ID A0A498K507_MALDO Unreviewed; 1740 AA.
AC A0A498K507;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=ATP-dependent helicase ATRX {ECO:0000256|ARBA:ARBA00031106};
GN ORFNames=DVH24_030395 {ECO:0000313|EMBL:RXI02466.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXI02466.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXI02466.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXI02466.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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:RXI02466.1}.
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DR EMBL; RDQH01000330; RXI02466.1; -; Genomic_DNA.
DR STRING; 3750.A0A498K507; -.
DR EnsemblPlants; mRNA:MD04G0200200; mRNA:MD04G0200200; MD04G0200200.
DR Gramene; mRNA:MD04G0200200; mRNA:MD04G0200200; MD04G0200200.
DR Proteomes; UP000290289; Chromosome 4.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd11726; ADDz_ATRX; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
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; IPR025766; ADD.
DR InterPro; IPR044574; ARIP4-like.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45797:SF1; HELICASE ARIP4; 1.
DR PANTHER; PTHR45797; RAD54-LIKE; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51533; ADD; 1.
DR PROSITE; PS51473; GNK2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022895};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
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:UP000290289};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1740
FT /note="ATP-dependent helicase ATRX"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019850377"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 28..137
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 144..244
FT /note="Gnk2-homologous"
FT /evidence="ECO:0000259|PROSITE:PS51473"
FT DOMAIN 735..868
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1002..1185
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1386..1554
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 296..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 395..429
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 296..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1740 AA; 194613 MW; 24E26060ED691037 CRC64;
MDSTFLRFAS LLLLLSLASS ANPNSDYNSL VYKKCANQTF TTLSTKSQVQ QQTLSSFFQQ
LASHSSQSKF YKHAEASGDN NEAGISGLFQ CRQDISNEEC HTCVKTLRNL SNALCKESVS
ARVQLHGCYV HYELDGVDSI PSSHRLMQKT CGKDLANGVA AGFEKMRAAA FAALESGVAD
GGGFCQTSYE AVQVMAQCVG GLGGCACGEC VSRAVQTAEE ECGGAVSGQI YLEECFLSYS
YHPDGIPEDD HPHDRENKGG GNGGNGKKVA IVVGGAAALV FAFIFLLFVS TMEESHDQME
ENGEQVEESH EQVENIGSAS SGSDSDSFID DSEVDEEPLS DKEIEELIAE FLEVESKAAE
AQEALEKESL AKVESEVRKE LAQTLHGDNL EAAVAEEMDT LIEEWQAELD ELETESAHLL
EQLDGAGIEL PSLYKCIESQ APNGCCTEAW KRRIHWIGSQ ETGEFTKSRA DAEQYLQTHR
PVRRRHGKLL EDGASGFLQK KLAIDGSKDA VTADVDYWGS FNKLFSDGAT AGDALFGSKH
WASVYLASTP QQAAEMGLKF PGVDEVEEID DIDGNSGDPF VAAAVANERE LDLTEEQKKN
YRKVKEEDDV NVDRKLQIRL KRRRHRKRSK QDAGRKDFCL VDQEIGSNMD LSSSMLDSSI
SISNGKIDQD LETANNIDQE SITSNGSSPV TSSSEARGSK RLSEDEELNI DNKRSRTVII
DSDDDTPLKD NSDCNAIKSE DQSYVEENIC IAATGGLPSQ SLNDKLYCTA CSKHAVEVCS
HPLLKDPDCS ECYCGWCGQS KDLVNCKSCK TLVCATCIKR NIGEECLSDA QTSGWQCCFC
CPSLLKTLTS QLEQAISSQD LIVSSSDSDS DSSDSEIDVA ISSKRRRKKK IRRIIDDTEL
GEETRRKIAI EKERQERLMS LQVQFSAKSK MKSFATCNGR LPEGASAEVL GDASAGYIVN
VVREKGEEAV RIPPSISAKL KAHQITGVRF IWENIIQSVR KVKAGDKGLG CILAHMMGLG
KTFQVIAFLY TAMRSIDLGL NTALIVTPVN VLHNWRQEFM KWRPSELKPL RIFMLEDVSR
DRRAELLAKW RRKGGVFLIG YSAFRNLSFG KNVKDRQIAT EICHALQDGT DILVCDEAHV
IKNTRADVTQ ALKQVKCQRR IALTGSPLQN NLMEYYCMVD FVREGFLGSS HEFRNRFQNP
IEYGQHTNST VDDVKIMNQR SHILYEELKG FVQRMDMNVV KKDLPPKTVF VIAVKLSTLQ
RKLYKRFLVA HGFTKDKDYN EKIGKRSFFA GYQALAQIWN HPGILQLRKD DKDYERRGDA
VENFLADDSS SDENIDYNLG FGEKNVNEIL PGKKDDIFRK DWWNDLLHEN DYKELDYSGK
MVLLLDILAT SSDVGDKALV FSQSIPTLDL IELYLSRLPR HGNKGKFWKK GKDWYRLDGR
TEGSERQKLV ERFNDPLNKR VKCVIISTRA GSLGINLYAA NRVIIVDGSW NPTYDLQAIY
RAWRYGQTKP VFAYRLMAHG TMEEKIYKRQ VTKEGLAARV VDRQQVHRTI SKEEMLHLFE
FGDDENHVLD QDSVFLNDNV TGKVEILPKH VVPLSQGSCF SDKLMESLLG KHSPRWIANF
HEHETLLQEN EEEKLTKEEQ DMAWEVYRKS FGWEEVQRVP LNESAVDQKP AVSNTASSAP
TKSILAESTA KNAFVQRKCT NLSHLLTLRS QGTKQGCTTV CGECGRELSW EEHSRDSRLR
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