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Database: UniProt
Entry: A0A1I8N209_MUSDO
LinkDB: A0A1I8N209_MUSDO
Original site: A0A1I8N209_MUSDO 
ID   A0A1I8N209_MUSDO        Unreviewed;      1207 AA.
AC   A0A1I8N209;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   Name=101889225 {ECO:0000313|EnsemblMetazoa:MDOA010723-PB};
GN   Synonyms=LOC101889225 {ECO:0000313|RefSeq:XP_005178386.1};
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Musca.
OX   NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA010723-PB};
RN   [1] {ECO:0000313|EnsemblMetazoa:MDOA010723-PB}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA010723-PB};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_005178386.1}
RP   IDENTIFICATION.
RC   STRAIN=Aabys {ECO:0000313|RefSeq:XP_005178386.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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DR   RefSeq; XP_005178386.1; XM_005178329.3.
DR   EnsemblMetazoa; MDOA010723-RB; MDOA010723-PB; MDOA010723.
DR   GeneID; 101889225; -.
DR   VEuPathDB; VectorBase:MDOA010723; -.
DR   OrthoDB; 3269924at2759; -.
DR   Proteomes; UP000095301; Unassembled WGS sequence.
DR   Proteomes; UP000694905; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR   CDD; cd11726; ADDz_ATRX; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR025766; ADD.
DR   InterPro; IPR041430; ADD_ATRX.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46357; TRANSCRIPTIONAL REGULATOR ATRX; 1.
DR   PANTHER; PTHR46357:SF1; TRANSCRIPTIONAL REGULATOR ATRX; 1.
DR   Pfam; PF17981; ADD_ATRX; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS51533; ADD; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694905};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          51..189
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51533"
FT   REGION          227..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          900..1054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1095..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1130..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..667
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        900..945
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..1054
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1142..1189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1207 AA;  132945 MW;  4787693A3605C41B CRC64;
     MSEAMAAIAG GSSSLEMASP SNVADGSKAV SYEFHSSISE EEKRFYLKAY PTVDIVRDRK
     VHCTVCKTHI GTAPVQETGI KMHPILRVTH CLKCHDFYNS GEFSKGEDGS ELYCRWCGQG
     GEVYCCSSCP YVFCKSCIVK NLSRGVVADI EQNENWNCFS CAPKILWPLR AQHWALMNYI
     EQQKKEAYAM NLSEQELDQF LRRDRSKCCR LAKAKCGNMS DSMESLDSVL SKRSQGSSGS
     AKKAAKHGTT PSPQQPNAKR PKNNDEVVCT PDLLSMLEPD CQITVSQKNN GGTPQRPLST
     QSGPSPRIIS IQQSPNSFGG QSVSSSTPKT SAPPPLLLRN TAIKLRPATQ PPIVRRTVIG
     PRAPAPGGNT APVYHTINGY RIDLNSAAQQ ETFRLPNGKL IQVKRQGPPP GSNQAPTTNW
     QQMSQQQQQQ RVVPQTIASR PVQITAHPYP GPNAIQTPGQ PQVVRYHNNV IGSTTINAIA
     HNGTPLQAIN GQIPAQAQVV PNAPQMAPGQ PIRPVMVRHI FPDTPIGQAR TQLQEQVFNA
     MEICTHLTNK VQTLTNSNAY KQAKNYLEVK ELYIHLSYLL TYAIGRFKGL QDKCLADMRH
     LGFGNDADCL ENGQLAADKQ ASDDEDNEIE IVEPKTDLIT LDSDDDEPTP TPTATPTAAS
     KPTQTQPLIK IQKSIPATPP TSTTIAQSRV VITPLLLNQQ KTPSASNNIM SARGTYVPPT
     AAKITPIKVG HSPAPMPLPP LVPVTTATTP TPTPPKGVPS EEEDNMDLMS MAQSFLASML
     EVDVNDGSSL SSCDSTPHKK KQPRKKLTSK PNPTLIKQKA IMELERLEEM KRNDQKLKMK
     CKVELSRAED EYPFVKNLLE AKKKNEEDMK VKSSPDGTTM MVNTGQETVE VHLVIEDDLL
     NSSLEEKSSK EEENGNREKT KNEEHKRKEI TETNLEDEDG NGKKNTAMEV FEISDDVLAD
     AKENSSESLR QKEAKTTIEE EKSIDEKAIE SSSKEPKENS EEFSVTETIE KLVKSKESVV
     ETSEESKMEV DASPEEQSQR CEEETPAKIA ADSDDVDVYK EIAKVLQRKS SVEEQQQETE
     DTVQEKITAA VANTMTTTEQ NAENNDNLTQ GDTEKDSNIE KCIDSAIEEV TDDILQKPST
     PLVDETMESD DIQTDINQTP TTTREAEISC IDATSKEQNT AYPSVTEETQ PVTEEKEQQK
     STSNGNV
//
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