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ADDA_SYNWW
ID   ADDA_SYNWW              Reviewed;        1236 AA.
AC   Q0AXU8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=Swol_1146;
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen;
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68456.1; -; Genomic_DNA.
DR   RefSeq; WP_011640560.1; NC_008346.1.
DR   AlphaFoldDB; Q0AXU8; -.
DR   SMR; Q0AXU8; -.
DR   STRING; 335541.Swol_1146; -.
DR   EnsemblBacteria; ABI68456; ABI68456; Swol_1146.
DR   KEGG; swo:Swol_1146; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000001968; 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   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_0000379359"
FT   DOMAIN          2..457
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   BINDING         23..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1236 AA;  143767 MW;  0ECBB039DED9E286 CRC64;
     MAHWTIEQEE AINARNSNLL VAAAAGSGKT TVLVERIIQL VLRDRIDIDR LLIVTFTQAA
     AGEMRERINA AFFKELEKGR EDGHLRRQLY LLNRSSISTI HAFCSDVVRQ HFHLVNIDPH
     FRIADSTETE LIKMEVLEEL LDGEYEKGND GFLDLVEAFG SNKDDKPLEA LILRLHSFIQ
     SHPQPLSWLE EKIDNLALGE DNWAENPWAS ELSQQIKIEL SAAQDILNQA LKLSNKAGGP
     RGYLEAIESD QKWVELLLKA ADQGLPVLYS CLQQLSFTRL GRVSRDVDEN LKNQVKILRD
     ESKKILNAIN SLLGRDPLEY LQDLNEIYSL MKYLGEIIQS FAEIYQEKKR EKGIVDFNDL
     EHLALQILSN EAVAREYRDY YSYLFIDEYQ DSNLVQETIL NYIKKEDNLF MVGDVKQSIY
     RFRLADPSLF LEKQKSYPLQ DGSVNRRVDL NKNFRSHPEI LNAVNYIFRH LMSEELGEID
     YDEKSYLYPG LNTGQELKYQ EIDKASSQEG KEKENTAKRV EICILENNPD LITKLEENET
     EEREIPGEAE NDFIERIIEM DNTEIEALLI AQKIRQLIQE DIYDPELQCM RKIEYRDMVI
     LLRATRNSAG IFMEQLSAEG IPVYADASSG YFDTLELNLF INLLRLIDNK RQDIALLSVM
     RSPIGGFSID DFIKIRTKLI PRREKQPYSF YEAMEFYMED NNDDLKDRLV FFIQRLKEWE
     LESRIMALDE FMGKLFMDTG YYYYAGAMPG GGQRQANLRI LLHRAREFQK SSFKGLFSFI
     KYIEKIKSSG SDMGNACIIG ENDNVVRIMS IHKSKGLEFP VVILGGLGKN FNIRDSNENV
     LLHRKLGIGP RYINTQLRTY HDTIARLAIK NRIKLENLAE EMRILYVACT RPQEKLIMVG
     TTRQLESAWR RWSQPVNSYN QSRARSFLDW LIPIIMRHKK EGQYLREIAG GDWDREILWE
     DESRWKVKLI SPWQLTAEEI RKKEEKYEWE RLLEQGGYSC PSAESEEIIK RLNWKYPYQE
     AENIPAKLSV SQVSQISSGY LEDGAADTFL TRVPAFLSGE KDKKTRLSPA DKGSIVHLVM
     QNIDYRRVSR EDSINQQLGE MVEREILTSE QLAVVEVNKI WRFFQTKLGQ RVLQAKWLFR
     EAPFNLLIAA SEVFPALESQ EELLIQGIID LYFYEGEDIV LLDFKSDIVH HKSEEEILAP
     YRVQLKLYKR ALENITDHRV KESYLYFFDL NRAIRV
 
 
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