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Database: UniProt
Entry: A0A446BDD4_9PEZI
LinkDB: A0A446BDD4_9PEZI
Original site: A0A446BDD4_9PEZI 
ID   A0A446BDD4_9PEZI        Unreviewed;       458 AA.
AC   A0A446BDD4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   08-NOV-2023, entry version 16.
DE   RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
GN   ORFNames=TT172_LOCUS2931 {ECO:0000313|EMBL:SPQ20512.1};
OS   Thermothielavioides terrestris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX   NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ20512.1, ECO:0000313|Proteomes:UP000289323};
RN   [1] {ECO:0000313|EMBL:SPQ20512.1, ECO:0000313|Proteomes:UP000289323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Huttner S., Dainat J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA helicase participates in several chromatin remodeling
CC       complexes, including the SWR1 and the INO80 complexes.
CC       {ECO:0000256|RuleBase:RU363048}.
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; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665,
CC         ECO:0000256|RuleBase:RU363048};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU363048}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000256|ARBA:ARBA00007519,
CC       ECO:0000256|RuleBase:RU363048}.
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DR   EMBL; OUUZ01000004; SPQ20512.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A446BDD4; -.
DR   Proteomes; UP000289323; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.50.360; RuvB-like helicase, domain II; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR027238; RuvB-like.
DR   InterPro; IPR041048; RuvB-like_C.
DR   InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR   InterPro; IPR010339; TIP49_P-loop.
DR   PANTHER; PTHR11093:SF6; RUVB-LIKE 1; 1.
DR   PANTHER; PTHR11093; RUVB-RELATED REPTIN AND PONTIN; 1.
DR   Pfam; PF06068; TIP49; 1.
DR   Pfam; PF17856; TIP49_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363048};
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|RuleBase:RU363048};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU363048};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU363048};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363048};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363048};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363048};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU363048};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU363048};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU363048}.
FT   DOMAIN          63..352
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   458 AA;  49722 MW;  E7D6B7D227D63173 CRC64;
     MVQISEVRGN SRDNRTAAHT HIKGLGLNSS GIAEKQAAGF VGQTAAREAC GVVVDLIKAH
     KMAGRGVLLA GGPGTGKTAL ALAISQELGT KIPFCPITGS EIYSTEVKKT EVLMENFRRA
     IGLKVRETKD VYEGEVTELT PEEAENPLGG YGKTISTLLI GLKSARGQKK LRLDPSIYEA
     IQKERVQVGD VIYIETNTGA CKRVGRSDAY ATEFDLEAEE YVPIPKGEVH KKKEIVQDVS
     LHDLDVANAR PQGGQDIMSM MGQLMKPKMT EITDKLRSEI NKVVSKYINQ GVAELVPGVL
     FIDEAHMLDV ECFTYLNKAL ESPISPIVVL ASNRGMATIR GADDLVAAHG IPPDFLARLL
     IIPTHPYEPD EIKRIVRIRA STEGVQVTDA AIDKIAEHGV RISLRYCLQL LTPASILARV
     NGRSQIDVQD VAECEDLFLD ARRSANILAS ESGQGFIS
//
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