ID M7BL95_CHEMY Unreviewed; 1029 AA.
AC M7BL95;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=UY3_10060 {ECO:0000313|EMBL:EMP32788.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP32788.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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; KB538686; EMP32788.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BL95; -.
DR STRING; 8469.M7BL95; -.
DR eggNOG; KOG0389; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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; 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; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000031443}.
FT DOMAIN 250..293
FT /note="CUE"
FT /evidence="ECO:0000259|PROSITE:PS51140"
FT DOMAIN 512..680
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 861..1013
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 116188 MW; A1AAC57D6626C80E CRC64;
MSLFNLDRFR FEKKSKKVEQ ENPPPSLPIA ELAAAPSAAA DSVAAAGGGG DDEVTDDSSR
PDTPTSDVTE KTEKCLSDGE AKGSHKSGHT ALPSRAEDSS VPETPEAERT KNLSSFKNRR
GIQFIDVSSD SEDQGPPKCS STKQDSVPMS EVIVIYNCGG SPAQPLNSCI GSHAQLRCGI
ARVVMLLIES TSTMDEAIAA GLKFNDEAAS RKRKLNQSPT NNSEDCGDQI SKKQKMNSLE
GAESQKEWEK QEALVKKLQN KFPSLDKEEL KDVLQEHNWV FHEALESLKV FAEDQQDVQY
PSKSEVSSWN EVSTNSKKHY NNDTKVKVKQ KSSAKAQNGF RKKDKGKKGV WRTKRETEDS
EYESASEGGS SLDEDYSSGD EVMEDGYKTK ILSFLQDASL GELTLIPQCS QKKAQKITEH
RPFNSWEALF TKMSKTNGLS EDIIWNCKIL LKEREVVLKL MNKCEDISNK LTKQVTRITE
DGGCGWNIEQ PSILNQSMEL KPYQKIGLNW LALLHKHGLN GILADEMGLG KTIQAIAFLA
YLYQEGDKGP HLIVVPASTL DNWIREVNLW CPALDVLFYY GSQEDRKQLR IDINNKVVNF
NVIVTTYNSA ISSADDRSLF RRLKLNYAIF DEGHMLKNMG SVRYQHLMTI NAKNRLLLTG
TPVQNNLLEL MSLLNFVMPH MFSGSTSEIR RMFSSKTKAA EEHSIYEKER IAHAKQIIKP
FILRRVKDEV LKQLPPKKDL IELCDMSEKQ EQLYYDLFNK LKKSFDSQEK NSEMGNVMMQ
LRKMANHPLL HRQYYTADKL KMMSTLMLKE PTHCDANPDL IFEDMSVMTD FELHLLCKQY
ASVSDFKLEM DTILDSGKFR TLERILSDLK EKGDRVVLFS QFTMMLDILE VLLKQQQHRY
IRLDGKTQIS ERIHLIDEFN TDMGIFVFLL STKAGGLGIN LTSANIVILH DIDCNPYNDK
QAEDRCHRVG QTREVQVIKL ISKGTIEESM LKISQQKLKL EQDMTAVDLG EEGTIPADIA
TLLKASLGL
//
