ID K0HUK2_9BURK Unreviewed; 1740 AA.
AC K0HUK2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=RecQ familyATP-dependent DNA helicase {ECO:0000313|EMBL:AFU46623.1};
GN ORFNames=C380_14620 {ECO:0000313|EMBL:AFU46623.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU46623.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU46623.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU46623.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(2012).
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|ARBA:ARBA00001665};
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};
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DR EMBL; CP003872; AFU46623.1; -; Genomic_DNA.
DR STRING; 358220.C380_14620; -.
DR KEGG; ack:C380_14620; -.
DR PATRIC; fig|358220.3.peg.2978; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG0514; Bacteria.
DR eggNOG; COG0847; Bacteria.
DR HOGENOM; CLU_002862_0_0_4; -.
DR Proteomes; UP000006306; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 5.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
PE 4: Predicted;
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 324..499
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 524..693
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1107..1323
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT BINDING 1128..1135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1740 AA; 193792 MW; 4C3863AD8827D687 CRC64;
MLRFAWPSLE TPVLDSFRAR ARRIAAEGRI VSVDVEAHPE KDDQIFAVGA VRSDGQDTFR
STCSPAKAAS VATALNSFAR DGQVLLGHNL KRHDIPLMRA QLPQLECLQW PVLDTLELSA
LAFPSNPYHR LVKGYKLLSD ERNNPTKDAR VALNVFEEAV EALLETNDQE PWWLTVLHFL
LRNDESMATL LAQVREETTP AREAIGPIVA SRFADRCCAT RLEALVAEIV TSFDGHDPWS
VAFALGWIRV AGGNSTLPHW VFHELPAVRQ LIAELREIDC GQTNCPYCRE NHNPEALLSS
LFGKPSFRAQ PTTTDGSSLQ RAIVSAGLTR ESLLAVLPTG GGKSICYQLP ALVHYRRSGR
LTIVISPLQS LMRDQVDNLM KADIQCAATV NGMLTPLERR DVLDRIRLGD VGIVLVSPEQ
FRSKTFVEAI RVREIAAWVF DEAHCLSKWG HDFRTDYLYV SRFIREQFPG QAPIACFTAT
AKPDVIEDLC DHFQEGLQVE LKTFLGGHER TNLSYAVVPT SGGEKPQRIV ELLRDGLRRE
DAAVVFCATR RSAETIAQIV TQQGVACACY HGGLSADLRK ETQRRFLDGE LQVIAATNAF
GMGVDKPNVR LVIHAEIPGS LENYLQEAGR AGRDGNEAKC VLLFDPKDVE TQFRLSSTSQ
LSQRDFIGLL RALRFQAKKL GKGEIVISAK ELLAQSVGTS IELDAPDAST KVTTALSWLE
RHGFLTRNEN ATKVFPASLR VTSLQEAKER IAKADFSANV RQKFLAVATA LFRSETPEGL
STDELMLDAG IRPEECFRIV HQLAKLGILV NDLGLTVRLM RGVRGASVSR LEYLSAMEKE
LVELMAENAP DADQDDAQQH LNLRAVCTEL RSRLNLDDEK GHLDPTQVRA CLRSMADGFG
SGNDKRSMIQ LQSLGDDTLR VTLRRPWSQI RRICELRRAV AQVTLTRLLA EVPDGVKGAC
LVECKAQALI DALSDDLVLK TQLREPDVAL ENALLYLHQT RVLELDKGRS VFRSAMTIQM
EEDTSRRFSQ ASFAPLEEFY KERTLQTHVM HEYAKLGAED PAKALDLVKA YFTLPHKQFI
KEFFRGRTDL LERKTTDESY QRIVDDLQHP VQEALVTQPR TGNHLVLAGP GSGKTRVIVH
RIAYLLRVQR VNPGRIIALA YNRGAAVQLR RRLLTLAGDD ARGVLVMTYH AMALRLTGTS
LAGAERTSSN VDFKKMLQDA IDLLEGKSSA LIDADEVRDR LLQGYEYIFV DEYQDIDAQQ
YALVSALAGR RRADADTKLS IMAVGDDDQN IYSFKGANIE FIRRFRADYE GDLTYLVENF
RSTQNIISAA NHVIQRGADR MKVDHPIRID ERRKDDLPGG RWAALDKEGR GAVRLITSPA
APNLQAQLVH AEIERIRCID PTVKLSEIAV LCRTHAPLEK MRAICDVEGL PCEVTGPEAA
KGQIALMRTR EGWALAQALR RRQLRMVRLS ALRRSLTYLQ RAQPRNAALL DLLDIVDDVA
SSLQADIVPA AEALDLFYEA AGEMRRDGRD SAIKLMTAHA AKGLEFDHVI VMDCADWRWD
EEDERRLLYV TMTRARQSLS LMRAEGGRNP YLVDLGTIDG VQDQLPRARP KHRADLERQY
VMLGPASMDI GFAGRASLAQ PIHRAIAALR IGDVVEVKGR FVHSTSGQIV GRLAASIDAT
HLQRGVASVV AVMVRTRSQT PEEYWPALQA DHWETPLAEV RLADPSATSA VDELQALGRQ
//
