ADDA_CLONN
ID ADDA_CLONN Reviewed; 1236 AA.
AC A0PY67;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=NT01CX_1236;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK61679.1; -; Genomic_DNA.
DR RefSeq; WP_011721327.1; NC_008593.1.
DR AlphaFoldDB; A0PY67; -.
DR SMR; A0PY67; -.
DR STRING; 386415.NT01CX_1236; -.
DR PRIDE; A0PY67; -.
DR EnsemblBacteria; ABK61679; ABK61679; NT01CX_1236.
DR KEGG; cno:NT01CX_1236; -.
DR PATRIC; fig|386415.7.peg.346; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000008220; 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; 1.
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..1236
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379260"
FT DOMAIN 4..473
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 512..806
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1236 AA; 143760 MW; C298347A75141BB3 CRC64;
MGEVKWTKEQ QQAIDVHGCN LLVSAAAGSG KTAVLVERII KMITDIKNPV DIDRLLVVTF
TNAAASEMKE RIGKAIGKEL TKHPKSKQLQ RQLTLLNRAS ITTIHSFCLE TIRNNFHYID
LDPNFRIGDE TETVLLKGEI IEGIFEDLYE PENCTQEFLN LVEFYSSNKD DVALQNIVLN
LYDFVMSSKN PKKQLQDMAE QFNVDESYNF GESKWAKVLM DDVELELSGL KDMMEEALKL
INDTNGLDAY LEGFTDELLM INDLILNAKT SWDSLYNGLS EVKFGRLKTC RNCEDKKTQE
KVKDIRNKVK KQLQDEIKKK ITSYSTKEIV TDLRNLYPIM KSLCDLVIEF MDRYSKAKKE
RGIIDFNDFE HFCLEILGHE EVALKLRQKY IEILVDEYQD SNYVQEAIIN SIARRHEETG
NPINVFMVGD VKQSIYRFRQ AKPELFLKKY NSYLEGENAK ERKVNLFKNF RSRKEVLDGV
NFIFKQIMSE NIGELEYGDD EALYLGADFE QYEDKSLVGG PIELNLIEKS KDETKEEESE
EEEILSNIQV EARFVAKKIN ELVNPKIGEP FKVYDNELKA YRNVEYRDIV VLLRSTSNWA
PVFTDEMKEN LIPAYADVGN GYFETVEIKT ILSLLEIIDN PRQDIPLIAV LRSPIASFTP
EELIDIRLEN KDGDFYGGLL KVASSEDRDD NWILFKRKCN SFLEKLNYWR EKSIHMPIDE
FIWYLYMETG YYGYVGALAG GMQRQANLKI LFQRARQYEK TSYKGLFNFI NFINRLKVSS
GDMGSAKILG ENDNVVRIMS IHKSKGLEFP VIILSALGKN FNMQDLNKRI LYHDELGFGP
DYIDLDKRII YETVPKSALK KKIKLESLSE EMRILYVALT RAKEKLILTG AVNDIEKSAK
KWSYALEGED YKLSQYQVMT GKNYLDWICP VIMRHKDGEV LRELAGIEIF EKVNLLSDES
SWKITTDNIS GILQNDDETN EIILEDIKEI EDIEESSSYY DEINERLNFK YKYIESSKLP
TLLTVTELKR MKNSSMYEDY SRDMYTPKLV KKPMFMEKDK KLKGAEKGTA MHAVMQKINY
SEELTIEDIN RQMETMVEKE FITKEQADSV EAEKILNFFK SNIGKRLLKA ENVRRETPFH
MELKSTEIYE SLPKEIYENE NIMIQGIIDC YFEEEDGIVL LDYKSDYFKE GQEEAIIKKY
KVQIDYYARA IEELTGKVVK EKYLYLFYGD KEVEIK
