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Database: UniProt
Entry: A0A0Q8PY89_9BURK
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ID   A0A0Q8PY89_9BURK        Unreviewed;       716 AA.
AC   A0A0Q8PY89;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=ATP-dependent DNA helicase {ECO:0000313|EMBL:KRB78290.1};
GN   ORFNames=ASE07_26120 {ECO:0000313|EMBL:KRB78290.1};
OS   Noviherbaspirillum sp. Root189.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=1736487 {ECO:0000313|EMBL:KRB78290.1, ECO:0000313|Proteomes:UP000051303};
RN   [1] {ECO:0000313|EMBL:KRB78290.1, ECO:0000313|Proteomes:UP000051303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root189 {ECO:0000313|EMBL:KRB78290.1,
RC   ECO:0000313|Proteomes:UP000051303};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB78290.1, ECO:0000313|Proteomes:UP000051303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root189 {ECO:0000313|EMBL:KRB78290.1,
RC   ECO:0000313|Proteomes:UP000051303};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRB78290.1}.
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DR   EMBL; LMHZ01000039; KRB78290.1; -; Genomic_DNA.
DR   STRING; 1736487.ASE07_26120; -.
DR   OrthoDB; 9765586at2; -.
DR   Proteomes; UP000051303; 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: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; 1.10.275.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010614; RAD3-like_helicase_DEAD.
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; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00488; DEXDc2; 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, ECO:0000313|EMBL:KRB78290.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051303}.
FT   DOMAIN          173..434
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51193"
SQ   SEQUENCE   716 AA;  80450 MW;  AE0FB21DFCD9904A CRC64;
     MEYQVAVRAL AEFTARRGDL DLRFTPAPTA QEGIAGHVEV TARRAADYQR EVTLTSRHRH
     LVVRGRADGY DPACNRLEEI KTYRGDLSRM PANHRALHWA QAKIYAWLLC EKLQLTEVNV
     ALVYFEIGSR QETMLEESHQ ATALQSFFME QCESFLNWST QELDHRIARN AALSALRFPH
     AGFRPGQRAL SEAVYRAANT GRCLAAEAPT GIGKTVGTLF PLLKAVPGKD LDKIFFLAAK
     TTGRSLALDA LEQLKNHQPG MPLRVLELVA RDKACEYPDK ACHGESCPLA KGFYDRLPPA
     RSAAIASGAL NKAALRAVAL EHQVCPYYLS QDLVRWADVV VGDYNYYFDS SALLYGLTTA
     NQWRVTVLTD EAHNLIERAR KMYSAELDQS TLQAVRRTTP DALGKAIDRL QRQWTALNKT
     QESDYKIFSE IPAKFANALQ KTVSEISEFF AENPAYVNSA LQNFYFEALH FTRLLEVLDT
     HSLFDLAKQE RNEHIRSRIG IRNVVPAKFL APRFTEAQSA ILFSATLSPW HFYADMLGLP
     SDTAYIDVES PFKAEQLSVF VAGYISTRYR QREQSIAPIV ALMEKQYQSQ RGNYLAFFSS
     FEYLDKVSAL FRARHPDIPV WEQSRGMDET ARDAFLARFT PGGCGIGFAV LGGPFSEGID
     LPGERLIGAF IATLGLPQFN AVNEEHREXL SGNSHAAWTR LHVTRFSRAL HRVVVE
//
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