ID D3LN35_MICLU Unreviewed; 963 AA.
AC D3LN35;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=HMPREF0569_0172 {ECO:0000313|EMBL:EFD51134.1};
OS Micrococcus luteus SK58.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=596312 {ECO:0000313|EMBL:EFD51134.1, ECO:0000313|Proteomes:UP000002933};
RN [1] {ECO:0000313|EMBL:EFD51134.1, ECO:0000313|Proteomes:UP000002933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK58 {ECO:0000313|EMBL:EFD51134.1,
RC ECO:0000313|Proteomes:UP000002933};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (NOV-2009) 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:EFD51134.1}.
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DR EMBL; ADCD01000044; EFD51134.1; -; Genomic_DNA.
DR AlphaFoldDB; D3LN35; -.
DR Proteomes; UP000002933; 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 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 64..355
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 356..642
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 14..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..831
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..963
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 963 AA; 104570 MW; 016EB348243C16C2 CRC64;
MADLFSALGR TPLNLDRTRR PADPETALPG LVPPAVTRVA ADPEAWGEDA RPAAPAHTPE
SLVAGLNPQQ AAAVTHTGAP LLIVAGAGSG KTRVLTHRIA WLLATGRARP HEILAITFTN
KAAAEMRERV AGLIGPTAQR MWISTFHSSA VRLLRNEAAN IGLKSTFTIY DSADSLRLVT
TVAKQHELDP KRFAPKALLN RISSLKNELV EADDYAATVA EGDPWGRAVA AVYRGYTARL
RQANALDFDD LIGMTVHMFE AFPRVLDNYR RRFRHVLVDE YQDTNHAQYR LIRLLAGPAG
DPEGVETPGG ELTVVGDSDQ SIYAFRGADI RNIVEFEQDF TDAVTIKLEQ NYRSTQTILD
AANAVIERNP DRRPKRLWTA EGEGPAIVGY AAENESAEAE WIASTIDRLQ DEDGIRPADV
AVFYRTNAQS RALEERLVTR GIPYRVIGGT RFYDRKEIKD ALAYLRVIVN PDDDVNVRRI
LNEPKRGIGD RAEGAVAAWA ERNRSTFSAA LRDAENAPGM AARSLKAVRG FVQMMDDLGQ
VAESAGPATV LEAVLEQSGM LAALRESEDL QDESRADNLG ELVAVVRSFE TTHPDGTLSD
FLEQVALVAD ADQLPTAPDV EGEALAEQQG QVTLMTLHTA KGLEFPVVFL TGMEHGVFPH
ARSMTDEKEL AEERRRGLRG PDARPPSPVP DARRGTLAVG PAPVQPAQPV PRGDPGGAHR
LGAGGHHALG RLVEPDRRRH LALRGAVRGR AAGLAVPGRR RRAAPAPHPR GRAGGPHGAL
RRGAGEGAEP GAAAEGDRGA QPGRPRLPRD LRRGARGRRR GRRGQDRRDR HLRRHRGAEA
AAAALRPADE GRGLTGPARR PPGLSAVWTR VSRGTPPSAA LLCPRARPGH GGGVDVGRAR
GRGRQTLSST KKDTPPWTCM STRRAICSRR TASPCWPASL RRPRTRPRRP RRRSAASPSS
RRR
//
