INO80_NEUCR
ID INO80_NEUCR Reviewed; 1997 AA.
AC Q872I5; Q7S251; V5ILU4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000250|UniProtKB:P53115};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:P53115};
DE AltName: Full=Chromatin remodeling factor 2-1;
GN Name=crf2-1; Synonyms=ino80; ORFNames=B24G20.040, NCU08919;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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-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. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD70746.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX294010; CAD70746.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM002240; ESA42365.1; -; Genomic_DNA.
DR RefSeq; XP_011394745.1; XM_011396443.1.
DR AlphaFoldDB; Q872I5; -.
DR SMR; Q872I5; -.
DR STRING; 5141.EFNCRP00000008850; -.
DR PRIDE; Q872I5; -.
DR EnsemblFungi; ESA42365; ESA42365; NCU08919.
DR GeneID; 3874826; -.
DR KEGG; ncr:NCU08919; -.
DR VEuPathDB; FungiDB:NCU08919; -.
DR HOGENOM; CLU_000315_26_1_1; -.
DR InParanoid; Q872I5; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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-rel_dom; 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; Coiled coil; DNA damage; DNA repair; DNA-binding;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1997
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000074327"
FT DOMAIN 881..1006
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 1130..1302
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1702..1858
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1891..1986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 666..735
FT /evidence="ECO:0000255"
FT MOTIF 1253..1256
FT /note="DEAQ box"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..170
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1912..1934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1143..1150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1997 AA; 223073 MW; 749AF1E8F98F1142 CRC64;
MDHFSTVLQR PPHFDEDGTE GRGDRGNGAG PGPAPPPPPP RGGLRDILNP VSSNSAVQSQ
AAAAAPPPPP AVASSSLHGI AASVPPPSST NSMRATPHSS SSFNLRSPTR EPSEYRHPLS
SLATPAPFAA SPPTSIANAN NTNNNNALGA AGSLSSQPPP PPPTGPRSIL NPPTPSQQHQ
QQHHHPNPFV AASAPSLPPP PSSLQAPPAI TPIAGLSAPA PASGSLPLSA GGIGNSITVS
SSSQPPARAS QLHAPSAYYS PAESFRDRDS SVREKSSTGG SFYDPTAEAS NGISGSSPRK
DRDRDRDHRG TTRESQRRSV SGHSDTGSSW RNATQTSASN KTRDPYNYSP SSADYYNTRK
KENYPVDNTT SSSIAAPSNF TVATRSPVAA LSHPASIAAP ASVGSLTGSI SPRLSLRPPS
MASPTIRSAV LANPTNGTTS TALPALGRND SPPSKMSPGT STNPSRAAGV MSFSNILSSS
EPVPRPRATS PNNPDDDDDV PMKVERADSS EKVVKEKKER KPRQPKQPRI SDIRHSESTP
KGRRGSTKQE SPLPNIRIPA KRMANGAPKQ QKTFSAENEE KIRKAMDRIE TRELPHEDEF
EEELRLWRER REYKRQQMNQ RDLRQRRQRR ADYTEVEAQK LKLHADFGKR RYDDLNYDDA
LQEVRERELF AEKERKKDMQ RKRRREKSMA TTMEAKAAAL ARASAAQDEA ERQKYMREAE
RANKKVQQTR LILQKGIKGP SRNTGPIEPN LEGGTMATFQ AENMEPGKTK GKGRAGARPK
KSKEQKQAEK DAAEAAQAAL DAGLELPPKE ETNKIRIKLT KTKAPKEADV DKDKENKEPQ
EPKEPKEPKE KVIKEKVVEE PKDPLELKFQ SKGFNQIYDQ IWRDLARKDV NKVFRLAIDS
YSTKSSNLKK TAILASKEAK RWQLRTNKGT KDLQARAKRV MRDMMGFWKR NEREERDLRK
AAEKQELENA RKEEADREAA RQKRKLNFLI SQTELYSHFI GKKIKTNEVE RSTDHPDEIA
AEKDKIPENE MDIEVPTGPI GAKVTNFENL DFDAEDESTL RAAAMANAQN AIAEAQKKAR
EFNKEESKLD EDGEMNFQNP TMMGDVEIEQ PKLLNCQLKE YQLKGLNWLV NLYEQGINGI
LADEMGLGKT VQSISVMAYL AEKYDIWGPF LVVAPASTLH NWQQEITKFV PQFKVLPYWG
TAGDRKVLRK FWDRKHTTYK KDAPFHVMIT SYQLVVSDVA YFQKMKWQYM ILDEAQAIKS
SQSSRWKCLL GFHCRNRLLL TGTPIQNNMQ ELWALLHFIM PSLFDSHDEF SEWFSKDIES
HAQSNTKLNE DQLKRLHMIL KPFMLRRVKK HVQKELGDKI EMDVFCDLTY RQRAMYANLR
NQISIMDLIE KATLGDDDSA SLMNLVMQFR KVCNHPDLFE RADTASPYSF GHFAETASFI
REGSQVTVGY STRSLIQYEL PRLLWRDGGR LHKAGEDNQV AGWRNQWLNE KFNIWTPEHI
RESLAGTDNF SWLRFADTSY EEAYRASHKD LFARAVEMST KKNRLAEIKI AYDEPEDLNF
TPAHALFHIR EREDRRPLAE ITEQGILGSL MNVSRSAFSE TGLGRLEQAA APKASAPPIE
VVCDSRSAVV ERENIMFNAP MRKVLFGPTL AEEKALVVQK VPPSRYPPPA LLPAPDKEKQ
KFTNITVPSM RRFVTDSGKL AKLDELLREL KENGHRVLLY FQMTRMIDLM EEYLTYRNYK
YCRLDGSTKL EDRRDTVADF QTRPEIFIFL LSTRAGGLGI NLTSADTVIF YDSDWNPTID
SQAMDRAHRL GQTKQVTVYR LITRGTIEER IRKRAMQKEE VQRVVITGGS SAAGGGVDFS
GRRAPENRNR DIAMWLADDE QAEMIEKRER ELLESGELDK MQKKSRGGNK RKRGGAGGEG
KEVSLDEMYH EGEGNFDDGG NNIKGSGTAT PNGAAGGEGG DGKGAVGGAA KKRKTGGSKK
AKTTKQRLAI ADGEIDI
