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ADDA_GEOTN
ID   ADDA_GEOTN              Reviewed;        1242 AA.
AC   A4IKW7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=GTNG_0589;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(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; CP000557; ABO65971.1; -; Genomic_DNA.
DR   RefSeq; WP_011886886.1; NC_009328.1.
DR   AlphaFoldDB; A4IKW7; -.
DR   SMR; A4IKW7; -.
DR   STRING; 420246.GTNG_0589; -.
DR   PRIDE; A4IKW7; -.
DR   EnsemblBacteria; ABO65971; ABO65971; GTNG_0589.
DR   KEGG; gtn:GTNG_0589; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 137860at2; -.
DR   Proteomes; UP000001578; 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.
FT   CHAIN           1..1242
FT                   /note="ATP-dependent helicase/nuclease subunit A"
FT                   /id="PRO_0000379273"
FT   DOMAIN          12..487
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   DOMAIN          514..808
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ   SEQUENCE   1242 AA;  141543 MW;  EB322B798EE48052 CRC64;
     MNATFRPKPA GSRWTDEQWK AIAAGGRDIL VAAAAGSGKT AVLVERIIQK VTAEEGAVDI
     DRLLVVTFTN AAAAEMKARI GEALERELAN RPHSLHLRRQ LSLLNRASIS TLHSFCLDVI
     RKYYYLLDLD PSFRIADETE IELLKEDVLE ELLEEEYGKA DNERFFAVVD AYTGDRSDAE
     LQEMILALYE FSRSHPAPDE WLADLVSMYD VDEQTNVETL PPARYIAQHA AMELAAAKRF
     IGLALALAEK ESGPKPYEKR LREDMDLIAD LERRLSGSWD ELYHALQSLS FGRLPPCRGD
     GFDAELIDEA KSLRDQAKKK IEALRDNVFS LHPSAWLRHM REMKPVVETI AALVRRFSAM
     FEAAKREKGI VDFSDLEHYC LRILRQYDPE TGEWQPSSAA LEYQAQFDEV LVDEYQDTNL
     VQETILQLVK KGSERTGNLF MVGDVKQSIY RFRLAEPMLF LDKYKRFTAD GEAGGMKIDL
     ASNFRSRAEV LDGTNFLFAQ IMGEAVGEMV YDEAAQLKYG ADYPEGTDAV PEVMIIDRQR
     TSEEDEEETA ELEAAELESR LMAEKIKEIV SRPFYVYDRS SGQQRRAMYR DIVVLVRSMT
     NAPQMIEQLQ AQGIPAAADL SSGYFQATEI SVMLSLLKVI DNPYQDIPLA AVLRSPLFRF
     DENELAMIRL SDPKGTFFEA LQAFCQKTAE TGEEENAKEK AISFLNKLEE WRTMARRRSL
     ADLIWQLYRD TQFYDFVGAL PGGKQRQANL RALYDRARQY ESTSFRGLFR FLRFIERLQE
     RGDDLGAARP LGDQEDVVRV MTIHSSKGLE FPIVFLVGLA RPFYTRDLHS PYLLDKELGF
     AARFVHPRLR ISYPTLPLLA IQVKKRLELL AEEMRILYVA LTRAKEKLYL LASVNDADKE
     IEKWKGVAAE SGWLLPDDVR ASARSYLDWI GRALIRHRDG RSLVEVNRPD EIASHPSVWR
     FEIVSAAKLR NAEVSTDRED GGALVALEQG RPVPTQGEWE EEARRRLLWR YRYGKETVVR
     AKQSVSELKE QQALFGEQAD EWLPRKGTAP LFSRPRFMQE KTLTPAEKGT ALHVVMRHLD
     LHAPMDESSI RSQIIRLVEK ELLSAEQAET VDAAAIVAFF ATDIGRRLCA AREVYREVPF
     SLGLPADELY GSEGMESGRR LLVQGVVDCV FADERGYVVI DYKTDEVTGR FAGQKEEATR
     FLLGRYGGQM RLYRRAIEQI WRVPVAECYL YSFDGEYFLA VE
 
 
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