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
//