ID D4BMW0_BIFBR Unreviewed; 1311 AA.
AC D4BMW0;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=BIFBRE_03407 {ECO:0000313|EMBL:EFE88997.1};
OS Bifidobacterium breve DSM 20213 = JCM 1192.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE88997.1, ECO:0000313|Proteomes:UP000003191};
RN [1] {ECO:0000313|EMBL:EFE88997.1, ECO:0000313|Proteomes:UP000003191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE88997.1,
RC ECO:0000313|Proteomes:UP000003191};
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., Nelson J., Hou S., 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 (FEB-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 -!- 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:EFE88997.1}.
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DR EMBL; ACCG02000009; EFE88997.1; -; Genomic_DNA.
DR RefSeq; WP_003828456.1; NZ_JDUD01000009.1.
DR STRING; 1685.RY69_1522; -.
DR KEGG; bbrd:BBBR_0429; -.
DR PATRIC; fig|518634.20.peg.454; -.
DR HOGENOM; CLU_003630_0_0_11; -.
DR Proteomes; UP000003191; 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; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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: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 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 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:UP000003191}.
FT DOMAIN 5..388
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 389..734
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1311 AA; 143275 MW; C14093068B4BA11B CRC64;
MSAFIPSVEQ AAIINAPAQD DVLVVAGAGS GKTFTMTQRI IALINRGVAP ERILGLTFTR
KAAGELLERV SAAVSREDSP AAQGAQTPGA STPNFDRAFL KPAIFTYDAF FQTIVRQYGL
LVGFDQNTQP LSEAGALQLA TEVIDEHMDQ ALSEDLGAFT SLARSVLALS GAIGSAMIGS
GCTGFDEAVE RVRQWDSAFV DALRLALENE DIPDIEPTIP KIKRLKKDSD TDWQAKLDDR
AQRLHARCAY HCAQLLEITR KREVLLQLVE AYAQAKRQKN MAEFSDFTIA AYQLIERFPS
IGERTRCRYS HVLLDEYQDT STTQAALLAA LFHVNNSERC AVNAVGDPFQ SIYAWRGASP
GAFRMFQRDF HMPAESKPFP LSVTRRNSRI VLEAANDLTL PLRSRPARPS SSLMREVDVS
SLDPMPDAPE GTLGVLGLAT AGQEIDAVVR FCKAAIARYR DAGAAQEAPV AVLFRSKSHM
PEYQEVLEKA GLTTFVVGYS ALLERPEIRD VLALLHVVAD HTDTGALMRL LATPRFGLSS
DDLTALACAA EAQNMEQRFR ALVQAGVAPA DTPRSQWGAV VREHRDQVAN AVFLPDLLMQ
DNSSVRLDQL SAYGRHAVEQ AVEALRQVHD MVGRSITDVI RAAIEALNLD IDTVLAGALR
DPQHRVNPSL ARMPMDSIVD LVDTYTQEIA VEQTPTLRGF MAWVDHLATV EDEAAKLPGS
PVDVELMTVH QSKGLEWDAV AVVGLNAGGF PSNQGDHLKV VLDDNHPGGT EQGQWTAPEY
HESADSWLTS PVAVPVPVRA DAGILPRFPH DADVHGDPID SLRNLDDVEL IDDEVFGSMR
EFGDGVEEVD PQSWYLTQSE EYGRRLHADE RRLAYVALTR ARNDALLTYC RYTGESSRDC
TNVPKGSRAA SPSNFWLEVH DALHGHDHAI EAQAYVEGLG SEVALVSPQG DPIDPPEGFI
VGENAEQYCD AVVGDAWRTP LEQTSGRNAL PWPASLGEDT AEHLTRGLAL VRNAINGKRN
AKDDGHNPAG PLLQRAQLLV DDDDLMTGTL EGAALDRAVK AKAQRILAAG RQNVTSLQAR
VGGMSQQEER FYWRSVIRPI PRVSSPAAEA GTRFHDWAER FINAGKPDEA ASSVDSSAAE
IITTGNGVSR SDLLADLNAI DQQSVPVCDR NLMMWQHRLA SSSWAQRTPV WAERSIAVDV
PEVGIVNGKL DAVFLGGINP ADTSKRYTVV DWKTGHRPTK PDDVEHKLAQ LDMYRLLLAA
VEGVELDSID ATLYYVSEPD EGLRELHARA KTKQEILTEL SSGIPEQSDN D
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