(data stored in SCRATCH zone)

SWISSPROT: Q47TX5_THEFY

ID   Q47TX5_THEFY            Unreviewed;       692 AA.
AC   Q47TX5;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 99.
DE   RecName: Full=DNA polymerase III subunit gamma/tau {ECO:0000256|RuleBase:RU364063};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU364063};
GN   Name=dnaX {ECO:0000256|RuleBase:RU364063};
GN   OrderedLocusNames=Tfu_0051 {ECO:0000313|EMBL:AAZ54089.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54089.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC       responsible for most of the replicative synthesis in bacteria.
CC       This DNA polymerase also exhibits 3' to 5' exonuclease activity.
CC       {ECO:0000256|RuleBase:RU364063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU364063};
CC   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha,
CC       epsilon and theta chains) that associates with a tau subunit. This
CC       core dimerizes to form the POLIII' complex. PolIII' associates
CC       with the gamma complex (composed of gamma, delta, delta', psi and
CC       chi chains) and with the beta chain to form the complete DNA
CC       polymerase III complex. {ECO:0000256|RuleBase:RU364063}.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC       {ECO:0000256|RuleBase:RU364063}.
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DR   EMBL; CP000088; AAZ54089.1; -; Genomic_DNA.
DR   RefSeq; WP_011290498.1; NC_007333.1.
DR   STRING; 269800.Tfu_0051; -.
DR   EnsemblBacteria; AAZ54089; AAZ54089; Tfu_0051.
DR   KEGG; tfu:Tfu_0051; -.
DR   eggNOG; ENOG4107QMP; Bacteria.
DR   eggNOG; COG2812; LUCA.
DR   HOGENOM; HOG000083933; -.
DR   KO; K02343; -.
DR   OMA; DVMEMDA; -.
DR   OrthoDB; 556582at2; -.
DR   BioCyc; TFUS269800:G1G4Q-49-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR022754; DNA_pol_III_gamma-3.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02397; dnaX_nterm; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TX5.
DR   SWISS-2DPAGE; Q47TX5.
KW   ATP-binding {ECO:0000256|RuleBase:RU364063};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   DNA replication {ECO:0000256|RuleBase:RU364063};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU364063};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063,
KW   ECO:0000313|EMBL:AAZ54089.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|RuleBase:RU364063,
KW   ECO:0000313|EMBL:AAZ54089.1}.
FT   DOMAIN       36    198       AAA. {ECO:0000259|SMART:SM00382}.
SQ   SEQUENCE   692 AA;  73168 MW;  55E09DECD6BE45B3 CRC64;
     MSIALYRKYR PATFAEVRGQ EHVTEPLRQA LRNGRVNHAY LFSGPRGCGK TSSARILARS
     LNCAKGPTPD PCGECDSCVA LAPDGGGSID VIEIDAASHG GVDDARDLRE RAFFAPVNSR
     YKVYIIDEAH MVTREGFNAL LKLVEEPPPH LKFVFATTEP EKVIGTIRSR THHYPFRLIP
     PNTLRELIEE ILNEEKVPYD PAALPLVIRA GGGSARDTLS ILDQLLAGSD ERGITREAAV
     QLLGYTDSSL LGEMVDALGA GDGAAVFELI DRVVEGGHDP RRFAADLLER VRDLVVLNAV
     PDALDKGLIN VPPDAVEQMR EQASRLGAAQ LTRAAEILNK GLTEMRGTTS PRLLLELMCS
     RILLPGVDPG DELALAARLE RLERNGIAAA PAAPAVSPPA AGTPATAPPS TPAAAPRPST
     AEPRPPQPPA PSARPHPAPA AADDWGAPRR PSQPAPAAPQ PAAPGPAGEG SFDDRWPHIV
     EYLASNRKRA AHAIVRDGVH ATLLQGRTLT LFFETEGLMR SFVTGGRARD IAEAVHRVFG
     LEVAVEAKAG HPGNVRQAPP QAPMSRPPQP VAQSTPPQPV QPSTAQPPGE PRDARAAAET
     GWDAPAAVPP STPVSTQEPA PVPEPEPEPP SAAEPAPAPP ASPVDASPAG EAEETNPEDT
     ADNDLDESSL TGAALIEKEL GGKLIKEIDH TD
//

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