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Database: UniProt
Entry: A0A1H3XIN9_9FIRM
LinkDB: A0A1H3XIN9_9FIRM
Original site: A0A1H3XIN9_9FIRM 
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}.
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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
//
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