ID A0A3Q3GPM8_9LABR Unreviewed; 2243 AA.
AC A0A3Q3GPM8;
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 Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000035366.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000035366.1}
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}.
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DR STRING; 56723.ENSLBEP00000035366; -.
DR Ensembl; ENSLBET00000036865.1; ENSLBEP00000035366.1; ENSLBEG00000026519.1.
DR GeneTree; ENSGT00940000155902; -.
DR InParanoid; A0A3Q3GPM8; -.
DR Proteomes; UP000261660; 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; RAD54-LIKE; 1.
DR PANTHER; PTHR45797:SF3; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 160..297
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1362..1549
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1798..1974
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 60..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..1257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1694..1775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..973
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1012
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2243 AA; 254485 MW; BBD42EE28802AC05 CRC64;
MDHSEQESIG GCWPIGMRTG FRLDAPFYRV HSHPARWSPC FVCPDRSCFV TQWCRRKAGK
MSLLSSESNT DQMAEKAEEA GSSTDTMKPS SSRNKRKSAT VTKHTEQNEP DSAESQNEGA
SSDNPSDNNT GSVSKGTLVM RPAGNENKGA MKLRVDFKQK STDDTLQKKI NCTACGKQVY
QFQRNSVYEH PALKVLICKS CYKYYTSDDI NRDSDGMDEQ CRWCAEGGKL ICCDYCNNAF
CKKCILRNLG RKELSVITDE LSKWQCYVCR PEPLQDLVSK CSSIMDKQEL KQRKVEKTSE
EREGKRHKSK AVKEHKAVVN GKEHIEGSGT MTFSYKRLHV PKDLVKKAKK LVETTTGLNN
TFIQFIQQAE EEQGDKSIRY RHLKAFKAVL TDLKKAHSAL EAALGPEFKN MELQNGTEEQ
AVVGKSTEVN APVEKDHSQD VTEAFDEADA VEEQGMEQIE AQNEQPAEDF DEEPDEQHNK
ELNEQCKEEL SEQSKEELNE QSKEELNEQR KEELNEQSKE ELNEQRSEEL NEQSNEELNE
QSNEELNEKR NEELNEQSNE ELSEQSNEEL NEQSKEGVNK QSKEGVNKQS KEGVNKQCNM
KLNKQCNEKL NKQRNEKLNE QRNEQDADSD QTSSETAVKD NQTETVSTKK TIKTEMCDDA
LMSTSEMSLD HDIMSVSPSV PEELFQMVES LADSSMLSQK DTDLVKNTDT KSDKNSTTDS
QRPQPKVKNL IVKLTPVPVV TTRGSRTSRS KNKEKDGEVP KKCKEEKCEE EEDNAAVDQT
DSPPPSRRSS RVKTTPLRKQ AESKSKDESS ESETEEDSKS KAKSSKKSRN TQKEDGKESK
ASEKKTIDSD SDEVPDILLE KAAAANSTDE EQESTNAKKC LFKSNNTSAK EKDTASKRKR
KSDSSDSNPE DKNKKTSKKK KKPNGTESSG SDSDQEKENK SKVSTARRRS SRVKKQDEAK
EEVSAERKGT DRKRSYEKKR KGRRSKANSK LQSSSSEAEE EEEEEGKPEG DSGEDSDEQK
IKPIVEDNVL GASGPFHQSS GEEMDDKEKP SGVCEDDDDD DDDDPENRIA KKMLLAQIKS
NYSSGAESSS DNDDDDKAEK SSKKVKKEDE GEEEQDSDSD ASSSDVDVKT SGKRHKLLRR
KLSLSEGESG EEKDTSKEKK KGGKKKSSRK VGSDDSADSD FEKTEGSSEE SGISEELSES
ENEGKRRKTR SSKKKKDEEK QRSYKQKKKR RRIKVQDSSS SNEKSGEDDE DAEGKKARKK
IRKILKDDKL RMETRDALKE EEDRRKRIAE REALREKLRE VIEVKESSQM TCPITTKLVL
DADEETKEPL VQVHRNLVTK LKPHQVDGVQ FMWDCCCESV KKMEKSSGSG CILAHCMGLG
KTLQVVAFLH TLLLCEKLDF STALVVCPLN TVLNWLNEFE KWQVGMQDDE SLQVIELATV
KRPQERAYAL QQWQESGGVM IIGYEMYRNL TQGRNTKSKK LKEIFQKTLV DPGPDMVICD
EGHILKNEAS AVSKAMNSIR TRRRVVLTGT PLQNNLVEYH CMVNFIKENL LGSVKEFKNR
FINPIQNGQC ADSTSHDVRI MKKRAHILYE MLAGCVQRKD YTALTKFLPP KHEYVLSVRV
TPLQCKLYRY YLEHFTGVGN ALEGGRGRAG TKLFQDFQML SRIWTHPWCL QLDYISKENR
GFFDEDSMDE FIASETDESS MSMTSEDEKK KKKKGGRGKK KGSEDSDSDD VEVIKEWNSS
SRGKNGLGRN RPEPVEEEPA PHTGSTPGSP TPDWHKEFVT EADAEILSHS GKIMLLFEIL
RMAEEVDEKV LVFSQSLISL DLIEDFLELS CRAKDEGKIS PYKGDGKWFR NIDYYRLDGS
TNAVTRKKWA EEFNDTSNIR GRLFLISTRA GSLGINLVAA NRVIIFDASW NPSYDIQSIF
RVYRFGQIKT VYVYRFLAQG TMEEKIYDRQ VTKQSLSFRV VDQQQIERHF TTNELAELYH
FEPDMLDDPS EKKSKKATPL LPKDPFLAEM LQNHKDYIVC YHEHDSLLDH KEEEALSEED
RKAAWAEYEA EKKGMSMRNN YQTQYSQMDM GNSSYFSYNV AALASMTNQQ LEELINQGRQ
KVIEATNALK TFCRESLEDT IARVWKENAS LTESQVQSIA LGRQASIELE VKRREAVYRD
VLTRQQTLMM YVQKLITNRK VQEQQLAMAN QASYLNQLAL QNGMMGGGGG GLSQMDLLGL
YQQLHGLNPP QGMGKNPGPS KGL
//
