ID A0A0A2G403_9PORP Unreviewed; 788 AA.
AC A0A0A2G403;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=HQ36_03175 {ECO:0000313|EMBL:KGN97946.1};
OS Porphyromonas gingivicanis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=266762 {ECO:0000313|EMBL:KGN97946.1, ECO:0000313|Proteomes:UP000030134};
RN [1] {ECO:0000313|EMBL:KGN97946.1, ECO:0000313|Proteomes:UP000030134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-022 OH1391 {ECO:0000313|Proteomes:UP000030134};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas gingivicanis strain:COT-022_OH1391 Genome sequencing.";
RL Submitted (AUG-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:KGN97946.1}.
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DR EMBL; JQZW01000008; KGN97946.1; -; Genomic_DNA.
DR RefSeq; WP_036883410.1; NZ_JQZW01000008.1.
DR AlphaFoldDB; A0A0A2G403; -.
DR STRING; 266762.HQ36_03175; -.
DR eggNOG; COG0210; Bacteria.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000030134; 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; 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|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:UP000030134}.
FT DOMAIN 6..291
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 292..583
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 788 AA; 89227 MW; 086599BCAA646DA0 CRC64;
MIDYKQELNS AQAEAVLYDG GPALVIAGAG SGKTRVLTYK LAHLIECGYA PEKLMALTFT
NKAAQEMQQR VAQMVSAHAA SKMRVGTFHS VFARILRRYA PLLGFTPNFS IYDTSDSKSL
VKKIVKELNL DNRLYTPKLI LNRISTSKNR LITPQAYNSQ VDMVSYDKSN GITLINSIYE
LYTQRCKEAN AMDFDDLLFL FNVLLRDFPE VLQEIQESID YLLIDEFQDT NPSQYLIVRR
LVESKQRIFA VGDDAQSIYS FRGASMQNIL SFTQLFPEAR LFKLEENYRS SQNIVNLANS
LIEHNRERIP KKVFSRRPKG TKTILNGADS GYEEAQNVTT SIAHYKRENP LLPYNSFAIL
YRTNAQSRLF EEQLRTAGIP YKIYGGLAFY GRAEIKNILA YLQLILNKDN NEAFERAAKY
PKKGIGDKTL QAIYDRARGE GISLYRASQK LLLEQAPLPR AGAKNLALYL ELLGDISTPV
EGNFVDWIKY IVVRSGIVEA LRLDNTEESE TRLENVEEFV SSVQEFLTAT IESDLLFDPN
YSTPQDLLAL FLQGISLASD RDDEEQEEDR DAVHLMTVHA SKGLEYDYIY IVGLEEGLFP
SQRSEMDDNL EEERRLLYVA ITRAKEQCNL YFARYRIING NGAPMLPSRF LKELDASLLA
QEGIRPEEHR FLSLTSAPVP KRGIPAPKAQ KEERKGVPIL GGPMRQEVRP APPTTPRKNV
EMEIPQATIA IQSAEELSLG DRVFHKLFGE GIVKEIEGIK ENAIATIDFG RAGEKQIFLR
FAALKKFV
//
