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ADDB_CLOK1
ID   ADDB_CLOK1              Reviewed;        1150 AA.
AC   B9E0C6;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01452};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01452};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01452};
DE   AltName: Full=ATP-dependent helicase/nuclease AddB {ECO:0000255|HAMAP-Rule:MF_01452};
GN   Name=addB {ECO:0000255|HAMAP-Rule:MF_01452}; OrderedLocusNames=CKR_0900;
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016;
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) 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 AddB nuclease domain is not
CC       required for chi fragment generation; this subunit has 5' -> 3'
CC       nuclease activity. {ECO:0000255|HAMAP-Rule:MF_01452}.
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_01452};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP-
CC       Rule:MF_01452}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01452}.
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DR   EMBL; AP009049; BAH05951.1; -; Genomic_DNA.
DR   RefSeq; WP_012101368.1; NC_011837.1.
DR   AlphaFoldDB; B9E0C6; -.
DR   SMR; B9E0C6; -.
DR   EnsemblBacteria; BAH05951; BAH05951; CKR_0900.
DR   KEGG; ckr:CKR_0900; -.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   Proteomes; UP000007969; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008409; F:5'-3' 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-EC.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_01452; AddB_type1; 1.
DR   InterPro; IPR014140; DNA_helicase_suAddB.
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   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02773; addB_Gpos; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; ATP-binding; DNA damage; DNA repair; Exonuclease; Hydrolase; Iron;
KW   Iron-sulfur; Metal-binding; Nuclease; Nucleotide-binding.
FT   CHAIN           1..1150
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379178"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         789
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1109
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1112
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1118
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ   SEQUENCE   1150 AA;  133639 MW;  F9EE18D0E9A5A5CC CRC64;
     MSIRFIYGRA GSGKSHYCLE DIKRRIQEVN DRNLILLVPE QFSFQAEKNL IKSIGEKGTL
     KAQVLSFRRM AEKVFDEVGG GIKKYINDAG KNILLYKIIE ENKNKLKVYK TSAKKQGFVN
     LVSDIIGEFK KYNISPEFLK ENLDSIENKS LKNKLEDIGM LFLEFQNRLS KNYIDLEDTL
     HILCEKLDKS IIFKNSEVWI DEFSTFTPQE YSIIEKIMCS AYRVNITLCM DALGEYSERE
     SIDLFLPIKI TERNILQIAE KNNIIYQKPV NLRCSPCYRF KNSTALQHLQ HSLFSYPYKN
     YEKSTEDINI FKALNKYTEI DYIARDIVKA CRDKNLRFKD MAVVTGDLDE YENLIKAVFN
     QYDIPYFIDK KREIIHNQIV ILIISAVEIL AKNWSYESVF RYLKTGLLDL EFDDIDILEN
     YVLANGIRGR QWLDTKPWSF KINYGNFKED DSEEEQEYLN KINCIRDKVR EPILKLSNDI
     KGKKKGRHIC EELYNFLCEL KIPEKVEELI IEFRNTDRLD KANEYSQIWD IVVDVLDQIV
     DVLGEQSFGM EIFNEALEIG FSQYEIGVIP PALDQVLVSN ITRIKSYNIS ALYIAGVNDG
     IFPVTISPEG IFTDQDRDEL KQNGLEIAPN TRSRAFEEQF LIYATLTIVD KYLTLTYSMS
     DEEGKAKRPS VVISMIKKIF PKLQEKSNLL DASGYEGGIE AVNSPKVTFN MLISNIRRNL
     GHRENINSLW IDVYRWYREH EIWNKRLDTV LGAFYYNNEI KISDLVKIRR LYGKHLNMSV
     SRLEKFAQCP FGYFVQYGLK VKDRKMYSLS APDLGSFMHG ILERFSIGLK QKSLTWENVD
     ERCCEENIND LVDNVLYDNP NSILNSSKKY KHVTDKLKKT LTRSVWLIAQ HMKKGRFIPR
     AYELVFGEIG DFPPISIELD SGEKVSLTGK VDRVDTAKED IITYIRIVDY KSGTREFKLS
     DVYYGFQLQL LIYLDAILTE FDKMTKGKSI PAGLLYFKLE DPIVRTKENI PDHEIEDRIT
     KSLKMNGLLL NDVNVIRQMD TSMEKSSDII SVSIKKDGNL SKSKSSLATR KQFEILRKYV
     RSTIADLCKK ILTGNIEVTP YKNKTKNGCS YCEYSAICQF DTSIKGNKYR IIEDKSDEEI
     WKHIENKVQE
 
 
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