ID E4HNJ1_9ACTN Unreviewed; 1066 AA.
AC E4HNJ1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=HMPREF9607_02638 {ECO:0000313|EMBL:EFS91345.1};
OS Cutibacterium modestum HL044PA1.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium; Cutibacterium modestum.
OX NCBI_TaxID=765109 {ECO:0000313|EMBL:EFS91345.1, ECO:0000313|Proteomes:UP000003179};
RN [1] {ECO:0000313|EMBL:EFS91345.1, ECO:0000313|Proteomes:UP000003179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL044PA1 {ECO:0000313|EMBL:EFS91345.1,
RC ECO:0000313|Proteomes:UP000003179};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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 -!- 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:EFS91345.1}.
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DR EMBL; ADZU01000041; EFS91345.1; -; Genomic_DNA.
DR AlphaFoldDB; E4HNJ1; -.
DR PATRIC; fig|765109.3.peg.2485; -.
DR HOGENOM; CLU_004900_0_0_11; -.
DR Proteomes; UP000003179; 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 Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF59; 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 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}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
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}.
FT DOMAIN 2..284
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 291..625
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 467..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1066 AA; 115545 MW; 131495E2A3818761 CRC64;
MHGWDDPQAR VLADDADMVL VMGGPGTGRT SLCLEIAARH VASGGLLSDV LVLAQTRPSA
QALRTALVRR LAGAHLEPQV MTVHALARRI VASPSRRLLT APEQEFRMRE LLAARDMSDW
PDELRTCAGT AQFASDVRVM AARLRQEGCD PQDLTDAGVT WGVPEWRVLG PFLADYLDVL
DLEGTLDYAE AVHRARIALT RPGADIEVRS RIKLLICDDV VECDSSQIRF LSQIARCHIP
CVLTADPDQT IYGFRGAVAE RLDEVIDEFP DVSVHHLATN YRNSQHIAEV VESLRTRMPA
VPSSSQLRRR ANHSAVTEDG TVAAVRAPSM TRLVRKIAGT LRHAHVADGV AWRNMAVVTR
HGGELGIIAT VLAAEDIPVL RSRDEHALSD INAVTHIVNA LAIAVALASG RQPSDRDVAT
LLSNPLAGID RSLVHRLETW CRLVRGIDID WPLLGELGAD PMAAVAAERG NERPEDGSRA
EVDGRAEEAG KEGSETAHEA YSVPPGLRAL AQPLAMMVQR VQRAADLLRS DASCHEALWA
LWQGSSWTSS LRSRALAGDS AADRDLDGLC SLFDMADGAQ TMAGIAGARR LIEVVRQEQI
PADRARESDE DRDGVSVVTA HRVKGREFDV VAVCGLEEGN WPADNHTGSL VRADRWSPDS
LVAAPGWSEN LRAETRLLLV ACSRARRQLL LCTVESAEEG KRPSGLVAGL PHVEDHVDSL
NFTSLTELVG ELRRVVVDNS ELPGVRAEAQ ALLDDLRVEK HRGRQLVPQA DPSTWWCQGA
PHQADVAGEI ELSASHIGEL LTCPRRWFMT RRAGASSGSA FQASIGSLVH RICAENMGHW
SLPGALTELE EAWPEIDVTA EWQRNAKLAD AKAAVQRFDG WLQSRHRQLI GTEVRVDGTI
EVPSGTARVR GSIDRLERDA EGACYVVDLK TGASQSEETK RSHRLQIGVY QAVVASGGVK
TIGPKPVSGA ELVHLQIGAG KGKLSPKVDH QSGLADVPWP NEIDPVDGCR NWIEASVDKA
LRIVISGDYP AVVNRGCGHC PAKAGCPALV PMDPATARSN RRRNAL
//
