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ADDB_DESAP
ID   ADDB_DESAP              Reviewed;        1165 AA.
AC   B1I494;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Daud_1277;
OS   Desulforudis audaxviator (strain MP104C).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Candidatus Desulforudis.
OX   NCBI_TaxID=477974;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA   Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT   "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL   Submitted (OCT-2007) 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; CP000860; ACA59788.1; -; Genomic_DNA.
DR   RefSeq; WP_012302373.1; NC_010424.1.
DR   AlphaFoldDB; B1I494; -.
DR   SMR; B1I494; -.
DR   STRING; 477974.Daud_1277; -.
DR   EnsemblBacteria; ACA59788; ACA59788; Daud_1277.
DR   KEGG; dau:Daud_1277; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   OMA; DRLENYV; -.
DR   OrthoDB; 1283891at2; -.
DR   Proteomes; UP000008544; 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; -; 3.
DR   HAMAP; MF_01452; AddB_type1; 1.
DR   InterPro; IPR014140; DNA_helicase_suAddB.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
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.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 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;
KW   Reference proteome.
FT   CHAIN           1..1165
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379188"
FT   DOMAIN          1..298
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   DOMAIN          279..584
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         800
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1119
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1122
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1128
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ   SEQUENCE   1165 AA;  129720 MW;  36FACEDE3303822E CRC64;
     MALRFILGRA GTGKTRLCLE EIRKELRQAP DGPPLVFLVP EQATFQTEYA LALTPGLSGM
     FRAQVLSFRR LAWRVFSEVG GAARPHVGDV GKRMMLARIL ARRRNELRLF GRAAGQYGFS
     GTLAGVLSEL KTYLVTPEAL EQAVRMLPGT AETDSLQAKL EDLRLLYTDF ERELAGKYID
     PDDYLTLLAA RLGESPTLRA AEVWVDGFAG FTPQEYAVLE ALLKAAARVN VALCLDPRSG
     RREDLELFQV TRDTRARLAE LARKNGVELE RPVELAGPPA RFRANPALAH LEREFFRRPT
     KKFAGPPENL RLVAAASRRA EVEGAAREIL RLSRERGWRW RDVSLVVRNL ADYHELVATV
     FADYGIPCFI DRKRPVRHHP LVELIRSALE TVTENWTYDP VFRYLKTDLV PVSRGDVDLL
     ENYVLAHGIK GAKWADPEDW HYRRSDALNR PVPNGTGAPA PSDRDRYLRE KVNRIRRRAA
     RHLLDFQRRV QAAGTVRELT AALYDLLSDL DVPGRIEEWS REAETEGRLE AAREHRQLWD
     GVVELLDQVV ETLGDEALTP EEYGRILDSG MDGLQLALIP PALDQVLVGS LERSRNPDIR
     AAFVLGVSEG VLPGRHGGTG LFTDREREVL LAAGLEVAPD TRRKVYEEQY LVYIALTRAG
     HYLWVSYPLA DEEGGALAPS SVIPRLRELF PGLREETLAL EPEGTAPGAD LPYVTAPGRT
     LGFLVTRLRD WKSGVTVDPV WWSVFNWFAA HAGWRERCAP VLAGLFYENR EPRLDPELTP
     ELYGSRLVVS VSRLEEFRGC PFAHFARYAL RLKERDVCRL AAPDIGLFFH AALKTFEDRL
     REAGMEWDAL ESADCTRLAS AVVEELAPQL QSEVLLSSPR LRFLTGKLER VVERTAGVMA
     AHARHSRFQP VAVEVAFGPG RDVPGPAYPL PGGGSVELAG RIDRVDVAHT DNAAYLRVID
     YKAGPRSLAL DDVYYGLNLQ LLVYLEAGLR EAAALAGREC RPAGAFYFRV QNPLLKGGTP
     VPPAEVAPRL LKAFRLQGLV LDDPALLRLM DDAIGSESAI VPAGLKQDGT VKKKPGVVSA
     AQLERLQEHV RRVVAETAAE IQAGVVAIAP YRKGQANACR YCAFKPVCAF DPLLESNRYR
     QLRALTAGEL WRLLGLPEED EPGDE
 
 
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