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Database: UniProt
Entry: A0A427XZG0_9TREE
LinkDB: A0A427XZG0_9TREE
Original site: A0A427XZG0_9TREE 
ID   A0A427XZG0_9TREE        Unreviewed;       461 AA.
AC   A0A427XZG0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=RuvB-like helicase {ECO:0000256|RuleBase:RU363048};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU363048};
GN   Name=RVB2 {ECO:0000313|EMBL:RSH84276.1};
GN   ORFNames=EHS24_005791 {ECO:0000313|EMBL:RSH84276.1};
OS   Apiotrichum porosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Apiotrichum.
OX   NCBI_TaxID=105984 {ECO:0000313|EMBL:RSH84276.1, ECO:0000313|Proteomes:UP000279236};
RN   [1] {ECO:0000313|EMBL:RSH84276.1, ECO:0000313|Proteomes:UP000279236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27194 {ECO:0000313|EMBL:RSH84276.1,
RC   ECO:0000313|Proteomes:UP000279236};
RA   Aliyu H., Gorte O., Ochsenreither K.;
RT   "Genome sequence of Apiotrichum porosum DSM 27194.";
RL   Submitted (NOV-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   -!- FUNCTION: DNA helicase which participates in several chromatin
CC       remodeling complexes, including the SWR1 and the INO80 complexes. The
CC       SWR1 complex mediates the ATP-dependent exchange of histone H2A for the
CC       H2A variant HZT1 leading to transcriptional regulation of selected
CC       genes by chromatin remodeling. The INO80 complex remodels chromatin by
CC       shifting nucleosomes and is involved in DNA repair. Also involved in
CC       pre-rRNA processing. {ECO:0000256|ARBA:ARBA00025345}.
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|ARBA:ARBA00004123,
CC       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:RSH84276.1}.
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DR   EMBL; RSCE01000003; RSH84276.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A427XZG0; -.
DR   STRING; 105984.A0A427XZG0; -.
DR   OrthoDB; 5479950at2759; -.
DR   Proteomes; UP000279236; 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:SF2; RUVB-LIKE 2; 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   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:UP000279236};
KW   Transcription {ECO:0000256|RuleBase:RU363048};
KW   Transcription regulation {ECO:0000256|RuleBase:RU363048}.
FT   DOMAIN          57..348
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   461 AA;  50484 MW;  76C307E32B943653 CRC64;
     MKDVTKMERI GPHSHIHGLG LDANLEPRGN SQGMIGQGKA RKAAGVILKM VQEGRIAGRA
     ILIAGPPSTG KTAIAMGMAQ TLGSDVPFVN LVGSEVFSLE MSKTEALTQA FRRAIGVRIK
     EETELIEGEV VEIQVDRSVT GATKTGRLTL KTTDMETVYD LGSKMIDQLQ KEKVLAGDVI
     SIDKTSGRIS KLGRSFGRAK DYDAMGADTR FVACPDGELQ TRKEVVHTVS LHEIDVINSR
     TQGFLALFAG DTGEIKPELR DQINEKVAEW REEGKAEIVP GVLFIDEVHM LDIECFSFLN
     RALESEMAPL VVMASNRGIT RIRGTKYKSP HGIPGDLLDR MLIISTSKYS EDEIKEIVKI
     RGDEEDVKLG PDSLELLATM GGQTSLRYAL NLIAPSQQIA IRRKNTQVEV DDIRLAYKYF
     LDVDRSASYA RETSGMMFGE EEDVVTVTTA QNGSMAMDTS A
//
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