIN GILADEMGLG KTVQSISVLA
     HLAEKYNIWG PFLVVTPAST LHNWVNEISK FVPQFKILPY WGNSNDRKIL RRFWDRKNLR
     YNKDSPFHVM ITSYQMVVSD TSYLQKMKWQ YMILDEAQAI KSSQSSRWRN LLSFHCRNRL
     LLTGTPIQNN MQELWALLHF IMPSLFDSHD EFNDWFSKDI ESHAEANTKL NQQQLRRLHM
     ILKPFMLRRV KKNVQSELGD KIEIDVMCDL TQRQAKLYQI LKSQMSTNYD VIENAAGDDD
     TGSDQNMINA VMQFRKVCNH PDLFERADVD SPFSFSIFGK SSSLSRDNEP LVDILYSTRN
     PITYHLPRLI YNDLILPNYE NDLGLKNKLL NYTFSIFNNE STCKEISRVT GLTYGEIKRV
     VHRDLLMNAI HLKEPYSRQT FLEKISVIED NDKTFSDMNF KSNLKLIERS AKLDALSRVT
     STGVLNSLLN IKEQVFDNEY YNAISRSYHP NVSSSPVSIQ VLGNRHFSIQ QEEELFKPVI
     SKALSEIPAS TQYNMAVEKK IPLHDFPVSG LYPSPLNKSF SSYISMPSMD RFITESAKLK
     KLDELLVELK KGDHRVLIYF QMTKMMDLME EYLTYRQYSH IRLDGSSKLE DRRDLVHDWQ
     TRPDIFIFLL STRAGGLGIN LTAADTVIFY DSDWNPTIDS QAMDRAHRLG QTRQVTVYRL
     LIRGTIEERM RDRAKQKEHV QQVVMEGKTL QKDVKTIESG GDVKAAAAAS TALTTN
//
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