ID E5BDJ5_9FUSO Unreviewed; 717 AA.
AC E5BDJ5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN Name=pcrA {ECO:0000313|EMBL:EFS21121.1};
GN ORFNames=FSBG_00618 {ECO:0000313|EMBL:EFS21121.1};
OS Fusobacterium gonidiaformans 3-1-5R.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=469605 {ECO:0000313|EMBL:EFS21121.1, ECO:0000313|Proteomes:UP000002975};
RN [1] {ECO:0000313|EMBL:EFS21121.1, ECO:0000313|Proteomes:UP000002975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_5R {ECO:0000313|EMBL:EFS21121.1,
RC ECO:0000313|Proteomes:UP000002975};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E.,
RA Nusbaum C., Galagan J., Birren B.;
RT "The Genome Sequence of Fusobacterium sp. 3_1_5R.";
RL Submitted (FEB-2009) 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}.
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DR EMBL; GG657971; EFS21121.1; -; Genomic_DNA.
DR RefSeq; WP_008801192.1; NZ_GG657971.1.
DR AlphaFoldDB; E5BDJ5; -.
DR HOGENOM; CLU_004585_5_2_0; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000002975; 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; 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; 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|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}; Reference proteome {ECO:0000313|Proteomes:UP000002975}.
FT DOMAIN 5..283
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 284..557
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 717 AA; 82235 MW; BE8DB5E3E30A7EEB CRC64;
MSLLEKLNDK QREAAATVEG PLLILAGAGS GKTRTITYRI AHMIEELGIP PYLILAVTFT
NKAAKEMKER VISLIGEEAE RATISTFHSF GVRLLRMYGS KLGYQANFTI YDVEDQKRII
KGIMKELNLQ NTDLSEKKLA SLISKLKEEG VSADDYEKDA YEYEAKTIAE IYRRYNIKLK
NQNGIDFSDI LLNTKNLLEI PEILEKIQTK YQYIMVDEYQ DTNNIQYQIV NKIAQKHRNI
CVVGDENQSI YGFRGANIQN ILNFEKDYKD AMVVKLEQNY RSTAIILDAA NAVIRHNTSS
KNKNLWTDKK EGDKIKVFKA LNQRDEVEKV ISEIAKEKQK GRAYRDMTIL YRTNAQSRVF
EEAFLRYRIP YKIFGGMQFY QRAEIKDILA YLSLINNPLD ETNLLRIINV PKRKIGDKSI
EKIRFFAREQ GLTLLDSLAR AGEISGIGSG LAVTIQQFYT LIRELMDLAP YENTSIIFSS
LLEKIGYKQY LETAYEDAEV RISNIEELGA SILELENLLG NLSLRDYLEN VSLVSATDDL
QENQDYVKLM TIHNAKGLEF PVVFLVGVEN ETFPGNSKFS SEDDLEEERR LCYVAITRAE
ERLVISFSTT KYVYGEVQAS QESIFLKEIP SEYKLEDWKE ERPKYQKLQT KNTISTEDLK
KKTSNLPFSV GERVLHKKFG LGIVRDLEEK KIIVEFVTGK KEIAAIVAEK FLSKAES
//
