ID A0A1W1VUD4_DESTI Unreviewed; 1113 AA.
AC A0A1W1VUD4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE Flags: Fragment;
GN ORFNames=SAMN00017405_1569 {ECO:0000313|EMBL:SMB96504.1};
OS Desulfonispora thiosulfatigenes DSM 11270.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulfonispora.
OX NCBI_TaxID=656914 {ECO:0000313|EMBL:SMB96504.1, ECO:0000313|Proteomes:UP000192731};
RN [1] {ECO:0000313|EMBL:SMB96504.1, ECO:0000313|Proteomes:UP000192731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11270 {ECO:0000313|EMBL:SMB96504.1,
RC ECO:0000313|Proteomes:UP000192731};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00560}.
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DR EMBL; FWWT01000023; SMB96504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1VUD4; -.
DR STRING; 656914.SAMN00017405_1569; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000192731; 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 GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR Gene3D; 1.10.274.50; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR HAMAP; MF_01451; AddA; 1.
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 3: Inferred from homology;
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}; Reference proteome {ECO:0000313|Proteomes:UP000192731}.
FT DOMAIN 1..372
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 401..686
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:SMB96504.1"
SQ SEQUENCE 1113 AA; 129869 MW; 9CCF688B93B2F8C4 CRC64;
LNNASITTLH SFCLEIVREN FFMLDIDPNF RIVNDTEGEL LRFDAVEEVL EEHYINSKED
DLFLKLIDAY GGEKDDSIVK ELILNLYEFS GSNPWPEKWL DESSENLSHL DWFSYLLPLV
KVEFKECENL LIKALSLANS SKGPLAYTKV LNEDLACIED LIGACNKSWD LIYNSLEEQQ
FARLPSIKKN DDVDPDLKEL VQGLRDEVKK KISKIENKYF MHNSEVLEAD LLVVKPMMKV
LIQLVKDFKT AYWNKKQKRN VLDFTDLEHF CLQILLEKDS SFQNLNASKV CLRLKENYEE
ILVDEYQDIN DVQETILHLV SKNNNRFMVG DVKQSIYRFR LANPELFIEK YRNYEKSPQD
IRIDLSKNFR CREEIVDGVN FIFSQIMNTE FGKIDYDDKA KLILGASYPD IAEESSIKGA
IEVHILDKKT DDEQNYLQRE ASLVGRKIKE LLKKESKIFD KNIGEYRNLT YRDIVILFRS
PRGNAEFFLE EFRSLDIPVY AELGSGYFDA TEIKVMLSLL KIIDNPYQDI PLASVLRSPL
IGLNTEELSI IALNNKEKNF FEAVKQTAVQ NQDELSQKLN DFLLNLDKWR TLARHGNLAD
LVWDLFLDTG YYEYVGGMPG GNQRQANLRV LHERARQYEE TSFRGLFMFL RFIERLRENK
GDMERARALG ENENVVRIMS IHKSKGLEFP LVFVVGLGKN FNLTDLNKDI ILDKDMGLGP
MYIDIDKRIK YPTIAKLVIE NKLKIETLAE ELRILYVALT RAREKLVLVG SISNIDKKAD
EWSQLIDNEQ VRLTFYNLVN SKNYLDWIGP CLARHTDGEN IRNLSALSIN SILKDNSKWE
VTLYQSENEI EKDEIKKTNE DLLEKINYLK PIEVESAKVI EVSKRLDWQY LFQSSLGKEA
KLSVTEIKDK FKKPVSENKK DKKEETKIYT NFNRRPNFMQ KEKGLTALEK GSAIHLVMQH
IELNQEITKD YLNNLVNFLI NQEILTNEQS RAVDLDLIIN FFKSKLGLRM KQSKNVKREL
PFSLTLPANM YYEDVENEKI LVQGIIDCLW QEEKGFILLD YKSDYVTRDN IPELVNRYEG
QINLYTKAIE KIYKEPVVEK YIYLFNLQEA IKM
//
