ID L5JTD5_PTEAL Unreviewed; 895 AA.
AC L5JTD5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=PAL_GLEAN10007286 {ECO:0000313|EMBL:ELK02262.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK02262.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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};
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DR EMBL; KB031138; ELK02262.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JTD5; -.
DR STRING; 9402.L5JTD5; -.
DR eggNOG; KOG0384; Eukaryota.
DR InParanoid; L5JTD5; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR CDD; cd18054; DEXHc_CHD2; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 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; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
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 PANTHER; PTHR45623:SF19; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 2; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:ELK02262.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:ELK02262.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 278..370
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 474..644
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 1..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..217
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..268
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 102278 MW; AAD4207A0019246A CRC64;
MGLPVLSSQG CHSASEEASG SDSGSQSESE QGSDPGSGHG SESNSSSESS ESPSESESES
AGSKSQPVLP EAKEKPASKK ERIADVKKMW EEYPDVYGVR RSNRSRQEPS RFNIKEEIVE
PGGGGVPKNC ELKSAIISPP YPLKASSGSD SGSPKRRGQR QLKKQEKWKR EPSEDEQEQG
TSAESEPEQK KVKARRPVPR RTVPKPRVKK QPKTQRGKKK KQESSDDDDE DDEAPKRQTR
RRAAKNVSYK EDDDFETDSD DLIEMTGEGA DEQQDNSETI EKVLDSRLGK KGATGASTTV
YAIEANGDPS GDFDSEKDEG EVQYLIKWKG WSYIHSTWES EESLQQQKVK GLKKLENFKK
KEDEIKQWLG KVSPEDVEYF NCQQELASEL NKQYQIVERV IECSWEDEAL IGKKFQSCID
SFHSRNNSKT IPTRECKALK QRPRFVALKK QPAYLGGENL ELRDYQLEGL NWLAHSWCKS
NSVILADEMG LGKTIQTISF LSYLFHQHQL YGPFLIVVPL STLTSWQREF EIWAPEINVV
VYIGDLMSRN TIREYEWIHS QTKRLKFNAL ITTYEILLKD KTVLGSINWA FLGVDEAHRL
KNDDSLLYKT LIDFKSNHRL LITGTPLQNS LKELWSLLHF IMPEKFEFWE DFEEDHGKGR
ENGYQSLHKV LEPFLLRRVK KDVEKSLPAK VEQILRVEMS ALQKQYYKWI LTRNYKALAK
GTRGSTSGFL NIVMELKKCC NHCYLIKPPE ENDRENGQEV LLSLIRSSGK LILLDKLLTR
LRDRGNRVLI FSQMVRMLDI LAEYLTIKHY PFQRLDGSIK GEIRKQALDH FNADGSEGRA
TPDKLETMVT SQFVHIELLS TRGLERSEEK RVGEGSAVGM CRDAEVHLDQ FWRER
//
