ID A0A444XL27_ARAHY Unreviewed; 812 AA.
AC A0A444XL27;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN ORFNames=Ahy_B09g096470 {ECO:0000313|EMBL:RYQ90326.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ90326.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ90326.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYQ90326.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU364117};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYQ90326.1}.
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DR EMBL; SDMP01000019; RYQ90326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444XL27; -.
DR Proteomes; UP000289738; Chromosome b09.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 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; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF69; ATP-DEPENDENT DNA HELICASE Q-LIKE SIM; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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, ECO:0000256|RuleBase:RU364117};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364117};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738}.
FT DOMAIN 180..356
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 512..655
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 48..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 90843 MW; A356B87177A68193 CRC64;
MGASNLSFDQ VLVEMLEMGF EYSSIVEGIK TVGLSIPNVV EHILTAGSGS GRATTSSKAS
TTTMQPSKFR APHGKALKRK ALSSTSQVRQ SSILDHFHSN DKSTVCNKIR DVAIVDLEMV
NEHDKPISKM PDDVTVMPGQ IVTGPMENLV VMSDWETRVG GLLQKHFGIL CLKSFQKEAL
NAWAAHKDCL VLAATGSGKS LCFQVPALLT GKVVVVISPL ISLMHDQCLK LARHGVSACF
LGSGQPDNTV EKKAMRGMYS IIYVCPETVL RLIQPLQKLA ESHGIALFAI DEVHCVSKWG
HDFRPDYSRL SVLRENFSTS KLKFLEFDIP LMALTATATH RVQEDILKSL RMSKETIVVL
TSFFRSNLRF MVKHSGTSQA FYEKDFHELI KVYGSKLNSN KNKKSSISKD SDDVSSSSGA
GRISNNDDVS PYDVDDNHDD YGGRYVNVMR SGNTDNLVKG KELSVEFLEN DNDDCQSVDD
WDVTCGEFCA QSPPKDWELS EIDDPPKEPE GSLKVLKGPL EQGPAIIYVP TRKETLKIAK
YLCKFGVKAA AYNAALPKSH LRRVHKEFHE NTIEVVVATI AFGMGIDKPN VRRIIHYGWP
QSLEAYYQEA GRAGRDGKLA DCILFANLAR VPSLLPSRRS EYQTKQAYIM LSDCFRYGMN
TSCCRAKTLV EYFGEEFSHR KCLLCDVCVD GPPQRQNMKD EACILLQTIA ASHACSYSMD
VAYDDDIHFE YGYGRHGERL CLKNIVGKIR EQSQKFLNTD ILLWRGLSRI LEAKGYIREG
DDKSCYMHAV ISCDCKLVIQ LWFLSRRRPM FR
//
