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Database: UniProt
Entry: A0A0C3RIQ1_9PORP
LinkDB: A0A0C3RIQ1_9PORP
Original site: A0A0C3RIQ1_9PORP 
ID   A0A0C3RIQ1_9PORP        Unreviewed;       371 AA.
AC   A0A0C3RIQ1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=BA92_00975 {ECO:0000313|EMBL:KIO47376.1};
OS   Sanguibacteroides justesenii.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Sanguibacteroides.
OX   NCBI_TaxID=1547597 {ECO:0000313|EMBL:KIO47376.1, ECO:0000313|Proteomes:UP000031980};
RN   [1] {ECO:0000313|EMBL:KIO47376.1, ECO:0000313|Proteomes:UP000031980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUH 308042 {ECO:0000313|EMBL:KIO47376.1,
RC   ECO:0000313|Proteomes:UP000031980};
RA   Sydenham T.V., Hasman H., Justensen U.S.;
RT   "Porphyromonadaceae bacterium OUH 308042 = ATCC BAA-2681 = DSM 28342 draft
RT   genome.";
RL   Submitted (JUL-2014) 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. This DNA
CC       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-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632,
CC         ECO:0000256|RuleBase:RU364063};
CC   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the POLIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III
CC       complex. {ECO:0000256|RuleBase:RU364063}.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC       {ECO:0000256|ARBA:ARBA00006360, ECO:0000256|RuleBase:RU364063}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIO47376.1}.
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DR   EMBL; JPIU01000023; KIO47376.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3RIQ1; -.
DR   Proteomes; UP000031980; Unassembled WGS sequence.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd00009; AAA; 1.
DR   CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau_N.
DR   InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR02397; dnaX_nterm; 1.
DR   PANTHER; PTHR11669:SF0; PROTEIN STICHEL-LIKE 2; 1.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   Pfam; PF13177; DNA_pol3_delta2; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU364063};
KW   DNA replication {ECO:0000256|RuleBase:RU364063};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU364063};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364063};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU364063,
KW   ECO:0000313|EMBL:KIO47376.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031980};
KW   Transferase {ECO:0000256|RuleBase:RU364063, ECO:0000313|EMBL:KIO47376.1}.
FT   DOMAIN          38..181
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   371 AA;  41889 MW;  95B0E1D78AA80EF7 CRC64;
     MENYVVSARK YRPASFDTVI GQRAITSTLK NAILNKQLAQ AYLFCGPRGV GKTTCARIFA
     KTINCMNLQP NGEPCNECES CVAFNNSRSL NIHELDAASN NSVDDIRGLV DQVRLLPQVG
     KYSVYIIDEV HMLSTSAFNA FLKTLEEPPA HAIFILATTE KHKILPTILS RCQIYDFNRI
     KVSDTIEHLK RIADKEGVQV EEEALNIIAQ KADGAMRDAL SIFDQVVSFC GKELTYAKVI
     ENLNVLDYEY YFKLTDLFYN GKVAETFLLF DEIMTKGFDA GNLIAGLGKH FRDLLVAKDE
     VTLSLLEVSA SIRERYLRQA KEVDVDFIFN ALKVIEQCEM QYKVRVEKRL CVEITLIKLC
     QINALKKKAL V
//
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