(data stored in SCRATCH zone)

SWISSPROT: Q13F12_RHOPS

ID   Q13F12_RHOPS            Unreviewed;       624 AA.
AC   Q13F12;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   16-JAN-2019, entry version 76.
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=RPD_0087 {ECO:0000313|EMBL:ABE37327.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37327.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37327.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37327.1,
RC   ECO:0000313|Proteomes:UP000001818};
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.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000283; ABE37327.1; -; Genomic_DNA.
DR   RefSeq; WP_011500520.1; NC_007958.1.
DR   STRING; 316057.RPD_0087; -.
DR   EnsemblBacteria; ABE37327; ABE37327; RPD_0087.
DR   KEGG; rpd:RPD_0087; -.
DR   eggNOG; ENOG4107QMP; Bacteria.
DR   eggNOG; COG2812; LUCA.
DR   HOGENOM; HOG000083933; -.
DR   KO; K02343; -.
DR   OMA; DVMEMDA; -.
DR   OrthoDB; 556582at2; -.
DR   BioCyc; RPAL316057:RPD_RS00435-MONOMER; -.
DR   Proteomes; UP000001818; 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; IPR022107; DNA_pol_III_gamma/tau_C.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   Pfam; PF12362; DUF3646; 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; Q13F12.
DR   SWISS-2DPAGE; Q13F12.
KW   ATP-binding {ECO:0000256|RuleBase:RU364063};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
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:ABE37327.1};
KW   Transferase {ECO:0000256|RuleBase:RU364063,
KW   ECO:0000313|EMBL:ABE37327.1}.
FT   DOMAIN       63    211       AAA. {ECO:0000259|SMART:SM00382}.
SQ   SEQUENCE   624 AA;  67093 MW;  859348D8EF280512 CRC64;
     MTDSGPPAIP SGDSEQTGLG LGAAPAGAYR VLARKYRPNS FEDLIGQEAV VRTVSNAFDT
     GRIPQAWILT GVRGVGKTTT ARILARALNY EMPDGSVKGP TIHMPVHGVH CKAIMESRHM
     DVLEMDAASH TGVDDVRQIN DSVRYAPASA RYKVYIIDEV HMLSTAAFNA FLKTLEEPPE
     HAKFVFATTE IRKVPVTVLS RCQRFDLRRV EADVLMKHLA GIAAKEGVEV EPEALGIIAR
     AAEGSVRDSL SLFDQAIAHA AGLVRADQVR QMLGLADRTR VIELFDALAR GDIASAFQEF
     RDQYDTGADP VVVLSDLAEF VNFVTRVKIV PATADNVAFG ETERLRGRDF AAKLSMRVLS
     RMWQMLLKGI AEVQGATRPA AAAEMVLVRI AYAADLPTPD EALRMLAQDG GSATPLPSGG
     GAAPRGASSP PVSAASVASA YAAPAAAAMP PRSAPTMARG GADSMARPQI SAPAAAPQQD
     AALKITTFPQ LVALASEKRD VMTRMALEAD VRLVRIDDGR LELALERTAS RSLINDLGRK
     LEQWTGRRWT VIVSNEPGQP TLRSQSEAQK NERERAAESD PRVREVLAKF PGAKFEVRRL
     ATDLAEADAG IEDPAEPVDD DDES
//

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