ID A0A093J704_FULGA Unreviewed; 1642 AA.
AC A0A093J704;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE Flags: Fragment;
GN ORFNames=N327_07323 {ECO:0000313|EMBL:KFW10770.1};
OS Fulmarus glacialis (Northern fulmar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC Fulmarus.
OX NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW10770.1, ECO:0000313|Proteomes:UP000053806};
RN [1] {ECO:0000313|EMBL:KFW10770.1, ECO:0000313|Proteomes:UP000053806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW10770.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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: Nucleus {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 EMBL; KK608731; KFW10770.1; -; Genomic_DNA.
DR Proteomes; UP000053806; Unassembled WGS sequence.
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 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
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; PF00176; SNF2-rel_dom; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51533; ADD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
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:UP000053806};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 154..291
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1511..1642
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 18..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1420..1448
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1026..1086
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW10770.1"
FT NON_TER 1642
FT /evidence="ECO:0000313|EMBL:KFW10770.1"
SQ SEQUENCE 1642 AA; 185607 MW; F068AABE2D2BBE67 CRC64;
SESKLNTLVQ KLHDFLAHSS EESEDAVSPP ALSKNKTIGK SREPKSSPAS MENNREEGSS
SSERTKSLGS SRSKRKPTIV TKYVGSDDEQ ILDETVNEDI SNENSENDVD MKSLPKGTVV
VQPEPVLNED KDDFKGPEFR SRNAVKMKPE APKKRGEEGL HGIVSCTACG QQVNHFQKDS
IYRHPTLKVL ICKTCYKYYM SDDISRDSDG MDEQCRWCAE GGNLICCDFC HNAFCKKCIL
RNLGRKELST ILDENNQWHC YICHPEPLLD LVTACDSVFE NLEQLLQQNK KKIRVESEKS
KIYDHTVKFS PKRNNSNCNG EEKKLDDSYS GSLTYSYKAL MVPKDLLKKT KKLVETTANL
NSSFVSFLKN AAENVEVSPT VQLCQLKAFK SVLSDMKKAH LALEEGLNLE IQALNVKIKD
KNTKEKKPDV RSEKNEVKKD EGKEHVALKE DDTVKTQKKV VSERPDSEPM DQSVPTTEQT
DNKRTSGEDK RSGRNEEPQY EPNSTEALDM DIVSIPSSVP EDIFETLESA MEIQVTSDEQ
DNGNTGTDHE TLNSNIKLNT PMKDTKGGTK LKSSAKGTKE LIVKLTPVSL SESTVKAEDQ
DSNLEKGSKD VDVIPRAENS DSVKQNHNAG SEPSTENETV SLVEESDLRR SPRVKTTPLR
RQTDVNPLTS NSEEDSNDTC NEKRKRKSSK QPRRKNDKRN SSDSTVDGPS PNKLSKSKKP
YVLDHSSDSD EMPAVLKEVA MMSHSSSDIE SNSEAPTNDQ KTLNFLKNQP VKDENGKRKR
KSSSSGSDLD AKRGKSAKNS AAAKKKRQNY SDSSNYDSEL EKEIKILSKI ESAKKAKKKY
SRKEDSYDSS EEEQRKKVNS KRKINLKKQR EKSSEDGDAE KSSPEKEINH SSQDKIGKGS
AAKERINRDL KEKTVKGKHD ESSDVEKSSL EKEESCPKGV KLTEVKKSKD LKKKKAQEDS
SSESTEKSAK KEQDFDSSKD RSKNKKGSES KAKKSEKLKK KSYKKEQDDS SSDVEKSCPE
KGSCNSSEND KTKNEPVFKE KKRRNLRERV SKRVQIDLSS DAEKSPLKEE SSSEDAVRSK
KQTETKEKKK ISHKKKISKK EQNDSLSSSD EESYEDSKKK IKRGSMKESK KSNLKKKVSK
KKVVVTSSSS SDKEENDEQN STGEGSSDEQ KIMPVTENLM LSAGTGFCQS SGDEGETKSR
AVPMEEEEDD DDDDPENRIA KKMLLEEIKA NLSSDEDASS DDESDEGKKK TGKQNENTGD
DEENEKEDNS ESDSEEEESK KPRYRHRLLR HKLTVSDGES GEEKKVKPKD KKEGKRRSRR
KVSSDDSNDS EFHESAVSEE VSESEDDQRP RTRSAKKAEA EENQRSYKQK KKRRRIKVQE
DSSSENNNKS NSEDEDNDDS KSPGKGRKKI RKIIKDDKLR TETQNALKEE EERRKRIAER
EREREKLREV IEIEDASPLK CPITTKLVLD EDEETKEPLV QVHRNIVTRL KPHQVDGVQF
MWDCCCESVK KTKTSPGSGC ILAHCMGLGK TLQVVSFLHT VLLCDKLDFR TALVVCPLNT
ALNWLNEFEK WQEGLEDDEK LEVCELATVK RPQERSYMLQ RWQDEGGVMI IGYEMYRNLA
QGRNVKSRKL KEIFNKALVD PG
//