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Database: UniProt
Entry: A0A3M0W0U7_9EURO
LinkDB: A0A3M0W0U7_9EURO
Original site: A0A3M0W0U7_9EURO 
ID   A0A3M0W0U7_9EURO        Unreviewed;      1119 AA.
AC   A0A3M0W0U7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   18-JUN-2025, entry version 29.
DE   RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=DV735_g4116 {ECO:0000313|EMBL:RMD41013.1};
OS   Chaetothyriales sp. CBS 134920.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales.
OX   NCBI_TaxID=2249417 {ECO:0000313|EMBL:RMD41013.1, ECO:0000313|Proteomes:UP000278137};
RN   [1] {ECO:0000313|EMBL:RMD41013.1, ECO:0000313|Proteomes:UP000278137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 134920 {ECO:0000313|EMBL:RMD41013.1,
RC   ECO:0000313|Proteomes:UP000278137};
RA   Moreno L.;
RT   "Genomic analysis of domatia-associated black yeasts (Chaetothyriales,
RT   Ascomycota).";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC       {ECO:0000256|ARBA:ARBA00009687}.
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:RMD41013.1}.
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DR   EMBL; QQSL01000056; RMD41013.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0W0U7; -.
DR   OrthoDB; 5857104at2759; -.
DR   Proteomes; UP000278137; Unassembled WGS sequence.
DR   GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
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:TreeGrafter.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:TreeGrafter.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; IEA:TreeGrafter.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   GO; GO:0034728; P:nucleosome organization; IEA:TreeGrafter.
DR   CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   FunFam; 3.40.50.10810:FF:000036; Chromatin remodelling complex ATPase chain; 1.
DR   FunFam; 3.40.50.300:FF:000082; ISWI chromatin remodeling complex ATPase ISW1; 1.
DR   FunFam; 1.20.5.1190:FF:000005; ISWI chromatin-remodeling complex ATPase ISW1; 1.
DR   FunFam; 1.10.10.60:FF:000234; ISWI chromatin-remodeling complex ATPase ISW2; 1.
DR   FunFam; 1.10.1040.30:FF:000003; ISWI chromatin-remodeling complex ATPase ISW2; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C-like.
DR   InterPro; IPR009057; Homeodomain-like_sf.
DR   InterPro; IPR044754; Isw1/2_DEXHc.
DR   InterPro; IPR015194; ISWI_HAND-dom.
DR   InterPro; IPR036306; ISWI_HAND-dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A MEMBER 5; 1.
DR   Pfam; PF09110; HAND; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278137}.
FT   DOMAIN          188..353
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          484..635
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          843..895
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1015..1119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..819
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1051
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1077..1110
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RMD41013.1"
FT   NON_TER         1119
FT                   /evidence="ECO:0000313|EMBL:RMD41013.1"
SQ   SEQUENCE   1119 AA;  128050 MW;  BD744C29CA91E9EE CRC64;
     MAPSKPKQTE SETSSNADTP MTDINDRPRR PHRPSFGRLN PYNDDTPDYT DSDTNANTTA
     SSIAGESPLG EGRRRRAEAL QLRKSILGKK HGQLGESKDD DSIRRFKYLL GLTDLFRHFI
     DTNPNPRIKE IMAEIDRQNA EEAAQQKKGL LRDEKRGAAS QTIFRESPAY IQGGQMRDYQ
     VAGLNWLISL HENGISGILA DEMGLGKTLQ TISFLGYLRH ICDIKGPHLI IVPKSTLDNW
     AREFKKWTPE VDVLVLQGSK QDRQDLINER IVEDKFDVLI TSYEMILREK AHLKKLAWEY
     IIVDEAHRIK NEESSLAQII RMFSSRNRLL ITGTPLQNNL HELWALLNFL LPDVFGDSEA
     FDSWFSNQDA DQDTVVQQLH KVLRPFLLRR VKADVEKSLL PKKEVNLYVG MSEMQVKWYQ
     KILEKDIDAV NGAGGKRESK TRLLNIVMQL RKCCNHPYLF EGAEPGPPYT TDEHLIYNSG
     KMLILDKILT RMKEQGSRVL IFSQMSRVLD ILEDYCVFRG HQYSRIDGAT AHEDRIAAID
     EYNAPGSEKF IFLLTTRAGG LGINLTSADI VILYDSDWNP QADLQAMDRA HRIGQTKQVR
     VFRFVTENAI EEKVLERAAQ KLRLDQVVIQ QGRAQQQAKQ AASKDELLNM IQHGAEKVFE
     TKGATGALDD IDAILARGEE RTAELNAKYE KLGIDDLQKF TSESAYEWNG EDFTNRKKDI
     GINWINPAKR ERKEQIYSID KYYKQALSTG SKPAETKPKI PRPPKQIHIH DWQFFPDGLA
     ELQERETAFY HKEIGYKAQL PDDDGERTLS DREGDRDLEQ TTIDNAEPLT EAEKQLKAEL
     QEQGFHNWNR RDFQQFINGS ARYGRDNFEG IALEVDSKNI DEIKQYAKAF WKNYKLIEDW
     EKHVRAIEAG EERLRKTEHQ RKMLRKKMQM YRVPLQQLKI NYTVSTTNKK VYTEEEDRFL
     LVMLDRHGLD AEDLYDKIRD DIRESPLFRF DWFFLSRTPI EIGRRCTTLL NTVTREFGDP
     DGPLTNGNHA TGKGRGRSRE DDDESEGDEE VEQPKKKKAK NGKDKENGVV NKKIKAVKSS
     AAAGSKGTSS SRSTSRAPSV SSAAATPTTK KGSKKKGHK
//
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