ID D4BP62_BIFBR Unreviewed; 901 AA.
AC D4BP62;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=BIFBRE_03870 {ECO:0000313|EMBL:EFE89449.1};
OS Bifidobacterium breve DSM 20213 = JCM 1192.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE89449.1, ECO:0000313|Proteomes:UP000003191};
RN [1] {ECO:0000313|EMBL:EFE89449.1, ECO:0000313|Proteomes:UP000003191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE89449.1,
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 -!- 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:EFE89449.1}.
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DR EMBL; ACCG02000009; EFE89449.1; -; Genomic_DNA.
DR AlphaFoldDB; D4BP62; -.
DR STRING; 1685.RY69_1099; -.
DR PATRIC; fig|518634.7.peg.921; -.
DR HOGENOM; CLU_004585_3_1_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:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_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; PF21196; PcrA_UvrD_tudor; 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|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:EFE89449.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000003191}.
FT DOMAIN 27..338
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 339..619
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 738..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 901 AA; 98529 MW; 41292D713D3079B9 CRC64;
MNVAIQREAT VYDEPEVIAR SAQELVGDLN PQQAEAVQYR GQALLIGAGA GSGKTRVLTR
RIAWILSQFG AWPSQILAIT FTNKAAVEMR ERLGSLIGPV AQRMWVSTFH SACVRILRRD
GKSIGLKSGF SIYDSADSER LVKIIATEFN LDIKRYTPRS ILGHISDLKN NLTGWKENLA
VHAPDFTPGQ RGYQFGTVGD LEAIYAVIYA EYEHRLALAN AVDFDDLIGR TVELLRTDPA
VAEYYHHRFR YILVDEYQDT NHAQYVLVRE LAGVDTGEKA IPGSPNAGKS GPAWITVVGD
SDQSIYAFRG ADIRNIQDFE QDFPNAKTIM LEQNYRSTQT ILDAANAVIS NNEGRKPKKL
WTALGKGEPI VGYAADNAQQ EAQWVATEIA RLHAEEDIAY SDMAIMYRAN AQSRSLEEAL
INAGLPYQLV GGTKFYERRE IKDALAYLQA LVNPDDDVNL RRILNVPKRG LGNRAEGILL
AYARERGTSF FYALMHLDEI QDVPTRTATQ LKAFRDLMGE LSQFTRAHDA KPSEIVAEVL
EKSGLRAELE KSVDPQDASR LENLSQLQST AAEFEQNTPD ATLSAFLETT ALVADSDQLP
GEAEDSGKVT LMTLHTAKGL EYPVVFLTGM EQGTFPHSRS MEDTTELQEE RRLAYVGITR
AKQRLYVTRA AVRSQWGQAA DMMPSQFLDE IPDSLIDWKR REAGVERMRA NWESDGFADD
YGGWDDDDFG GTTFGGSSTF GSRGSGSSYG SRSHYGSSSY GSGSSYGSRS GGSSYGSRSG
SSYGSRSRSG SSYGSGSGSS YGSRSRSGPA SGGTRAGKVT TRHTTPKSGS AGSSMPSSKL
AKDNGLNISD FAVGDMISHD QYGLGKVTDA QDKGRNSVIT VDFGSAGVKR LMLRVAPIEK
L
//