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Database: UniProt
Entry: A0A3B4BZ61_PYGNA
LinkDB: A0A3B4BZ61_PYGNA
Original site: A0A3B4BZ61_PYGNA 
ID   A0A3B4BZ61_PYGNA        Unreviewed;      1403 AA.
AC   A0A3B4BZ61;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000256|ARBA:ARBA00019805, ECO:0000256|RuleBase:RU368001};
DE            EC=3.6.4.- {ECO:0000256|RuleBase:RU368001};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000003806.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000003806.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   Ensembl; ENSPNAT00000008091.1; ENSPNAP00000003806.1; ENSPNAG00000010386.1.
DR   GeneTree; ENSGT00900000141110; -.
DR   OMA; DHRIMRS; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0031011; C:Ino80 complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        32..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          206..331
FT                   /note="DBINO"
FT                   /evidence="ECO:0000259|PROSITE:PS51413"
FT   DOMAIN          455..626
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1018..1173
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1193..1230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1271..1374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          287..317
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1271..1289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1305..1341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1403 AA;  160282 MW;  741E4A665BF39BC2 CRC64;
     MASEQDGMDS ACSKLAKPLH LQHLERSLRL DAFLLIQFFG NLFIYFGYIA QYITISPTEH
     KADKANLYNF SKLRKSRKWL KGILLSDDTT DSDTDSDDSD FSMTREELHD MLRLHKFTRL
     HQSKFHTDRE LQQYQYYSTG LLSTQDPFYE QQRHLLGPCL MLFYLSMEGR PYVTKIFAKF
     SHDAPPPITK KKHLTLEQLN ARRRKVWLTI AKKENPKAFK QKASAKNFVL TNAKKLAHQC
     MREVRRAAIQ AQKNCKETLP RARRLTKEML LYWKKYEKVE KEHRKRAEKE ALEQRKLDEE
     MREAKRQQRK LNFLITQTEL YAHFMGGKHN GGDSSQEEIL RKLDENTAQR QIDIGGGVMV
     NMGQEDYDSE YYKSQALRNA KEAYHIHQAR TRQFDEEAKD SRCASLHVAS VSGSGFGESY
     SLSNPSIQAG EDIPQPTIFN GKLKGYQLKG MNWLANLYEQ GINGILADEM GLGKTVQSIA
     LLAHLAERDN IWGPFLIISP ASTLNNWHQE FTRFVPKFKV LPYWGNPHDR KVIRKFWSQK
     TLYTQNAPFH VVITSYQLVV QDVKYFQRVK WQYMVLDEAQ ALKSSTSVRW KILLQFQCRN
     RLLLTGTPIQ NTMAELWALL HFIMPTLFDS HEEFNEWFSK DIESHAENKS AIDENQLSRL
     HMILKPFMLR RIKKDVENEL SDKIEILTYC QLTSRQRLLY QALKNKISIE DLLQSSMGTA
     QQAHSTTSSL MNLVMQFRKV CNHPDLFERQ ETRSPFHMSL KPFIMSKFLF RQGLLNTCSQ
     GRAKLLQVLL SPFSPQHIQQ SLFHRKSDDE GSCFSFLRFI DVSPAEMSNQ MLQGTLTRWL
     ALYLSFKSAH RLHHQRLWAE AEVCERKAEW SSVGHCLSNR DFVLWPDRPT SFPNTHSSTV
     LRVSHSGYHG ATRSPHSHYT DQPPKFILTV TAVPIERCCP DRSAEYEWRQ VRDGGSLAAK
     QCFLYGSPEL AYAWAARSHS FHPESPGGMM ALQPRHGWSF IRIPDKESLI TDSGKLHTLD
     LLLTRLKSQG HRVLIYSQMT RMIDLLEEYM VYRKHTYMRL DGSSKISERR DMVADFQSRT
     DIFVFLLSTR AGGLGINLTA ADTVIFYDSD WNPTVDQQAM DRAHRLGQTK QVTVYRLICK
     GTIEERILQR AKEKSEIQRM VISGGNFKPD TLKPKEVVSL LLDDEELEKK LRLRQEEKRQ
     QEESSKVKDR KRKREKYAEK RKKDDDVEAK KKKEGVNLVI PYAPSADNSN LSADGEDSFI
     SVDMDSAMPS PFSEISLSSE LQPGSLPADE SSSDMLVIVD EPVSSAPQSR ATNSPASGTG
     SVSDNMNGVS SQDTSSPGRG RSGRSRGRPK GSGGAGKCSS RKGRGRKSTA GSAAAIAGAM
     AGAAAASAAA YAAYGYSVSK GEF
//
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