ID A0A3B3D8I8_ORYME Unreviewed; 2060 AA.
AC A0A3B3D8I8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE AltName: Full=ATP-dependent helicase ATRX {ECO:0000256|ARBA:ARBA00031106};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000025814.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000025814.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSOMET00000006167.1; ENSOMEP00000025814.1; ENSOMEG00000007314.1.
DR GeneTree; ENSGT00940000155902; -.
DR OMA; QEMGGVM; -.
DR Proteomes; UP000261560; 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; cd11726; ADDz_ATRX; 1.
DR CDD; cd18068; DEXHc_ATRX; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 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; 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45797:SF1; HELICASE ARIP4; 1.
DR PANTHER; PTHR45797; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 72..209
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1180..1367
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1616..1796
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1089..1117
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 25..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..936
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..998
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2060 AA; 232328 MW; 843A459483095F96 CRC64;
MTTAGSRKPT SVAKHTEENE SAPSAESDNE GATSDNPSEG NTSSRSKGTL VMRPTGNENK
GAMKLRVDFK QKLSDDALQK KVSCTACGKQ VNQFQRNSLC EHPALKVLIC KSCYNYYTSD
DIGKDSDGMD EQCRWCAEGG KLICCDYCNN AFCKKCILRN LGRKELSNIT DENSKWHCYV
CRSDPLQDLV FKCRRIMEKL EHAQLKQHKA EKREERDKKK KKSRTTKEHK ALANGKEHAE
GSGVMTFSYK KMEIPKEYIK KAKRLVETTT GLNNTFIQFI QQTAEDQGDR SIRYRHLKAF
KAVLSDLRKA HNVLEAALEP EFKSMELQNG NDVQHVKKSS STAEPTGIDK MDADADSGDG
VDAAPKSDTE PHNEADAIPE MDVNEEPQDE TGSARDSGVN LKADENQDWG GGLQSGMSED
EEKETNEEAS AVQDAVVSKD EEQTNEQEAG SEEVSSKAVM KDHQTETDAL EKIIKTETCE
EPVSTGEMSL DQDIMSVPPS VPEELFQMVE SLADSSTLSK PDTNSVPANE AKSNSTPAED
QLPQPKVKNL IVKLTPVPVV KTSGSRSSRS KSKEKSEESK SKKKTEDDDQ SASKVKKETE
SPPPSRRSSR LKTTPLRKQS EKKVDGDSSE SEEDVKSKSK PSKKSSDHAK KLDKDNNTPA
QTIEDSDSDE IPHALLEKAA ESKSTDEEQE STKGKKGSIK SDDSSQNTEN LSKRKRKTAT
SESDTENKSQ KPSKKKKQKD SDCSDSDSDQ KKGTSKVSKR RSSRTKKNKA KEEEKKDSPE
SKTATRKRSY EKKRKGKSPK GSSQLQSSSS EEEEEEQAEG DSGDDSDAQK IKPIMDDNVI
NSVGIFQQSS GDEIDNKDSV NPVCAEDDDD DPENRIAKKM LLAQIKSHYS SGAESSSEEE
EKEEKSSKKV KKDKQDEEDE DDEEEDEDDD EGTEDSDSDV EVKKSVKRHK LLRHKLSMSE
GESGDGKEEG KKKKKRKEGK KKSRSTSDSD DSSDSDFKKS DSSSGSALSE EVSGSEDDGK
RRKTRSSKKK DDEKQRSYKQ QKKKRRRIKV QDSSSSNEKS GGEDDDDQDG EGRKGRKKIR
KILKDDNLRT ETRDALKEEE ERRKRIAERE ALREKLREVI VVEEASKVTC PVTTKLVLDE
DEETKEPLVQ VHRNLVTKLK PHQVDGVQFM WDCCCESVKK IQKSPGSGCI LAHCMGLGKT
LQVVTFLHTL LLCEKLDFAT ALVVCPLNTV LNWLNEFEKW QYGLKDEESL EVTELATVKR
PQERAYALQT WHESGGVMIM GYEMYRNLTQ GRNIKSKKLK ETLRKTLVDP GPDLVICDEG
HILKNEASAV SKAMNAIRTK RRIVLTGTPL QNNLIEYHCM VNFIKENLLG SVKEFRNRFI
NPIQNGQCAD STLHDVRIMK KRAHILYEML AGCVQRKDYT ALTKFLPPKH EYVLSVRMTP
LQCKLYRHYL EHFTGVGNAL EGGRGRAGTK LFQDFQMLSR IWTHPWCLHL DYISKENRGF
FDEDSMDDFV VSETDESSMS LSSENEKPKK KKNQGKGKKK ESEESDSDDV EVIKEWNSSS
RGRNGEGRNR REPVEEPQPS GAEPGSPRSA DWHKEFVTEA DADILAHSGK LTLLFEILRM
AEEVEDKVLV FSQSLISLDL IEDFLELSCK DEDDEDAKPS PYKGEGKWYR NIDYYRLDGS
TNAVARKKWA EEFNDTSNTR GRLFLISTRA GSLGINLVAA NRVVIFDASW NPSYDIQSIF
RVYRFGQIKP VYVYRFLAQG TMEEKIYERQ VTKQSLSFRV VDQQQIERHF TMNELTELYS
FEPDMLDDPS EKKSKKATPV LPKDPLLAEM LQNNKDQLVC YHEHDSLLDH KEEEALSEED
RKAAWAEYEA EKKGLSMRTN YQSPYSQMDM GNPNYVSYNM AALASMTNQQ LEDLINQGRQ
KVIEATNALK TLPRESLEDI IAEVWKENPA LTEVQVQSIA LGRQATVEME LKRREAVYRD
VLTKQQTLMM YVQKLITNRK VQEQQLAMAN QATYLNQLAM QNGMMGAGLS QMDLLGLYQQ
LHGMGAHQGV GKNPGPSKGL
//
