ID A0A0A2FJ78_9PORP Unreviewed; 779 AA.
AC A0A0A2FJ78;
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=HQ45_05035 {ECO:0000313|EMBL:KGN90167.1};
OS Porphyromonas crevioricanis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=393921 {ECO:0000313|EMBL:KGN90167.1, ECO:0000313|Proteomes:UP000030139};
RN [1] {ECO:0000313|EMBL:KGN90167.1, ECO:0000313|Proteomes:UP000030139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-253 OH2125 {ECO:0000313|Proteomes:UP000030139};
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 crevioricanis strain:COT-253_OH2125 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:KGN90167.1}.
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DR EMBL; JQJB01000006; KGN90167.1; -; Genomic_DNA.
DR RefSeq; WP_036888074.1; NZ_JQJB01000006.1.
DR AlphaFoldDB; A0A0A2FJ78; -.
DR STRING; 393921.HQ45_05035; -.
DR eggNOG; COG0210; Bacteria.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000030139; 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}.
FT DOMAIN 10..295
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 296..576
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 779 AA; 88404 MW; FB498B4AC56C258C CRC64;
MTEGQETYLD HLSPAQREAV EYISGPALVI AGAGSGKTRV LVAKVIHLLQ QGLLPQDIMA
LTFTNKAAKE MKERISRELN MRLPWNFRVG TFHSIFLREI RNHAERLGLK SDLTVYDTVD
QKSLVKLVVK DLLLDDKVYT PKFCLSRISN AKNRLIDARE YAENREFVAY DAKNRVGRFA
DVYSLYQSRL RASNAVDFDD ILVYTNVLLR DFPDLRDEMR AQTKYLLIDE YQDTNLAQYE
IAYRLMGENG KVFAVGDDAQ SIYSFRGANL DNILKFQQAF PTARLFKLEE NYRSTQNIVR
TANRLIARNT RQIPKEIYSS RPEGDEVEVH SCYTDITEAV YISEQLSELH QSEHIPFAQM
AVLYRTNAQS RLLEQELRKK SIPFHIHGGM SFFSYKEIKD IMAYLKLIVN PDDEEAIYRT
INFPRRGIGD TTIAKLRVLS REKGLSLSEL IASPARMSEA NIQRSAIVKI SGYVELLDRL
RQMAQDDLTA LVREVMSDTG IADFYFGDKS VEGISRQENI RELLSGIAQY QEAENEDGRV
PSLSSFLNDM ALLTDQDRSD EEEDQVTLMT IHAAKGLEFP YVFVVGLEEN LFPSSLCNTP
GEMEEERRLL YVAITRAKEK CVLTFAHNRY QSGRSEMRAP SRFIKELQGE GCRTAGKLSN
LGVFSGLKDQ YGNGQERPEW MLRPATDMEH APEHQPKTSG RKLRRISSGG NLLAKSFGET
QEGETEDFAV GDRVLHSRFG AGVVTSLDGL GSDARATVLF DTVGQKLLLL RFAKLKRIG
//
