ID A0A3B3QJ52_9TELE Unreviewed; 2126 AA.
AC A0A3B3QJ52;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000005590.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000005590.1}
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 -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR Ensembl; ENSPKIT00000029597.1; ENSPKIP00000005590.1; ENSPKIG00000022151.1.
DR GeneTree; ENSGT00940000155902; -.
DR Proteomes; UP000261540; 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: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: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 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; 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; PTHR46357; TRANSCRIPTIONAL REGULATOR ATRX; 1.
DR PANTHER; PTHR46357:SF1; TRANSCRIPTIONAL REGULATOR ATRX; 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 3: Inferred from homology;
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 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 Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 148..285
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1238..1425
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1673..1851
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 45..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2107..2126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1964..2010
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 45..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..627
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..982
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2126 AA; 237755 MW; 068CD514FF0BEFA7 CRC64;
MNETVYNVLD LRDCSFFGCN LLTVFMCFFL LPGKMSKVST EANTIDNNME EPGSSAEVPK
PSSSRSKRKP SVVTKHTGLD ESDTSNDSGN ENAMPTHPSD CSLDMSSLPK GTVVVKPEPV
GNEAKDDFRG PEFRSRGAGK LKSDSTRKRG GEHMHGIVSC TACGQQVNHF QKDSIYQHPV
LKVLICKSCF KYYMSDDISK DADGMDEQCR WCAEGGNLIC CDFCSNAFCK KCILRNLGRK
ELSGIMDEDS QWYCYVCSPE PLLDLVTACN SVLQNLEHLW YQHRKRSKAE HEKSAREYGT
PKRTPKEKAA LNGREHGVDG LSSGTLTFSY KALKVPKELA KKTKKLIETT TGLNNTFVKF
IQQGSQDQGT NVVRLRHLKA FRSVLEDLKK AHSAMEVALE KEFRDLELQN GQEKAATLIS
QRQCMDGETE VADTSDNHVG EQDCVNNLAE AAGECCEDGR AGHTDSDVEM KGSPDSSPQK
VLEVPEESQA KEKGADSEKD TDCNEESASA GDASDDKDIV SVPVSVPDEL FEMMEAAADS
SGVAERNELI VTKSRKSSRS SATRGKSPDS AKGAPAKVTK SLVVKLTPVP LKGSPESSLE
IKEANTSEIE EPVASEQEAD GDVDGAQLQE EGSENRRSPR VKTTPLRKPA DSKSRPAQSQ
DNSASDTDNE GSAEVEAPQN GEENTAEWES KPKRAAASSS RADDSDSDEM PAVLLQTAAM
MRSSDVGESG DEVTPKSVRK CLFQINKKTS QSKERKATKR KLKHGSSDSD QGDKKSTSKK
AAKKMKEKGS DSSDSDLEKE IKSLSKLNTV KKRLLREKKK DDEESDGGKD EKPSANVAKE
RKRPEGAKRR PKAKSTARKS ASSSSEEDEG NEDSGDDSGD QQKIKPITEE VMAMATETFQ
QSSGDEAEIK PEPILMADED DDPENRIAKK MLLAQIKANY SSGEDSSSDN EDSEKEDKKK
NKKAGDEEEG GDEEENEASD SGSDSDVDVK KTRHRHRLLR HKLSLSEGES GDEKPAGKAK
KEGKRKARRK VSSDDTADSD FEESDGSAQS GATGMSEEVS ESDEGNRRKT RSSKKAGEEN
QRSYHQKKKR RRIKVQDDSS SNEKSGSGEE DGDKEDDAGD DDDDDESKST PKGRKKIRKI
LKDDKLRSET QNALKEEEER RKRIAEREQL REKLREVIVV EEASQVPCPI TTKLVLDEDE
ETKEPLVQVH RNLVTKLKPH QVDGVQFMWD CCCESVRKAK KAFGSGCILA HCMGLGKTLQ
VVTFLHTMLL CDKLNYSTSL VVCPLNTVLN WLNEFEKWQE GMKDEESLEV TELATVKRPQ
ERAYALQRWQ EEGGVMIIGY EMYRNLTQGR NIKSKKLKEI FHKTLVDPGP DFVICDEGHI
LKNETSAISK AMNSIKTRRR VVLTGTPLQN NLVEYHCMVS FIKENLLGSV KEFRNRFVNP
IQNGQCADST PVDVRVMKKR AHILYEMLAG CVQRRDYTAL TKFLPPKYEY VLAVRVTPIQ
CKLYRYYLEH FTGVGSALEG GRGRAGTKLF QDFQILSRIW THPWCLQLDY ISKENKGYFD
EDSMEEFIAS ETDESSMSLT SEDEKIKKKK RGKGKKASMD ESDSDDLEVI KEWNTSSRGG
NPEGRNRAEP VEEVRATSSS GPGSPSPDWH KDFVTEADAE ILDHSGKMVL LFEILRIAEE
LNDKVLVFSQ SLISLDLIED FLELACRAKE EEKPSLYKGD GKWFRNIDYY RLDGSTAATT
RKKWAEDFND TSNIRGRLFL ISTRAGSLGI NLVAANRVII FDASWNPSYD IQSIFRVYRF
GQLKPVFVYR FLAQGTMEEK IYDRQVTKQS LSFRVVDRQQ IERHFTMNEL TELYTFEPDQ
LDEPNSEKKS KRATPMLPKD PLLAELLHSF KEQIVGYHEH DSLLDHKEEE ALSEEDRKAA
WAEYEAEKKG LSLRVNQPSY NQMGMAAPNS YFPFNVAALA TMTNQQLEDL VNQGRQKVIE
ATNALKSLPR ESLDETMQRL RVENRSLTEA QVQSMALGHQ ASLELELKRR EAVYRDVLNK
QQTLMMYVQK VITNRKMQEQ QIAMANRANL LSQLALQNGM IGPGGLSQME LLGLYQQLGS
QLSHALQSVP STTTQLNKNP GPSKGN
//
