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Database: UniProt
Entry: Q5LY80
LinkDB: Q5LY80
Original site: Q5LY80 
ID   ADDA_STRT1              Reviewed;        1217 AA.
AC   Q5LY80;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-APR-2018, entry version 87.
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}; Synonyms=rexA;
GN   OrderedLocusNames=str1716;
OS   Streptococcus thermophilus (strain CNRZ 1066).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=299768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNRZ 1066;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D.,
RA   Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D.,
RA   Ngui K., Masuy D., Hancy F., Burteau S., Boutry M., Delcour J.,
RA   Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy
RT   bacterium Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(2004).
CC   -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA
CC       helicase and an ATP-dependent, dual-direction single-stranded
CC       exonuclease. Recognizes the chi site generating a DNA molecule
CC       suitable for the initiation of homologous recombination. The AddA
CC       nuclease domain is required for chi fragment generation; this
CC       subunit has the helicase and 3' -> 5' nuclease activities.
CC       {ECO:0000255|HAMAP-Rule:MF_01451}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC       {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}.
DR   EMBL; CP000024; AAV63236.1; -; Genomic_DNA.
DR   RefSeq; WP_011227531.1; NC_006449.1.
DR   ProteinModelPortal; Q5LY80; -.
DR   SMR; Q5LY80; -.
DR   PRIDE; Q5LY80; -.
DR   EnsemblBacteria; AAV63236; AAV63236; str1716.
DR   GeneID; 31940065; -.
DR   KEGG; stc:str1716; -.
DR   HOGENOM; HOG000285114; -.
DR   KO; K16898; -.
DR   OMA; KQSIYRW; -.
DR   BioCyc; STHE299768:G1G42-1640-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
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; IPR011604; Exonuc_phg/RecB_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   InterPro; IPR034739; UvrD/AddA_N.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   PANTHER; PTHR11070:SF14; PTHR11070:SF14; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
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;
KW   Helicase; Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN         1   1217       ATP-dependent helicase/nuclease subunit
FT                                A.
FT                                /FTId=PRO_0000379356.
FT   DOMAIN       26    487       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01451}.
FT   DOMAIN      515    799       UvrD-like helicase C-terminal.
FT                                {ECO:0000255|HAMAP-Rule:MF_01451}.
FT   NP_BIND      47     54       ATP. {ECO:0000255|HAMAP-Rule:MF_01451}.
SQ   SEQUENCE   1217 AA;  138351 MW;  F133F4E0E43988A9 CRC64;
     MLTKAFLSPA EIEERIAQEA ASDKDRKLTP EQIEAIYSNG TNILVSASAG SGKTFVMVER
     ILDMIGRGVG IDQLFISTFT VKAAGELKER LEKRLTKHLG QAETDEERAF LSDQIAKIGT
     ADIGTMDAFT QKLVNQYGYL LGVSPTFRIM TDLAEQTLMK NEVYADLFND YMQGKDAQLF
     QKLVRNFTGH SKTSKAFRDL VYDIYSFSQA TADPEKWLCQ NLLKGQIEAK PEQAKNELLD
     GLKDGLLADF LAFLRDHLGI AQREFAKAKY LNNVSDAIIL LEGSLINDQT DMEDLLKQLL
     TLSGGTGLTN MTRPKDEELK AYKEAYNKTK NEFVAQLREV DTQLTVLEVL TKHNDDILPM
     LELLQSFVLD FSDQYLQAKI QENTFEFSDI AHFAIRILEE NPEVAVSYRD RYHEVMVDEY
     QDNSHTQERM LELLSNGHNR FMVGDIKQSI YRFRQADPQI FNDKFQLFLE NPDAGKLILL
     KENFRSQSEV LDATNGVFSH LMDQEIGDIL YDKTHMLVAG SQKQKEPHPE NETEVLIYNS
     DESSTSEDEE GPDQAISSGE ISLVIKEIIK LHEQGVRFED ITLLAPNRNT YLDLMVSFEE
     HGIPLVPDEY KSSYLESLEV MIMLDTLRAI NNPLNDYALV ALLRSPMFNF NEDDLTRIAV
     QADKGQFYDK LLAAHTKSGL HPEVVMQGLE AKLTLFTETL ADWRDYSKCH SIYDLIWKIY
     NDRFYYDYVG GLPRAEQRQA NLYALALRAN AYEKTGFKGL SRFIGMIDKI IASGNDLEEV
     TDLVPKNAVS LMTIHKSKGL EFKYVFVLQM NRKFIGHSKD GLSGKYIINR EKGLGIKYLA
     DLKDQINTNL PKLNVVLETL TFQDNRREER RASISEEMRL LYVAMTRAEK KLYLVGKGSK
     ETLTQQYGTD VENNRLPVAL RDQIATYQDW IMALDTAFMR KDLKFTVRFV EDEELTPEAI
     GQVEVKAAVD ADDLSNNRQT EEIERALTVL ESVEKLNHLY APAIDLPSVR TPSQLKTFYE
     PIMDTEGVDI MDKKEGVQPL ETASTFELPD FGQKTKVTGA AVGSATHELM QRLTLSDTVT
     LQDLTQALSR VSASDQVKAR VQLEKLLGFF DTELGKLILA NRDKLRREAP FAMLAEDPAS
     KEDFVVRGII DGYLLLEDRI VLFDYKTDHF THPSELKTRY QGQMSLYAKA LSQAYQMEKV
     DKYLILLGGK DLEVVEV
//
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