ID F9VI36_ARTSS Unreviewed; 1193 AA.
AC F9VI36;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=SFBM_0011 {ECO:0000313|EMBL:BAK55794.1};
OS Arthromitus sp. (strain SFB-mouse-Japan).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1029718 {ECO:0000313|EMBL:BAK55794.1, ECO:0000313|Proteomes:UP000001636};
RN [1] {ECO:0000313|EMBL:BAK55794.1, ECO:0000313|Proteomes:UP000001636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-mouse-Japan {ECO:0000313|Proteomes:UP000001636};
RX PubMed=21791478; DOI=10.1093/dnares/dsr022;
RA Kuwahara T., Ogura Y., Oshima K., Kurokawa K., Ooka T., Hirakawa H.,
RA Itoh T., Nakayama-Imaohji H., Ichimura M., Itoh K., Ishifune C.,
RA Maekawa Y., Yasutomo K., Hattori M., Hayashi T.;
RT "The lifestyle of the segmented filamentous bacterium: a non-culturable
RT gut-associated immunostimulating microbe inferred by whole-genome
RT sequencing.";
RL DNA Res. 18:291-303(2011).
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};
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DR EMBL; AP012202; BAK55794.1; -; Genomic_DNA.
DR RefSeq; WP_014017786.1; NC_015913.1.
DR AlphaFoldDB; F9VI36; -.
DR STRING; 1029718.SFBM_0011; -.
DR KEGG; asf:SFBM_0011; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000001636; Chromosome.
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 GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 2.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR014152; AddA.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR02785; addA_Gpos; 1.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 1..451
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 471..793
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 22..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1193 AA; 141100 MW; 2C5DDDF8A5F0A574 CRC64;
MDFSKNQKNV IELINGDLLV SASAGSGKTA VLVQRIINLI LNYCVSINEI LVITFTNAAA
VEMKERIVKA LEDNINDINK HILEEQLMLV SNSNIQTFHS FCLDILKNNY YKLNLGSNFK
IIKDSHRKML IGDALDDTFN FYYENEDEDF LTIVNIYGGK YSDVKLREII VYIYEFIQNI
VDIDGFIEKS TDIYIIKDND DIFSTKLGKV LRLRLINKFT LYKKKLIDFL LGISNNKKVY
SIIENDIFII NSFIKRLNNS YEDVYEYIYS FNFLRLSKLC DDYKEIRSGL KDFIDSLKKN
IFIVSENILK LQIGDLKNIV IKLFEIVCKF KEKFELGKLS ENYVDFNDME HLVIKLLNDT
RICDNYRNKF KYIFIDEYQD TNYIQEYIIN KIKNNYNVFM VGDIKQSIYG FRGAKVDLFS
KKYKNFKKVD DITFVEGNEN KILLYDNYRS RNEVISFVNF IFENIMIDGI SNIEYTPEEY
LNCASDYKVI KNNNENCEGE VTLSIIINDE KNSDIINEME DVECSLIIEY INKLINSEDT
IYKIYDKSIN GYRKIEYKDI VILVRNVNGA CISKLLHEEL EKNNIPSYFD GGDQFFDCIE
VITILSLLKV INNPTDDVDI LTVLKSEIFN FSNNDLAYIR IVNNDEYIYK NIKYILNLNC
CVENRVFLND EFSITYDRFK ILYDKCMFFV EKINEYREKS LFMKIDEFIW FIYKDSKYYF
LLSTMEDGLT KQSNLRIIFN KAKEFRVASF SGLFNFIEYL KYSKKFGDDI LVPKNISENE
NVVRIMSIHK SKGLEFPVVI LCNTSGRFNF KDLNNSIILH DEFGIGLNHI DYNLNLETDM
FIKNIIKEDH KDNIISEELR ILYVALTRAK EKLFITGTYN SDKDFQRVAD IYKCKSYLDF
LCNSLMKHRD GYILREYKGE NGLHNDLNKC EFKINVYNKS DFLKGEKHDS ENDDINLESI
MERESSSYNH INDIFNFKYD YDDVINMPIN LSVSEILSYD EEEKLNINFK VPKFIDDSKN
EKLYTALDIG NLYHFFMQNI VLGPSMVYDY LESELNRMVK CEMLSNDDIK YLNLNKILKF
FESNLGKRVI ECFNKDRRKV YREFEFLMNH RVDKINKNND LRIQGIIDLF FFDGDNIVLI
DYKTDKHIFN NKVIPNKYKE QLYYYKIALN KIFNLDISES YIYSFENNKA FMV
//
