ID W5N5I9_LEPOC Unreviewed; 978 AA.
AC W5N5I9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000015898.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000015898.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; AHAT01024716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5N5I9; -.
DR STRING; 7918.ENSLOCP00000015898; -.
DR Ensembl; ENSLOCT00000015928.1; ENSLOCP00000015898.1; ENSLOCG00000012909.1.
DR eggNOG; KOG0389; Eukaryota.
DR GeneTree; ENSGT00910000144252; -.
DR HOGENOM; CLU_000315_16_3_1; -.
DR InParanoid; W5N5I9; -.
DR OMA; MEMRRMA; -.
DR Proteomes; UP000018468; Linkage group LG2.
DR Bgee; ENSLOCG00000012909; Expressed in ovary and 13 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd14279; CUE; 1.
DR CDD; cd17998; DEXHc_SMARCAD1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1.
DR Pfam; PF02845; CUE; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00546; CUE; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51140; CUE; 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 Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 209..252
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 465..633
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 810..972
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 111957 MW; 606CAC8454289A19 CRC64;
MSLFNLDRFR FTKDKRKPDS AVLAEECRSE SPDSEKENKT ETPEPKRPPS NKQIKGVEFL
DSDSEADDLP STVSDAPSIK SKPVAKSLMH RNQQAGEPND SHWNTNEVDV ETTEERLSKL
KEIFPQKDSK QLKEVLKNTS TLDGAVASCM VLFGDEDNAR KRKNKDSSKS SSEDRDIVQP
SKKKKTAVSS SLFEVDENEA ANSMEEWEKQ EATLRRLQKK FPNLDKEELR DVLQEHEWCF
EDALEALRMF SDPDQDSSSS PEPKVTKEHT VSPDIKTWLS AGERPVARKQ NWICRPSESG
KNKARVTRVE DSSSEDEESI SSDYEKSSGE DSDAEDGLNQ EFKAKILTFL QDASVDELSL
ISQCSVKKAQ KIVELRPFKN WEDLIKTFTK ANGLTEDLIW GCKDVLKERD VVLGLMTKCE
KISKKMTEAV TRVTECGLNT FKQPALLNQR MQLKPYQLIG LNWLVLLHKN KLSGILADEM
GLGKTVQAIS FLANLYEEGD HGPHLITVPS STLDNWVREL KQWCPALKVL VYYGSVEDRR
YLRHDILNKE VDFNIIVSTY NLTISNADDR SLFRRLKLQS AIFDEGHMLK NMNSLRYKHL
MTINAKYRLL LTGTPLQNNL LELMSLLNFV MPHMFSSSTS EISRMFSMKS FEEQSTFERE
RIAHAKQIMK PFILRRVKNE VLKQLPSKEE KIEFCAMTEK QGKLYSALFE KLKRSVNGEK
KELCNVMMQL RKMANHPLLH RQYYTEDKLR QMSKLMLKEP THHDANPDLI FEDMEVMSDF
ELHNLCKQYK SLCKFQLDTN ILLNSGKFQV LEDILAKIKV KGDRVVLFSQ FTMMLDIVEV
LLKHLNLRYV RLDGSTPMAD RIHLIDDFNT DTDIFVFLLS TKAGGLGINL TSANVVVLHD
IDCNPYNDKQ AEDRCHRVGQ TKTVQVIKLI SKDTIEDCML KVSQKKLKLE QDMTAAVEGE
EGIIPEDMAS LLKATLGL
//