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ADDA_ACET2
ID   ADDA_ACET2              Reviewed;        1251 AA.
AC   A3DH19;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Cthe_2039;
OS   Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS   103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=203119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC   B-4536 / VPI 7372;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA   Newcomb M., Richardson P.;
RT   "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL   Submitted (FEB-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 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; CP000568; ABN53248.1; -; Genomic_DNA.
DR   RefSeq; WP_020457694.1; NC_009012.1.
DR   AlphaFoldDB; A3DH19; -.
DR   SMR; A3DH19; -.
DR   STRING; 203119.Cthe_2039; -.
DR   PRIDE; A3DH19; -.
DR   EnsemblBacteria; ABN53248; ABN53248; Cthe_2039.
DR   KEGG; cth:Cthe_2039; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000002145; 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..1251
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379265"
FT   DOMAIN          5..481
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          526..824
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   REGION          544..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1251 AA;  143346 MW;  615624C9539ACD73 CRC64;
     MSERTKWTDE QWEAITGNEK SLLVSAAAGA GKTAVLVERI IRKITDEENP VDIDRLLVVT
     FTNAAATEMR ERIAQAISEK LEENPGSANI QRQLTLLGKA CITTIHSFCL EVIRSNFQQI
     NIDPGFRIAD ETESRLMKLE ALDEVFEEQY ENENEDFFEL LECYGGNRDD RALQDMVLNL
     YDFIQSSPWP EEWLEKMTES MNIPDGTDFG KTLWGSVLLS SVKIELEGLK EMISRALEIL
     KDASGLEKYR AVYMEDLANV DALLKLLNEE SEMQWDRIFN ALQGFEFATL PRCGREVDKD
     KQEIVKKIRD DVKQRIRKFR EKVITSVSNE IISDLKALYP KMKCLANLVK QLAEKYAEKK
     NRKSVVDFND LEHFCLEILT ERKEDGSIIP SRTAISYRER FAEILVDEYQ DSNLVQETII
     NMISKGDDAS PGVFMVGDVK QSIYRFRQAR PELFLEKYNT YLPDKGSPCR KIILSRNFRS
     RREVIDAVNF LFKQIMSTGA GELDYTDAEA LNFGAVFDEN AKEDITVGGE VEFHLIQTED
     EDKNFTFENE GEEGRQADEG EEDEEMLDSI QCEARLVGRR ILELMKPDEN GRYFSVFDKA
     KNEYRRVEYR DVVILLRTTR NWAEVFVDEL SVMGIPVFAD TGTGFFKTVE VQVMLSLLQI
     IDNPLQDIPL LSVLRSPIVG FTTDELAELR LVDKKALLFD ALKKLAESGQ GEAAGKASAF
     LENLQKWREM SLYMSTDRLL WQLYNDTGYY SIVGAMPAGE QRQANLRILY ERARQFEETS
     YKGLFNFINF IDKLKSSRGD MGSAKILSEN DNVVRIMSIH KSKGLEFPVV IVAGCGKKFN
     LQDMNKSILL HHELGFGPDV VDHKLRLSWP SVAKQAIREK IKAETLSEEM RILYVALTRA
     REKLVITGAV KNVRKAVEKW LDSASVQKSR LSAYDMLSGA NYLDWIGPAL LRHKNCGGLR
     DCVGSAGFRG LLIDDPSVWS VKIWNKTDVQ SSGVSEEQGE SEFIKWLDSL EKEEPSEYAE
     ETARRLSWSY PYVKASKVPA KVSVTELKRR YNEVVSEDVM QFPDYMPVLV KKPMFLEEKK
     GLTYAEKGTI LHFVMQHLDY GREDIEAQIE EMVAKDLLTP QQAQSVDAAR IRRFLNSPLG
     KRMLASKSIN REVPFNIEIP CHELYRDMED EACHGETLLL QGVVDCYFEE PDGIVLVDYK
     TDYVAPGNVE TIRERYKVQI LYYARALEML TGKKVKEKYI YLFWDGRILG F
 
 
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