ID A0A1H3XIN9_9FIRM Unreviewed; 788 AA.
AC A0A1H3XIN9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=SAMN02745687_01341 {ECO:0000313|EMBL:SDZ99216.1};
OS Lachnospiraceae bacterium NK3A20.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=877406 {ECO:0000313|EMBL:SDZ99216.1, ECO:0000313|Proteomes:UP000199449};
RN [1] {ECO:0000313|EMBL:SDZ99216.1, ECO:0000313|Proteomes:UP000199449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NK3A20 {ECO:0000313|EMBL:SDZ99216.1,
RC ECO:0000313|Proteomes:UP000199449};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNQX01000016; SDZ99216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3XIN9; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000199449; 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:UP000199449}.
FT DOMAIN 5..285
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 286..567
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 656..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 788 AA; 90088 MW; EB30549977B23883 CRC64;
MSIYDTLNRE QYKACMRTEG PVLILAGAGS GKTRVITHRI AYLMEECDVN PWNILAITFT
NKAAGEMRER VDRLIGFGSE SVWISTFHSM CVRILRRHSD LIGYDHNFTI YDTDDQKTLI
RQICARMGID TKQLRERTIM SAISAAKDKL QTAINYKDTH KIDFEQQQIG DVYEEYERQL
RKNNAFDFDD LLMKTVELFN AREEVLANYQ ERFRYIMVDE YQDTNEAQFQ LVRMLAAKHR
NLCVVGDDDQ SIYKFRGADI RNILDFEKVY PDAMVVKLEQ NYRSTQTILD AANHVIRNNA
RRKDKKLWTD AGSGAKIHFR SFNTGIEEAS FIAEDVKKRI HENPSLHFRD FAVLYRTNAQ
SRLLEDRFVQ ESIPYNIVGG HNFYDRMEVK DILSYLRTID NGRDDINTQR ILNVPKRGIG
KTTSDRVMAY AQAMGISFME ALERLDDIPD ITRAKTKLQA FTDLIHRLRD EAKTSSVGDL
INAIVEETEY EQYLKDYDEE NSEDRMDNVG ELISKAAAYE QDAAEDAEGD GPSLSGFLEE
VALVADIDQL GDDDDRVLLM TLHSAKGLEF PFVYLAGMDE NIFPSYMSIN SDDEDGIEEE
RRLAYVGITR AKKDLTLTHA ASRMMRGEVQ FYGVSRFVLE IPEDLLDETP RAGRRVFGEE
KSPDDDADMP WSDGYREHRT PFAGRGTERA KASAKKDTRL KAVYVKPHTS EGRKPFIAKM
GSLDSLQKGL PAGVKPDYDI GDRVSHVKYG EGTVLSLEKG PKDYKVKVDF DEAGQKVMYA
AFAKLSKV
//