ID A0A1E3NR43_9ASCO Unreviewed; 1221 AA.
AC A0A1E3NR43;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000256|ARBA:ARBA00019805, ECO:0000256|RuleBase:RU368001};
DE EC=3.6.4.- {ECO:0000256|RuleBase:RU368001};
DE Flags: Fragment;
GN ORFNames=PICMEDRAFT_26067 {ECO:0000313|EMBL:ODQ48544.1};
OS Pichia membranifaciens NRRL Y-2026.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=763406 {ECO:0000313|EMBL:ODQ48544.1, ECO:0000313|Proteomes:UP000094455};
RN [1] {ECO:0000313|EMBL:ODQ48544.1, ECO:0000313|Proteomes:UP000094455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2026 {ECO:0000313|EMBL:ODQ48544.1,
RC ECO:0000313|Proteomes:UP000094455};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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|ARBA:ARBA00001836,
CC 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV454001; ODQ48544.1; -; Genomic_DNA.
DR RefSeq; XP_019019657.1; XM_019162429.1.
DR AlphaFoldDB; A0A1E3NR43; -.
DR STRING; 763406.A0A1E3NR43; -.
DR GeneID; 30179116; -.
DR OrthoDB; 5475375at2759; -.
DR Proteomes; UP000094455; 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 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000094455}.
FT DOMAIN 237..362
FT /note="DBINO"
FT /evidence="ECO:0000259|PROSITE:PS51413"
FT DOMAIN 491..663
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1050..1209
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 105..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 306..348
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 105..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ODQ48544.1"
FT NON_TER 1221
FT /evidence="ECO:0000313|EMBL:ODQ48544.1"
SQ SEQUENCE 1221 AA; 141003 MW; D84D86426FCED3D9 CRC64;
ELLSVFQQKL NSAVRLDNLA NTSINHLKFL NDEFQFLATT NGVCLDNKFA ENLKNDVNLL
NSKNSILEKI FKRHKQVESE SNLLNNLKSE VLNYLVDVQT EREGKKTSLA STAISNNAAA
GSKRRRKPTT KAEEMLDEAD MENEFAEIFE QPKKRRRRAG AAAAATTAAA SSASTSKSSA
ATATAGRSGA TKKSPDADEN TLESNDENDD QEGTTPKLSV KELKSLERQY DNTYLSIWKD
LSRKDSPKAY RLFQQTAQAK SINLRKTAQL AARESRKWQV KTTKAQKDQV TKARRSMREM
LNFWKKNERE ERNLRLKAEQ EALQRAKKEE EEREAKRQAR KLNFLINQTE LYSHFIGRKI
KTSEFEGDMG AEPIPGYGAG SASHKVANEA DVDMSLATKD FDNLNFDEEN EEALHKMAAA
NAQSALMEAK NKAHQFNDGI PRASDGDDDE KNEGEMNFQN PTSIGDITVE QPKLLNCTLK
EYQRKGLNWL ANLYEQGING ILADEMGLGK TVQSISVLAY LAETHDIWGP FLVVTPASTL
HNWQQEISNF VPNFNVLPYW GTAKDRKVLR KFWDRKNIIY NRNSPFHVVV TSYQLVVADS
AYFQKMKWQY MILDEAQAIK SSQSSRWRSL LSFQCRNRLL LTGTPIQNNM QELWALLHFI
MPSLFDSHDE FSEWFSKDIE AHAQSNSKLN EEQLRRLHAI LKPFMLRRIK KNVQSELGEK
IEIDVYCDLT NRQKKLYRML RSQINLMDLI ENNKRIGTNE DVESLMNVVM QFRKVCNHPD
LFERADTKSA FCFGDFPMTE SLIREVNEST LELNYNTKNL IKYKLPKTIL EECLLPSYEK
RSLTEKDSLI NRMFNVYQPR HYIHDDDSEL SILKFVNETP CEIEKIVSRN LVTNAINNKS
YIESTKDEQN RLYREIYCTD NKNSLIFSDS KDRVPSFLKN LTHDVSKSMY MRSFQPGYFE
TALASPIEIV CSKENFNVIK DDAFFNKTIR QALLPLDLNT QAELLEKQVW VKDWPKAEML
PVEDSNYKQG GTIRLPSMER FVLESAKLKK LDQMLVDLKK GDHKCLIYFQ MTKMMDLMEE
YLSYRQYKYI RLDGSSKLSD RRDLVNDWQS NPELFIFLLS TRAGGLGINL TAADTVIFYD
SDWNPTIDSQ AMDRAHRLGQ TRQVTVYRLL VRGTIEERMR DRAKQKEHVQ QVVMEGKVDA
VNEKEEKERE KKEMALWLLE D
//
