ID A0A3Q4H5H8_NEOBR Unreviewed; 1922 AA.
AC A0A3Q4H5H8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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 Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000016971.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000016971.1}
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}.
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 STRING; 32507.ENSNBRP00000016971; -.
DR Ensembl; ENSNBRT00000017428.1; ENSNBRP00000016971.1; ENSNBRG00000013037.1.
DR GeneTree; ENSGT00940000155902; -.
DR OMA; QEMGGVM; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000013037; Expressed in testis and 8 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: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 Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 64..200
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1048..1235
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1482..1657
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 958..986
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1769..1796
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 195..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..945
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1922 AA; 216936 MW; CD3DC632CC514150 CRC64;
PGSSAETMKP SSSRNKKPTS VAKHTDQNGS ESSAESEGAT SDNPSDNNTG SVSKTLVMRP
AGNENKGDAL QKKVNCTACG KQVNQFQRNS VFVHPVLKVL ICKSCYKYYT SDDISRDSDG
MDEQCWCAEG GKLICCDYCN NAFCKKCILR NLGRKELSGI TDENSKWHCY VCRSEPLQDL
VSKCSRIMEK QQLKQKKTEK TEERESKKHK NKAAKEHKAV VNGKEHTEDS GTMTFSYRKL
HIPKELVKKA KKLVETTTGL NNTFIQFIQQ EAEDQGDRPI RYRHLKAFKA VLSDLRKAHS
ALEEALEPEF RNMELQNGNE GQHVVRKSTN VEAVAENDTM DNTADSVLER DPPKEVDEET
LQEQDVEKDQ VSEQSEMKDH QTETDATQKT IKKEVCEDGL VSAGEMSLDH DIMSVPPSVP
EELFQMVESL ADSTMLSQAD TSSVTDAESQ SNGNPEDTQP QPKVKNLIVK LTPVPVVTTC
GSRSSRSKNK EKGGEMSKKS EQECEEEENA ASDEVDGTKS PPPSRRSSRV KTTPLRKQTE
NKDKNVSSDS DSESEEDHKD KVKSSKKSRS TKKEDEKQAK ASDKKTADSD SDEVPDVLME
KAAAGDSTDE GSAKSKKHSL KLKPSTEDAE KLSKRKRKSV SSDSDLASKG KKTSKKKKRN
GSDSSDSDSE EKDSKARVAR RRSTRVKKQD DTKEESKNSP ETKPKRSYEK KCKGKGSRTS
SKLQLTSSDE EEEEAEGASG EDSDEQKIKP IVEDNVLAGS AAFIQSSDEV DTKEGITGFC
DDDDDDDPEN IAKKMLLAQI KSNYSSGAES SSDNEEAEKE EKSSKKVKKE NEEDEQQDED
TEDSGSDVEV KKSGRRHKLL RHKLSLSEGE SGEEKAAGKE KKKGKKKSGR KDSDDSADSD
FEKSESSGES AVSEVVSDSD NEDKRRKTSG EEGGEDQDGE GRKGRKKIRK ILKDDKLRTE
TRDALKEEEE RRKRIAEREA LREKLREVIV VEESSQVVCP ITTKLVLDED EETKEPLVQV
HRNLVTKLKP HQVDVQFMWD CCCESMKKIE KSSGSGCILA HCMGLGKTLQ VVTFLHTLLL
CEKLDFTTAL VVCPLNTVLN WLNEFEKWQE GMKDEESLEQ VTELATVKRP QERAYALQRW
QEMGGVMIMG YEMYRNLTQG RNIKSKKIKE TFQKTLVDPP DLAICDEGHI LKNEASAVSK
AMNSIRTRRR IVLTGTPLQN NLIEDHCMVN FIKENLLGSV KEFRNRFINP IQNGQCADST
LQDVRVMKKR AHILYEMLAG CVQRKDYTAL TKFLPPKHEY VLSVRMTPIQ AKLYRYYLEH
FTVGNAVEGS RGRAGTKLFQ DFQMLSRIWT HPWCLQLDYI SKENRLQGFF DEDSMDDFIA
SETEESSMSL TSEDEKIKKK KQGKGKKKGS DDSDSDDVEV IKEWNTSSRG RNGEGRNRAE
SVEERPSGSA PGSPTADWHK EFVTEADAEI LEHSGKIMLL FEILRMAEEV DDKLVFSQSL
ISLDLIEDFL ELACRAKDEE KISPYKEGKW YRNIDYYRLD GSTNATTRKK WAEEFNDTSN
TGRLFLISTR AGSLGINLVA ANRVIIFDAS WNPSYDIQSI FRVYRFGQLK TVYVYRLLAQ
GTMEEKIYER QVTKQSLSFR VVDQQQIERH FTMNELAELY TFEPDLLDDP SEKKSKKATP
MLPKDPFLAE MLQNNKDQIV CYHEHDSLLD HKEEEALSEE DRKAAWAEYE AEKKGMSMRT
NYQTAYAHAD MNNPSYFTYN IGALPSMTNQ QLEELINQGR QKVIEATNAL KSLSRESLED
IISRQWKENP ALTENQVQAV ALGRQATVEL ELKRREAIYR DVLNRQQSLM MYVQKLITNR
KVQEQQLAMA NQASYLNQLA LQNGMMGAGG LSQMDLLTLY QQLHGLGGHQ GMGKNPGPSK
GL
//
