ID A0A0A2E3E7_9PORP Unreviewed; 782 AA.
AC A0A0A2E3E7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=HQ37_00745 {ECO:0000313|EMBL:KGN72172.1};
OS Porphyromonas sp. COT-239 OH1446.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1515613 {ECO:0000313|EMBL:KGN72172.1, ECO:0000313|Proteomes:UP000030150};
RN [1] {ECO:0000313|EMBL:KGN72172.1, ECO:0000313|Proteomes:UP000030150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-239 OH1446 {ECO:0000313|Proteomes:UP000030150};
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 sp. COT-239_OH1446 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:KGN72172.1}.
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DR EMBL; JRAO01000003; KGN72172.1; -; Genomic_DNA.
DR RefSeq; WP_036878866.1; NZ_JRAO01000003.1.
DR AlphaFoldDB; A0A0A2E3E7; -.
DR STRING; 1515613.HQ37_00745; -.
DR eggNOG; COG0210; Bacteria.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000030150; 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:UniProtKB-KW.
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|PROSITE-ProRule:PRU00560,
KW ECO:0000313|EMBL:KGN72172.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000030150}.
FT DOMAIN 11..295
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 296..578
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 782 AA; 88931 MW; 5EF4E715B84769A4 CRC64;
MHLFPNEDYP NELNAAQRAA VEYNDGPALV IAGAGSGKTR VLVYKILHLI RLGYDPSRLM
ALTFTNKAAR EMRQRIELII GPAARRLRMG TFHSIFLSIL RQHASLLGYS PSFSVYNSSD
SKNRIKAIIK QMSLDDKVYK PNAVAGAISR AKNRLISPEA YRANVEYLRL DAKAGLGRLW
EIYARYTQEL KQSNAMDFDD LLFEINILLR NHPDVLAYWQ GQIDYLLIDE YQDTNFAQYM
IARQLMQERG NIFVVGDDAQ SIYSFRGANL DNILRFRETF AGAKIFKLEQ NYRSSQTIVQ
AAGALIQHNK HQIPKEVFSL GEVGEAIELH EAFSGDMEAS WVCKRIDDLR RQTGATYDQF
AVLYRTNVQS RTLEQVFRRT GIPFRIYGGR SFFDHKEIMD VVAYMRLVVN PNDEEALLRV
INYPRRGIGE TTMAKLRQQA FEVGKPLMEV LQELELYELG ISRATQSKLS GFAALITELR
GLSESTADFY EGMQLMISRT GIPVDLMSDT SLEGKSRQEN IKEMLSGIEE YSRNAQEQGQ
EPSLEAYLSE IALLTDQDKK EHHTETGVTL MTIHAAKGLE FKHVFIVGLE EMLFPSILSV
ESEKDLEEER RLFYVAITRA EKTCHLGYAR QRFRNGRTEN TQPSRFLREL PPALLKRNSA
SIDTMVEFER SGWRQQRGYG RDQMASELPQ HFTSQSFLPP SPTGGKRRHI GRRVAGEDAE
PEVSHERIGD LRVGGRVRHR IFGDGQITAL EGLGDNAKAI VAFDKVGSKK LLIQFARLEP
LD
//