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Database: UniProt
Entry: A0A087DFA0_9BIFI
LinkDB: A0A087DFA0_9BIFI
Original site: A0A087DFA0_9BIFI 
ID   A0A087DFA0_9BIFI        Unreviewed;       532 AA.
AC   A0A087DFA0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=BISA_0238 {ECO:0000313|EMBL:KFI94200.1};
OS   Bifidobacterium saguini DSM 23967.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1437607 {ECO:0000313|EMBL:KFI94200.1, ECO:0000313|Proteomes:UP000029066};
RN   [1] {ECO:0000313|EMBL:KFI94200.1, ECO:0000313|Proteomes:UP000029066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23967 {ECO:0000313|EMBL:KFI94200.1,
RC   ECO:0000313|Proteomes:UP000029066};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) 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:KFI94200.1}.
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DR   EMBL; JGZN01000003; KFI94200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087DFA0; -.
DR   STRING; 1437607.BISA_0238; -.
DR   Proteomes; UP000029066; 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   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; 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; 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; 2.
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          21..323
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          324..532
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   532 AA;  58064 MW;  A106F42602A0122F CRC64;
     MRENWQRVTM ESMEQAQNIL EGLDERQRKA ATTLQGPVRI IAGAGAGKTR TVTRRIAYAC
     ATGAWRPEQV LAVTFSVKAA AEMRARLTQL GLADARGGAA GGVTAATFHS AALHQLNSVW
     EDVCDAPFPH LIEDQRDVVS RAITRVSANA DTDPIMVRDV LAEINWAKVS LIALQDYASV
     CMRAHHLPPA GLEPNRFADI YAAYEQEKTS RGEIDFDDIL LLVCHIMDDF PEAAAQIRSS
     IGWLTVDEYQ DISPLQHRLM TLWLGGGSLN DATILNRNVC VVGDPAQTIY SFAGASSWDL
     LRFADEFGPL AADIDLNTDY RSTPQIVSLA NKVLAAAPDR QDYLKLVSAR QSGARVSRTV
     YETDIEEAQG VVARILRLIQ QGAKPSDCAI LTRINAQQQV FAAALRQAGM KFRIRKDAGW
     QSSALADDAA SKRAILEALG LNASGNTLVE DPGVTISTIH ASKGLEFDHV FLIGCSEGLL
     PYGAPESGEA LEEERRLMYV GITRAQDSLH VSFARTKDGY GAQQRRPSRF LS
//
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