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Database: UniProt
Entry: A0A136KSJ4_9BACT
LinkDB: A0A136KSJ4_9BACT
Original site: A0A136KSJ4_9BACT 
ID   A0A136KSJ4_9BACT        Unreviewed;       801 AA.
AC   A0A136KSJ4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=UZ18_ATM001002146 {ECO:0000313|EMBL:KXK12358.1};
OS   Armatimonadetes bacterium OLB18.
OC   Bacteria; Armatimonadota.
OX   NCBI_TaxID=1617424 {ECO:0000313|EMBL:KXK12358.1, ECO:0000313|Proteomes:UP000070351};
RN   [1] {ECO:0000313|EMBL:KXK12358.1, ECO:0000313|Proteomes:UP000070351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB18 {ECO:0000313|EMBL:KXK12358.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Improved understanding of the partial-nitritation anammox process through
RT   23 genomes representing the majority of the microbial community.";
RL   Submitted (MAR-2015) 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=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034618};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC         translocating in the 3'-5' direction.; EC=5.6.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034617};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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:KXK12358.1}.
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DR   EMBL; JZQX01000183; KXK12358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136KSJ4; -.
DR   STRING; 1617424.UZ18_ATM001002146; -.
DR   PATRIC; fig|1617424.3.peg.2282; -.
DR   Proteomes; UP000070351; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          7..285
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          286..561
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         28..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   801 AA;  90159 MW;  49EBF9C5F6A6E595 CRC64;
     MPTTQSIPLN EEQRRAVEHE GGPLLVFAGA GSGKTRVIAA RIARLVAGGV YADRILAVTF
     TNKAAREMSE RVESLTGASV RPMWIGTFHS ICSRMLRRDA DKLGLSRDFV IYDDSDQLSL
     VREIFKSKNL DEKSINPRVI LREISNAKER LESPDAMAGR VAGFIERIAV DVYRSYSERL
     QKSNAMDFDD LIYWAVRLLE QRADVREQYQ SRFQHVLVDE YQDVNLSQYR FVQLMAEKSR
     NLVVVGDDDQ SIYRWRGADV KLILSFKADW PDATIIKLQQ NYRSTKTILR AANEVIRNNR
     SRAHKELWTE NIEGAHIHLI EAGTELDEAM AVAETILQDT STGRRKYGEF AVLYRTNAQS
     RVLEEALLTL RIPHVLIGGQ RFYERKEIKD AVAYLRLVLN SQDDVSFRRV INVPTRGIGA
     TSLQAIEQFA AANSISLLEA CATEEFLQQL SSRARNPIGA FSKAILEARH LSESGGVTQV
     LKSLLQASGY LSSLREDRSP DAQSRLENLQ ELLNVTTQYD ASADEPTLSG FLESVALVSD
     ADSIGEGGEA VTLMTLHTAK GLEFPVVFIT GLEEGVFPHS RSMQDDAELE EERRLCYVGM
     TRAQQELYLL RAHRRSVYGQ PQFNRPSRFL EEIPRELIRV MGGSRPAPEG LSTVYQERSG
     RYGVIEPRAA ASAAPAHGPA LAGLETAFRR RADGAPCEVW RRGRGGLRAD QGRHRSDRRV
     SGCHWSQETG ARPCEARTYL AAVWGPRCRS WRQAAARRTS TSRSMWETRG RSEFERGMGR
     FPSPFVRRGK SRSGATRAWN W
//
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