ID A0A1W4WN36_AGRPL Unreviewed; 2035 AA.
AC A0A1W4WN36;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ATP-dependent helicase ATRX {ECO:0000256|ARBA:ARBA00031106};
GN Name=LOC108734396 {ECO:0000313|RefSeq:XP_018321455.1};
OS Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018321455.1};
RN [1] {ECO:0000313|RefSeq:XP_018321455.1}
RP IDENTIFICATION.
RC TISSUE=Entire body {ECO:0000313|RefSeq:XP_018321455.1};
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: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_018321455.1; XM_018465953.2.
DR EnsemblMetazoa; XM_018465953.2; XP_018321455.1; LOC108734396.
DR GeneID; 108734396; -.
DR OrthoDB; 12329at2759; -.
DR Proteomes; UP000192223; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
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 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; cd18007; DEXHc_ATRX-like; 1.
DR CDD; cd18793; SF2_C_SNF; 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; IPR025766; ADD.
DR InterPro; IPR041430; ADD_ATRX.
DR InterPro; IPR044574; ARIP4-like.
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 InterPro; IPR011011; Znf_FYVE_PHD.
DR PANTHER; PTHR45797; RAD54-LIKE; 1.
DR PANTHER; PTHR45797:SF3; RAD54-LIKE; 1.
DR Pfam; PF17981; ADD_ATRX; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51533; ADD; 1.
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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
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:UP000192223};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 15..141
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1162..1350
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1526..1694
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 283..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..1931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2035 AA; 233427 MW; 98F63CC16E86B653 CRC64;
MTTSKQETNF RMYYDIDKES IRNELYCTIC GISIKLGQKV EEHPVLKVAV CKPCLLEYNA
ADFNKNDLCV WCGEKNNTLR RCFMCKTGFC KKCLSHNLDD KGKWEGKWFC LKCDTEPIWP
LRNIFVKADL CSRKQRSLSQ EKILPNEQPL RRLKRSKSVG CALSLKGDSL ANQISKETMK
NLKKTNYQTL QDFLRIIAKD MILLFNECNK SVDDFKLDVF QPYTTKISQI ISWFSYLCFF
IDSVNDNLNH LRTKILKESV ECKNYDGILL LSDYRMKLKK NGKKVDTSPD SMVLPFSSSS
QSSQDDLYPL QSTSQVKKNS PKNFRLSLKN RRIIYSSDES SDEVESSTTH KKTFEEIQEK
KKNSKQQSPD AQEKAENKLR DMEAKDEAAI LKELEDSNKK REENKQGSSC SESTEIYSHD
FLTARDSSAQ FVDSEETIVR PSVADIAGVE AQAVAKHAET EKGQNENGVN SNNLETNTNE
GELIINVGDH EGEIKDKKQV LNENKDDEIN EGAELSEKNS DLKLDANYVE EKIDVEEEKP
RKIDSITDDE VFIQENSMQE VKDEDNVEEQ INKILNTVSE YTNYINPSNV DVKEEYNYST
DELEDLLSES DENEKDMSTN VDEEKLKKAF THLQNDNFMT DVNITSESSL DVSSDDSFSD
SDGLNAVCSS KEQEKVLGRI VSLPLQELIV QNNSLNDSRE GDNVVEEETG GTSTDNTPDI
LPATSLSNEQ DEKIVNEKSS DKPFVPKSCC VLLDRLPKDF VLNKLREMKM DKERDIEDAE
LKKLLNLKTL DRKRRHSSSD EENQKKRQRN SVYSPKITQQ KDTSSSSEDD QFYEDSDEEG
HNVSDKIEEI KKNSETQDNQ GLHILDEIAI RHKASNFLSS DSEDDSDAYD DEEEEENEKK
KTFKKKLEKD KEKESEKDKT KEKTKSTSWR SDPLLRQRFE ISLDSEDSDT GEEKKSKSVS
KKKQELVETI EDDLDIEMPQ RQRKRKKSYS SSFTDDDKDI KTELSDDFQM PASFNSNKTI
ILLSSSDSDI EFITDSPIRN KAKSRKKNKS ESENDEDSLR KKGRKNIREI LSDDVLEEDT
KKAIEEEKQR NIRVSQKQQL MSNFLSQSSE NLEEEGLILD VDSETQKPLI VVNHNLSKRL
KNHQSEGVKF MWSSCYESVE QIKQDNKGSG CILAHCMGLG KTFQVITLIH TLFKYQKETR
TKCVLVVCPL STVLNWENEF KIAFNIASNS KRPIVYILGD QQNSTFSKAS RIKRWHDQGG
ILVMGYEAYS SALKTIRYSQ NTHDKINAAL VDPGPDLVIL DEGHLLKNGK TSRTITLMQI
KTKRRIILTG TPMQNNLKEY YHMVNFVKPN LLGSWLEYSN QFVNPIVNGQ YDDSTEEDVR
KMKYRSHVLN KKLKRTIQRF EVSELETYLP PKLDYVLFVQ LHPVQVQLYQ AFLENLNVDV
IQAGRLFAHY HYLQNVWSHP YLLVLQDKMK NMTKDKNIKE IDTIDLDPEI TMVEQKPIAT
NWWSRIIPKD VGTNIEYGSK FYIMLSIIEE AISCGDKIVV FSNSLNELDG IEHFLKLVGT
PSCKVWRNKI DYYRMDGTIK PDSRMSLCMS FNNPKNTQTK VFLVSHKVGG LGLNLVAANR
VILMDVNWNP SYESQSIFRT YRFGQKKTCY VYRLVSMGTM EEVVYERSVT KLAVAGRVVD
ERQISRHYKS DDLQKMYRAN FDLNQLRPNL NVPEDVVLGK VYQKHTKELF KYHSHQALLE
NLPHESLTEE EMERAWLEFG RENEAARKLE ISKQFIENAK KNSVDIRYQK NIETINALAE
DVANKGPLLN STIMRNGNFL NIPNTSMSAS LVPAACRAFA KENLNNFISS QKTLTQTLPL
ISNVSSASRN SSTQVGQFEE VFVPTRFGDV DANENRDNDV IVLEDNSWYN PSPASVDNNK
SSEYSKTDGR IKASEQVPNK NRFPPSNRIN INLLRKPAST RLVPRATNTM ISQEVIDVEN
HSLLAKLAKN HDISVSQILK PKIPEVDDQT DKGNTSNNCD NVVETSNVFY ATFLV
//
