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Database: UniProt
Entry: A0A242K732_9ENTE
LinkDB: A0A242K732_9ENTE
Original site: A0A242K732_9ENTE 
ID   A0A242K732_9ENTE        Unreviewed;       786 AA.
AC   A0A242K732;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0000259|PROSITE:PS51193};
GN   ORFNames=A5888_002342 {ECO:0000313|EMBL:OTP16128.1};
OS   Enterococcus sp. 9E7_DIV0242.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1834193 {ECO:0000313|EMBL:OTP16128.1, ECO:0000313|Proteomes:UP000195141};
RN   [1] {ECO:0000313|EMBL:OTP16128.1, ECO:0000313|Proteomes:UP000195141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9E7_DIV0242 {ECO:0000313|EMBL:OTP16128.1,
RC   ECO:0000313|Proteomes:UP000195141};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genomic Center for Infectious Diseases;
RA   Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA   Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Enterococcus sp. 9E7_DIV0242.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC       {ECO:0000256|ARBA:ARBA00038058}.
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:OTP16128.1}.
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DR   EMBL; NGMM01000003; OTP16128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A242K732; -.
DR   OrthoDB; 9765586at2; -.
DR   Proteomes; UP000195141; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.275.40; -; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 1.10.30.20; Bacterial XPD DNA helicase, FeS cluster domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR   InterPro; IPR042493; XPD_DNA_FeS.
DR   PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR   PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000195141}.
FT   DOMAIN          182..433
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
SQ   SEQUENCE   786 AA;  91833 MW;  BF7D3230F05A294F CRC64;
     MFHSEKIPIR RLVEFILRQG SIDSRRTSNH TAQEGARIHR KLQKEAGKGY QKEVKIAKEV
     VLNDKPYFVE GRMDGLFTNE QEQLVIDEIK TSESAFEDIY DEQLAMYWHQ IKCYGAIYSE
     QEELEEITLQ LTYFQTTTEE VTKTQKVFSR IELKQFLDEL LEEYEKWLIF SENWRTVRNQ
     SLKELPFPYG EYRKGQRELA VSVYKTILSE QRLFVEAPTG TGKTISTLFP SLKAIGEGKA
     EKIFYLTAKT ITRQVAEDAV QAMNQKEMKI KSLTITAKDK ICFLTERNCT PEHCPFAAGY
     YDRLNEGLWD ILHHENQFSR EVIEKYAQKH QLCPYELSLD VSLWCDLIIC DYNYVFDPTV
     YLRRFFDEGV KKDYLFLIDE AHNLVSRSRE MYSAELSKGQ LLMMKKLLKK KSAPLTRAVN
     KVVDEFDRLD ELCISEEKEF ISQPAYLDGM EKKVFRLTEK IGEWLPQNQE LPELNQLLEI
     YFALLNYLKI GEFYDDHYCT YIQKKNRGLS VKLFCLDPSY LLAQKLSMAN ASILFSASFT
     PLSYYKDILG GEEESLTYRI PNPFPEENQR LLIARYVQTT YREREKSLDY LVESLTTMIN
     QKMGNYLFFF PSYAYLDMVY EAFKKANPQV KTLIQQTEMN EKERELFLAQ FVSEPQETLI
     GFCVLGGVFS EGIDLKGDRL IGTAVISVGL PQINEEQELI KNYFDEQGLG FQYAYQIPGM
     NKVLQAAGRV IRDAEDHGVV LLLDQRFASP AYQRLVPPHW YRAQILPTVH HLEKNIQAFW
     KEIDSK
//
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