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Database: UniProt
Entry: A0A317SAX5_9PEZI
LinkDB: A0A317SAX5_9PEZI
Original site: A0A317SAX5_9PEZI 
ID   A0A317SAX5_9PEZI        Unreviewed;       458 AA.
AC   A0A317SAX5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   08-NOV-2023, entry version 18.
DE   RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
GN   ORFNames=C7212DRAFT_355030 {ECO:0000313|EMBL:PWW71689.1};
OS   Tuber magnatum (white Piedmont truffle).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Tuber.
OX   NCBI_TaxID=42249 {ECO:0000313|EMBL:PWW71689.1, ECO:0000313|Proteomes:UP000246991};
RN   [1] {ECO:0000313|EMBL:PWW71689.1, ECO:0000313|Proteomes:UP000246991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=091103-1 {ECO:0000313|EMBL:PWW71689.1};
RA   Murat C., Payen T., Noel B., Kuo A., Martin F.M.;
RT   "Genomes of Pezizomycetes fungi and the evolution of truffles.";
RL   Submitted (MAR-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWW71689.1}.
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DR   EMBL; PYWC01000149; PWW71689.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317SAX5; -.
DR   STRING; 42249.A0A317SAX5; -.
DR   Proteomes; UP000246991; 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   Reference proteome {ECO:0000313|Proteomes:UP000246991};
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          64..367
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   458 AA;  49888 MW;  E5E470CDA7964B1C CRC64;
     MVTISEVKSG NSRENRTAAH THIKGLGLRS DGTAEKVAAG FVGQESAREA CGVVVDLIKA
     KKMSGRAVLL AGGPGTGKTA LALAVSQELG TKVPFRPIVG SEIYSAEVKK TEALMENFRR
     AIGLRIKETK EVYEGEVTDL TPEEAENPLG GYGKTISHVI VGLKSGKGTK KLRLDPSIYE
     SIQKERVAVG DVIYIEANTG AVKRVGRSDA YATEFDLEAE EYVPIPKGDV HKKKEIVQDV
     TLHDLDVANA KPQGGQDIMS MMGQLMKPKK TEITDKLRTE INKVVEKYID QGVAELVPGV
     LFIDEVHILD IECFTFLNRA LESKISPIVI LASNRGVCTI RGTEDIMSAH GIPADLLGRL
     LIVPTYPYDL DDIRVIIRIR TKIESLDLED AAVEKLAHRG VDTSLRYALQ LLTPASILAK
     VSGRTKIQVA DVQECEELFI DTKKSAEIVS ELGRSFIS
//
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