ADDA_DESRM
ID ADDA_DESRM Reviewed; 1244 AA.
AC A4J4E3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=Dred_1416;
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC and an ATP-dependent, dual-direction single-stranded exonuclease.
CC Recognizes the chi site generating a DNA molecule suitable for the
CC initiation of homologous recombination. The AddA nuclease domain is
CC required for chi fragment generation; this subunit has the helicase and
CC 3' -> 5' nuclease activities. {ECO:0000255|HAMAP-Rule:MF_01451}.
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=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000255|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01451}.
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DR EMBL; CP000612; ABO49946.1; -; Genomic_DNA.
DR RefSeq; WP_011877765.1; NC_009253.1.
DR AlphaFoldDB; A4J4E3; -.
DR SMR; A4J4E3; -.
DR STRING; 349161.Dred_1416; -.
DR PRIDE; A4J4E3; -.
DR EnsemblBacteria; ABO49946; ABO49946; Dred_1416.
DR KEGG; drm:Dred_1416; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 4.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; DNA_helicase_suAddA.
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 PANTHER; PTHR11070; PTHR11070; 1.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR02785; addA_Gpos; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1244
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379269"
FT DOMAIN 4..475
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 515..816
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT REGION 538..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1244 AA; 141080 MW; 66072DE93E6E0323 CRC64;
MSDKKWTAEQ LAAITTRDTN LLVAAAAGAG KTAVLVERII GLITDPHRPV DVDQLLIVTF
TNAAAAEMRE RIGQALSKAL QENPHSKRLA RQLTMLNRAS ITTLHSFCLD LLRRYFYQLD
LDPGFRVADE VEAELLRLDV LEELFERRYN QDNVEVFARL VDSYGGQRDD SRLQDLVLEL
YRFSGSHPLP VQWLTSLAEN YVIPEGKTLD DQTWIVQIKK TIFQEVEGVL GLLKQAQWLA
KQPGGPEPYS KTLTEDIINI KPLTNNDWDA SWEKLYRSIT AIKWSKLSPC RGEIDDQLKN
KAQNLRNKAK EKFNDIINTY FSAEPTVILE DLRSLQPLIA DLAKLTIEFM ELYQKKKQAK
GLVDFGDLEH YCLTILLDKE NDAAEFRPSA VAIELQQQYA EVLVDEYQDI NAVQETILRL
VSKKNNRFMV GDVKQSIYRF RLAEPKLFLS KSELYANTDN CQGTRIGLSK NFRSRLEVVN
AVNFIFRQIM TKKAGEITYD ELEELHCGAD YPQAEDVKTA TGPVEVYLID RKDAQLEEQN
TDSAEEKLTD GEEQEDLDSD QAEARLIGRR IQAMVKGTDK AMGPEFKVWD KEIGKYRPVS
YRDIVILLRA TTGRANTFLE ELRTMGVPTY AEVGTGYFEA VEVETFLSLL KIIDNPRQDV
PLAGVLRSPV VGLKASDLAE IRLCSKEGDF YDAVRIAAAA DLGDVAVTLT KFLRQLENWR
SRARRDTLAD LIWLLYRETG YYDYVGGMVG GTQRQANLRV LYHRAKQFEA TSFRGLFRFL
RFVERLKDSG SDLGAARSLS ENEDVVRIMS IHKSKGLEFP VLFVAGLGKR FNMMDLNKDM
LMHKELGLGP QIIHLGSRVS YPSLPKLLIK QQIRKESVAE EMRVLYVALT RAREKLILVG
AVRDLEKSLE KWCTSTYQAG WTLPDAELMA AKCYLDWLCP AIARHHNGHE LRSLAKTEGQ
PFSEVATDPS AWQLVFQALK DIKNQTQENK EQSQGLLVKI KDMEPFEDAG LIKEVERRLS
WQYPRAEVTT RPAKAAVTEV KHKFDELARQ EAGVMSYRPK ISGRPRFLQQ DKGLTPAERG
SAIHLVMQHI PLDKLPDEEG VQVLLQNLIQ KEILLPQQAA AINPNHITGF FASSIGQRVL
QAPKVERELP FSLALPATEV YQELPECGDE MVLVQGVIDC LVDEGDGFLL IDYKSDAVYP
GQDSPVDRYR GQINLYARAV QDILGKPVKD RVIYLFNNGQ IVHI
