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Database: UniProt
Entry: A0A093J704_FULGA
LinkDB: A0A093J704_FULGA
Original site: A0A093J704_FULGA 
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}.
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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
//
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