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Database: UniProt
Entry: D6E6Y2_9ACTN
LinkDB: D6E6Y2_9ACTN
Original site: D6E6Y2_9ACTN 
ID   D6E6Y2_9ACTN            Unreviewed;       732 AA.
AC   D6E6Y2;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=GPA_05160 {ECO:0000313|EMBL:CBL03479.1};
OS   Gordonibacter pamelaeae 7-10-1-b.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Gordonibacter.
OX   NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL03479.1, ECO:0000313|Proteomes:UP000008805};
RN   [1] {ECO:0000313|EMBL:CBL03479.1, ECO:0000313|Proteomes:UP000008805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT   "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL03479.1, ECO:0000313|Proteomes:UP000008805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA   Pajon A.;
RL   Submitted (MAR-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}.
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DR   EMBL; FP929047; CBL03479.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6E6Y2; -.
DR   KEGG; gpa:GPA_05160; -.
DR   PATRIC; fig|657308.3.peg.92; -.
DR   HOGENOM; CLU_004585_5_5_11; -.
DR   BioCyc; GPAM657308:GPA_RS02395-MONOMER; -.
DR   Proteomes; UP000008805; Chromosome.
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; 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:UP000008805}.
FT   DOMAIN          20..307
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          308..576
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   732 AA;  82951 MW;  1771340F48C03D95 CRC64;
     MEQMIETAAS DQPDGAGAPP RLNAAQREAV TTTEGYVRVI AGAGTGKTRA LTERFAYLVN
     ELGIMPGNVL CATFTNKAAG EMRRRIRRLT GDNDTGYINT FHGFCVSVLQ EDAHALQYPK
     SFLVLDNADI DAMLQVVYEE RGLTLRDMTF AKARDMIEIM KLKERPGYYR DMLAMPLEDL
     RQKYLDAEAA KDIIFYGYLY QEKKCFGLDY NDLIVFVLYL FEQNPAIRSK WQRRLEYVMV
     DEFQDIDGLQ HELMEVLAGY HKNLFVVGDP DQTIYTWRGA DVRYLLDFDK RFPKTHTVMM
     LENYRSAPRV VAVANSLIEK NRERMPKRLV AARLAHGPTV WHHAKSAADE ADWIAQGALA
     LHVEGVAFRD MAVLYRAHYA SRPVEEALLR AEVPHAVHSG VPFFGRREIK DALSYLRLVA
     YRDDLDFARV ANVPKRNLGQ RRMAFLRQQA DERGCSLYEA LALAADDDLF KRTKARQLLD
     LIERFHSSYE GRPVSEVLAA VLSESGYERA LRTEGSQERL DNLAELKQSV YEFETTCGEE
     VTLEHYLAHV ALFSNADAMD DAQDKVRLMT VHAAKGLEFR HVFLCSMSEG VLPSRKTSTP
     QGMEEERRLA FVAMTRARDG LYLTEAEGRS HEGAARYPSR FLLDIDPAAL EFSDKPSDPQ
     MADARSVYAL TDRWIADLVR DARFSVGDRV VHAVFGAGRV SAVDTGKRAY EVEFDGMDTP
     RTISFKAKLE EA
//
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