ID Q0S2T3_RHOJR Unreviewed; 1115 AA.
AC Q0S2T3;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=RHA1_ro06376 {ECO:0000313|EMBL:ABG98153.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG98153.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG98153.1; -; Genomic_DNA.
DR RefSeq; WP_011598296.1; NC_008268.1.
DR AlphaFoldDB; Q0S2T3; -.
DR KEGG; rha:RHA1_ro06376; -.
DR PATRIC; fig|101510.16.peg.6429; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG2887; Bacteria.
DR HOGENOM; CLU_003630_1_1_11; -.
DR OrthoDB; 4812256at2; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF55; DNA HELICASE; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 17..359
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 360..679
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 820..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1115 AA; 118998 MW; D08931C00F915CB8 CRC64;
MTIRIDPVEL AVGLGQHPPT PEQAAVIAAP LGPTLVVAGA GAGKTETMAA RVVWLVANGV
VDPEAVLGLT FTRKAAQQLT ARIRKRLARL AGSDLLRRVD PSGDLRSRIL AGEPEVSTYH
SYAGRLLSEH GLLLPIEPSA TLLSETELWQ LAHRVVSSWD GDLDTDRNPA SVTEAVLALS
GQLAEHLVEP DDLREAHTEL DKLVHTLPAG PRQRGGPGKE LLDILDTQHR RVELLPLVQR
LADTLRREGA LDFGSQMSLA ARVAADHPEV GLAERTRFRV VLLDEYQDTG HSQRVLLSSL
FGGGLDGELA LTAVGDPMQS IYGWRGASAA NLPRFATDFP LANGDPAPTL ELLTSWRNPP
EALALANMAS ASLRERGVSV STLRARPQAV PGDVRLALTG DVVQEREWVA DRIAEQYADA
TSRGEDPPTA AVLIRRNADA APIAEVLRSR GLPVEVVGLG GLLHTPEVAD VIAMLRVVAD
PMAGSAAVRM LTGARWQIGA ADLTALSRRA SELAIGTGYG TTGAVTDSSA LADAVGQALP
GEHAEQAGLA DALADPGPAE RYSQVGYARI TAVAAELASL RERIGQPLTE LVAEVERALG
IGIEAQARTR RSARGSAGRE HLDAFADVVA GYASRTSATV TGLLAFLSAG ESVEKGLAPG
EVEVDPHRVQ VLTVHSAKGL EWEVVAVPHL TAGVFPSRTA SGSWLGAVGE LPPSLRGDRA
RPGESADGVP VLELENLYDR KDLEEAVKAH KAALAARKLD EDRRLFYVAL TRTERVLFAS
GHHWAESGTE PKGPSEFLTE LRDTVTDEEH EGIGIVDIWA PAPEPDEQNP LTSTPKSAVW
PRDPLGLRRE SVERGAALVV AALKRAGAPT PAGEDDDPEN WAADVDALLA EREARANART
EVVLPGQLSV SQLVELEADP DALAARLRRP LPFPPNPLAR RGTAFHAWVE RRFGATRLLD
LDELPGAADT DAGPDTDLAT LQDAFLRSSW ADRNPTEVEV PFETSVAGTV LRGRIDAVFT
DPDGGWTVID WKTGAEPSAA NEKAVVMQLA AYRLAWAELM DVPIERVRAA FHYVRTGRTI
APDHLPDADA LARLLRSAGS PDEEIRPDAE PSATR
//
