ID A0A2Y9R1E3_TRIMA Unreviewed; 2480 AA.
AC A0A2Y9R1E3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Transcriptional regulator ATRX {ECO:0000256|ARBA:ARBA00016932};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE AltName: Full=ATP-dependent helicase ATRX {ECO:0000256|ARBA:ARBA00031106};
DE AltName: Full=X-linked nuclear protein {ECO:0000256|ARBA:ARBA00043074};
GN Name=LOC101348181 {ECO:0000313|RefSeq:XP_023589395.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023589395.1};
RN [1] {ECO:0000313|RefSeq:XP_023589395.1}
RP IDENTIFICATION.
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}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR RefSeq; XP_023589395.1; XM_023733627.1.
DR Proteomes; UP000248480; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 149..286
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1568..1755
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 2013..2193
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1900..1988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2450..2480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..430
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 15..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..1136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1185
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1929..1943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1957..1986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2480 AA; 281047 MW; B227B23E38E71642 CRC64;
MTAEPMRDNP DDPELSTSGV ITSTNKMPTC NSSSWNESKL NTLVQKLHDF LAHSSEESEE
TGSPPRSAIN QNTDKISGAG TNSDMMENSK EEGTSSSEKS KSSGSSRSKR KPSVVTKYVE
SDDEKPLDET VNEDASNENS ENDITMQSLP KEDGLHGIVS CTACGQQVNH FQKDSIYRHP
SLQVLICKNC FKYYMSDDIS RDSDGMDEQC RWCAEGGNLI CCDFCHNAFC KKCILRNLGR
KELSTIMDEN NQWYCYICHP EPLLDLVTAC NSVFENLEQL LQQNKKKIKV DNEKSNKVYD
HTPRFSPKKN SSNCNGEEKK LDDPCSGSIT YSYSALIVPK EMIKKAKKLI ETTANMNSSY
VKFLKQATDN SEITSATKLR QLKAFKSVLA DIKKAHVALE EDLNSEIRAL DAVNKEKNTK
EHKVIDAKSE TKVRKGEKSC ALERKDISKS EGKLSRKQTD SEYMDQSVPT EEQRANKSTS
GEHKKCGRKE EPQYEPANTS EDLDMDIVSV PSSVPEDIFE NLETAMEVQG SADYQGDSNS
GTEQELESSV KLNISSKDNR GGIKSKTSAK VTKELYVKLT PVSLSNSPVK GADCQEVSQD
KDGYKSSDLN PKSENCGPVQ ESSDNEHLVE NEGPLLLEES DLRRSPRVKT TPLRRQTELN
PATSNSDEES SETVKEKQKL SVPLRKKDKR NSSDSAIDNP KPNKLPKSKQ SEIVDQNSDF
DEMLAILKEV SRMSHSSSSE SDINEAHTNH EKTLFDLKTQ TEKDDKGKRK RKSSTSGSDF
DTKKGKSTKS SIISKKKRQN QSESSNYDSE LEKEIQSMSK IGAARTTRKR VPNKEDYDSS
EEEKHNKKGM ANQREKSLKT AREKSSDNVE RKQEREKFFS AEGTVDKDKT IMELRDGLSK
KQQPSVSSDG TDKPSSRRGE GFNSPEDKKV AETKEKSKHL KTKMCMKVQG GLSGVAEKFP
KKEQTDESSG DDKKQGKKGT EEKENKTTNL KKKVIKMEQH YDSSSDDNEK LPEGEEICHF
PKDIKQNKND TTDGEKKSKK IKEKISKKKN ELSDNAEKLP GKGDSYDSSE DKKSRNGASD
REKKRCNLPE KSSRRRQDCS SSDTEKYYLK EDGCDSSDKR LKRTELRERR NLNSKRSTKE
IQSGSSSSDA EESCSEDNKK QKKQRPTAKK KTNNVKEKKR NSLRTSTKRK QAEITSSSSD
IGDDDQNSVG DGSSDEQKIK PVTENLVLSS HTGFCQSSGD EALSKSVPLT VDDDDDDNDP
ENRIAKKMLL EEIKANLSSD EDGSSDDEPE EGKKRTGKQN EENPGDEEAK SQLNSDSDSD
SEESKKPRYR HRLLRHKLTM SDGESGEEKK MKPKEHKEAK GRNRRKVSSD DSEDSDFQES
GVSEEVSESE DEQRPRTRSA KKAELEENQR SYKQKKKRRR IKVQEDSSSE NKSNSGEEEK
EEEEEEEEEE DDENDDSKSP GKGRKKIRKI LKDDKLRTET QNALKEEEER RKRIAERERE
REKLREVIEI EDASPTKCPI TTKLVLDEDE ETKEPLVQVH RNMVIKLKPH QVDGVQFMWD
CCCESVKKTK KSPGSGCILA HCMGLGKTLQ VVSFLHTVLL CDKLDFSTAL VVCPLNTALN
WMNEFEKWQE GLNDDEKLEV SELATVKRPQ ERSYMLQRWQ EDGGVMIIGY EMYRNLAQGR
NVKSRKLKEI FNKALVDPGP DFVVCDEGHI LKNEASAVSK AMNSIRSRRR IILTGTPLQN
NLIEYHCMVN FIKENLLGSI KEFRNRFINP IQNGQCADST MVDVRVMKKR AHILYEMLAG
CVQRKDYTAL TKFLPPKHEY VLAVRMTPIQ CKLYQYYLDH LTGVGNSSEG GRGKAGAKLF
QDFQMLSRIW THPWCLQLDY ISKENKGYFD EDSMDEFIAS DSDETSMSLS SDDYTKKKKT
KGKKGKKDSS SSGSGSDNDV EVIKVWNSRS RGGGEGNVDE TGNNPSVSLK LEESKATSSS
NPSSPAPDWY KDFVTDADAE VLEHSGKMVL LFEILRMAEE IGDKVLVFSQ SLISLDLIED
FLELASREKT EDKDKPLIYK GEGKWLRNID YYRLDGSTTA QSRKKWAEEF NDETNVRGRL
FIISTKAGSL GINLVAANRV IIFDASWNPS YDIQSIFRVY RFGQTKPVYV YRFLAQGTME
DKIYDRQVTK QSLSFRVVDQ QQVERHFTMN ELTELYTFEP DLLDDPNSEK KKKRDTPMLP
KDTILAELLQ IHKEHIVGYH EHDSLLDHKE EEELTEEERK AAWAEYEAEK KGLTMRFNIP
TGTNLPPVSF NSQTPYIPFN LGALSAMSNQ QLEDLINQGR EKVVEATNSV TAVRIQPLED
IISAVWKENM NLSEAQVQAL ALSRQASQEL DVKRREAIYN DVLTKQQMLI SCVQRILMNR
RLQQQYNQQQ QQQMTYQQAT LGHLMMPKPP NLIMNPSNYQ QIDMRGMYQS VAGGMQPPPL
QRAPPPMRSK NPGPSQGKSM
//
