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Database: UniProt
Entry: W5N5I9_LEPOC
LinkDB: W5N5I9_LEPOC
Original site: W5N5I9_LEPOC 
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
//
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