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ADDA_STRSV
ID   ADDA_STRSV              Reviewed;        1224 AA.
AC   A3CNT9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=SSA_1451;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/jb.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA   Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA   Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
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; CP000387; ABN44844.1; -; Genomic_DNA.
DR   RefSeq; WP_011837144.1; NC_009009.1.
DR   RefSeq; YP_001035394.1; NC_009009.1.
DR   AlphaFoldDB; A3CNT9; -.
DR   SMR; A3CNT9; -.
DR   STRING; 388919.SSA_1451; -.
DR   EnsemblBacteria; ABN44844; ABN44844; SSA_1451.
DR   KEGG; ssa:SSA_1451; -.
DR   PATRIC; fig|388919.9.peg.1376; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000002148; 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..1224
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379351"
FT   DOMAIN          26..491
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          519..809
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1224 AA;  139912 MW;  6E7DFE103418B867 CRC64;
     MKRIPFLTAE EIALKQAQEA ASDKPQKKTA EQIEAIYSSG RNILVSASAG SGKTFVMVQR
     IIDQILRGVA VSQLFISTFT VKAAGELKER LEKELGQALK EAESPELKQH LAQQLADLPN
     ADIGTMDSFT QKVLSRYGYL LGLAPNFRIL QSASEQLILQ NEVFSQVFDH YYDSERQALF
     SRLVKNFTGK RKDLSAFREQ VYRIYSFLQS TSSPQRWLEE TFLYGYEHSD FAAERERIFC
     QIKSALWELE TFFSAHLEHE GREFAGAKYQ ENVQDALTVL AGLNESSSIE ETAQILKQIV
     ALSQLSNGQA FTARVGKNAD ELKKEMAKDY NEARKPMIER LRSFDQQLYQ LDFIEQHQDE
     CLPLVELLRD FVADFAQAYL ERKKAENAFE FGDISHFAIE ILETFPEVRR FYQERYHEVM
     VDEYQDTNHT QERMLDLLSR GKNRFMVGDI KQSIYRFRQA DPQIFSDKFK AYQEDSSQGK
     LIVLKENFRS HLEVLEATND VFKRLMDEEV GEIDYNETHY LVAGNPAKRE PNPANRASFL
     IYEGSKESPE EEADEGLPQA VSAGEVDLVI KEIIRLHNEE GVAFKDITLL TASRTRNDLI
     LAAFEQHQIP LVPDDGAANY LQSVEVLVML DTLRTINNPL NDYALTALLK SPMFDFGEDE
     LARLSLQASQ ERSQENLYEK LVNALEGRGL NPALVTEELQ KKLQHFYETL QSWRTYSKTH
     SLYDLIWKIY QDRFYYDMVG TLVNGAQRQA NLYALSLRAN EYEKSSFKGL SRFIGMIDRI
     LENQHDLASV PVAAPKDAVR LMTIHKSKGL EFKYVFLLNM DKAFNRQDSS SAIILSRTKG
     VGIKYVADVS VSVKDSYAPN QLRISMDTLP YQQNLAELQL ASLSEQMRLL YVAMTRAETK
     LYLVGKGSQE ALDKRQWGKS QQGRLSASLR SQISNFQDWL YAIQDVFSDE NLAYETRFVT
     DEELTAEEIG RINEPVLFPA DDLADNRQSD DIRRALDILE SVDRLNSQYR SAIELPSVRT
     PSQIKKFYEP IMDTDGLDIM DERAAFRPQP SFELPDFGKK AKVTGAQVGS AVHELMQRIP
     LDSSPSMAVL RSALAQVQAD DAVKKQIQLS KIASFFETDL GRLLIENSDR VRREAPFAML
     KRDEASGQEF VLRGILDGYL LFEDRIILFD YKTDKYKDSS ELIARYRGQL DLYAQALSRS
     YGISQIEKYL ILLGGEQLQV VKVD
 
 
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