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Database: UniProt
Entry: D4BP62_BIFBR
LinkDB: D4BP62_BIFBR
Original site: D4BP62_BIFBR 
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
//
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