ID L5L4C6_PTEAL Unreviewed; 1272 AA.
AC L5L4C6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=PAL_GLEAN10009516 {ECO:0000313|EMBL:ELK18290.1};
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:ELK18290.1, 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};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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DR EMBL; KB030332; ELK18290.1; -; Genomic_DNA.
DR AlphaFoldDB; L5L4C6; -.
DR STRING; 9402.L5L4C6; -.
DR eggNOG; KOG0351; Eukaryota.
DR InParanoid; L5L4C6; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd18016; DEXHc_RecQ2_BLM; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR012532; BDHCT.
DR InterPro; IPR032439; BDHCT_assoc.
DR InterPro; IPR032437; BLM_N.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 2.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF08072; BDHCT; 1.
DR Pfam; PF16204; BDHCT_assoc; 1.
DR Pfam; PF16202; BLM_N; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00570; HRDC; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552}.
FT DOMAIN 684..859
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 845..986
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1174..1254
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1272 AA; 142812 MW; BA417D99E8F43D0A CRC64;
MAAVPQNNLQ EQLERHSARK LNNKLSFSKP KSSGFTFKKK ISAANDVSVT SVSVAKTPVL
SDKDINVTEA FFFSEPLAHT TSQQTEIDDF QNAPARQQTK RAGSKPLLPD LVQEVLHTTQ
STPIIKESRD PAFKKLEFSS SSDSFIAINN WDDMDDFDTS GNSKAFVTPL RNHFVRVSTA
QKSKKSKRNF FKAHLHKANT VKVDLTSSSS ESNQVYSTKE QKADSKWLNS GVICIDDSPN
SQELINEDSQ DSHSLKTHLR EEGDNSEKKK NFEETELYSI EKSPCIELDE DDYDIDFVPP
SPEEEMTSAS SSSLKCFSML KDLDTCDQKK ESFGTSEDLT KPEKMPTQQS NEESSTDCDA
KQINLQQQLI RVMDNICNLV DTIPDNELKS LDCGNNLLQQ RNIRRKLLAE ADFNPGDAGV
LGVVWRCRPD ALGSPMGDVA SVSSPYAFPK GDFCPRGNSD EFNFPLVPSN SISTGECLVT
TTPGRAGFSA TRKNLTEGPS FISHVQQCFV SSDQADTPRI EKRNESSHFP RNVLTSTAMT
DQNEHIASVD LEREIQASYD TDNFDIDGFD DDDEWEDIMH NLAASKSSTA VYQPIKEGRP
VKSVSERVSP SKTNCLPVAS TPQNKNFSES IQNYTDESAQ NLPSRHLKHE RFQSLSFPHT
REMMKIFHKK FGLHNFRTNQ LEAINAALLG EDCFILMPTG GGKSLCYQLP ACVSPGVTIV
ISPLRSLIVD QVQKLTSLDI PATYLTGDKT DSEATSIYLQ LSKKDPIIKL LYVTPEKVCA
SNRLISTLEN LYERNLLARF VIDEAHCVSQ WGHDFRQDYK RMNMLRQKFP SVPVMALTAT
ANLRVQKDIL TQLKILRPQV RECDTMADTL QKNGLAALAY HAGLSDSARD EVQHKWINQD
GCQVICATVA FGMGIDKPDV RFVIHASLPK SVEGYYQESG RAGRDGEVSH CLLFYTYYDV
TRLKRLILME KDGNHHTKET HFNNLYSMVH YCENITECRR IQLLAYFGEI GFNPDFCKKY
PDVSCDNCCK TKDYKTRDVT DVTKNIIRFV QEHSSSQGTR NIKHVGPCGR FTMNMLVDIF
LGSKSAKIQS GLFGKGSTYS RHNAERLFKK LILDKILDED LYINANDQPI AYVMTGSKAQ
TVLNGHLKVD FMETENSSSI KKQKALVTKV SQREEVVKKC LGELTEVCKA LGKVFGVHYF
NIFNTATLKK LAESLSSDPE VLLQIDGVTE DKLEKYGAEV IPVLQKYSEW TLPGKVWQDR
DHPISLENVA LK
//
