ID F6Q374_MONDO Unreviewed; 2362 AA.
AC F6Q374;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 84.
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};
GN Name=ATRX {ECO:0000313|Ensembl:ENSMODP00000027603.2};
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000027603.2, ECO:0000313|Proteomes:UP000002280};
RN [1] {ECO:0000313|Ensembl:ENSMODP00000027603.2, ECO:0000313|Proteomes:UP000002280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17495919; DOI=10.1038/nature05805;
RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT coding sequences.";
RL Nature 447:167-177(2007).
RN [2] {ECO:0000313|Ensembl:ENSMODP00000027603.2}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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; ENSMODT00000029142.3; ENSMODP00000027603.2; ENSMODG00000003920.4.
DR eggNOG; KOG1015; Eukaryota.
DR GeneTree; ENSGT00940000155902; -.
DR HOGENOM; CLU_000863_1_0_1; -.
DR TreeFam; TF313172; -.
DR Proteomes; UP000002280; Chromosome X.
DR Bgee; ENSMODG00000003920; Expressed in skeleton of lower jaw and 19 other cell types or tissues.
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: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; 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 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:UP000002280};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 158..295
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1529..1716
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1974..2154
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 22..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1861..1898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1930..1949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1155
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1930..1947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2362 AA; 268330 MW; EC3D7B660AB2179B CRC64;
MAALKPNESK LNTLVQKLHD FLAQSSEESE EAHSPPRLTM SKVIDKGSRS GNTSDPMEVI
REEGSTSSEK AKSLGPHRSK RKPTVVTKYV GSDEEKVFDD TLNPDVSIDT SETDIAMQSL
PKGTVVVQPE PVLNEDKDDF KGPEFRSRSK MKTESLKKRG EEGLHGIVSC TACGQQVNHF
QKDSIYRHPT LKVLICKNCY KYYMSDDISR DADGMDEQCR WCAEGGNLIC CDFCHNAFCK
KCILRNLGRK ELSAIMDENN QWYCYICRPE PLLDLVTACD SVFENLEQLL QQNKKKIKVE
SEKSNKLFEH SHKFSPKKNV STCNGEEKKV DDSHSGSVTY SFTALMVPKE IVKKTKKLVE
TTTSMNASFA RFLKQASENS EMSTVVKLRQ LKAFKSVLND IKKVHHSLEE GVNMEIRALD
TLNKETVTME HKADILKPET EVTKLEVYYE SKKKDFSKCD NKLSMKRVGS EMVGQSLPVV
GQPANKSAGA EDKKSNRKEA RFEPANTSEA LDMDIVSVPS SVPEDIFENP EAAMEVQVSS
ENQRDGNNAT ERDVEHSVKS KDHKGVKAAD CQEATQEKEE NKSSVTSKAE NRSSQKERSC
DEDFVENDIP LVSEEADLRR SPRVKTTPLR RQTEANPITS NSDEENNDVY NEKRKRKSLV
QSVKKDKRTS SDSAIDSPKP TKVPKCKPLD TVAPSSDSEE IPAVLKEVAM MSHSSSDTEQ
NETNENVPKK SLYDIKTQTS KGDKGKRKRK NSTSGSEFDT KKGKAVKSFT GSKKKRHSHS
ESSNYDSELE REIKNMCKIG AAKQSQKRHS NKEDYGSSED EKQNAKGSSK QKKKGTKTLI
NESSDDDGED RQKNSCFSED TVNKESMSSQ LREPVTKKDA ATSSDVHKSY VKEEVCSSPE
TCKEAEAIEQ SRHLKSKPMK KDSSFDDVTE KSSQKEECGD SSEDEKKQKK RRIETKEKKS
SELKKFPSQE NEVTSSDIIE KSLEREDSSH LTEDFDQNKQ GSAEAEKKNK KLREKNSKKK
EELSDDIEKL TGKSESGDYS EGKKGLSGRE RKKENLGEKS SKTVHYGSSS DVEKCLPKEE
CCDSSDEKRR KRIESRERRN LSAKINIKAK QSGSSSSEAE ESFSEDSKRK KKIPLTKNKK
KENVKDKKKK SPRRNGKKQQ EIISSSSDEL GDDDQNSTGE GSGDEQKIKP VTEDITLPSN
VHSSGDEADR RDPVNVDDDE DEDDPENRIA KKMLLEEIQA NITTDEDASS DEEPTKMKKR
SAKQNEENTG DESEPQKEHN VEHDEHGNSD TDSDSEQSKK PRYRHRLLRH KLSGSDGESG
EEKKSRPKET KETKRRNRRK VSSEDSVDTD FQESGVSEEV TESEDDQRPR TRSAKKAELE
ENQRSYKQKK KRRRIKVQED SSSENKSNSE EEDENDDSKS PGKGRKKIRK ILKDDKLRTE
TQNALKEEEE RRKRIAERER EREKLREVIE IEDASPIKCP ITTKLVLDED EETKEPLVQV
HRNMVTKLKP HQVDGVQFMW DCCCESVSKT KKSAGSGCIL AHCMGLGKTL QVVSFLHTVL
LCDKLDFSTA LVVCPLNTAL NWMNEFEKWQ DGLDDEEKLE VSELATVKRP QERSYMLQRW
QEDGGVMIIG YEMYRNLAQG RNVKSRKLKE IFNKALVDPG PDFVVCDEGH ILKNEASAVS
KAMNSIRSRR RIILTGTPLQ NNLIEYHCMV NFIKENLLGS IKEFRNRFIN PIQNGQCADS
TMVDVRVMKK RAHILYEMLA GCVQRKDYTA LTKFLPPKHE YVLAVRMTPI QCKLYQYYLD
HLTGVGNSSE GGRGKAGAKL FQDFQMLSRI WTHPWCLQLD YISKENKGYF DEDSMDEFIA
SDSDETSMSL SSDDYTKKKK SKGKKGKKDS SSSDSCSDND VEVIKVWNSR SRGGGDGSVE
EIPNISAVSF KQEESKTASS SNPSSPAPDW YKDFVTDADA EVLEHSGKMV LLFEILRMAE
ELGDKVLVFS QSLISLDLIE DFLELASREK SDDKDKPLIY KGEGKWFRNI DYYRLDGSTT
AQSRKKWAEE FNDETNVRGR LFIISTKAGS LGINLVAANR VIIFDASWNP SYDIQSIFRV
YRFGQNKPVY VYRFLAQGTM EDKIYDRQVT KQSLSFRVVD QQQVERHFTM NELTELYTFE
PDLLDDPNSE KKKKRDTPML PKDTILAELL QIHKEHIVGY HEHDSLLDHK EEEELTEEER
KAAWAEYEAE KKGLTMRFNM PTGTTLPPVN FNSQTPYIPF NLGALSTMSN QQLEDLINQG
REKVVEATNS VTAVRIQPLE DIISAVWKEN MNLTEAQVQA LALNRQASQE LDVKRREAIY
NDVLTKQQMV RVPQSLNCIL FH
//
