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Database: UniProt
Entry: A0A2T3HGY4_9SPHI
LinkDB: A0A2T3HGY4_9SPHI
Original site: A0A2T3HGY4_9SPHI 
ID   A0A2T3HGY4_9SPHI        Unreviewed;       606 AA.
AC   A0A2T3HGY4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=C7T94_18795 {ECO:0000313|EMBL:PST81663.1};
OS   Pedobacter yulinensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=2126353 {ECO:0000313|EMBL:PST81663.1, ECO:0000313|Proteomes:UP000240912};
RN   [1] {ECO:0000313|EMBL:PST81663.1, ECO:0000313|Proteomes:UP000240912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YL28-9 {ECO:0000313|EMBL:PST81663.1,
RC   ECO:0000313|Proteomes:UP000240912};
RA   Keele B.F.;
RL   Submitted (MAR-2018) 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:PST81663.1}.
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DR   EMBL; PYLS01000009; PST81663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3HGY4; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000240912; 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; IPR022754; DNA_pol_III_gamma-3.
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   Pfam; PF12169; DNA_pol3_gamma3; 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   Reference proteome {ECO:0000313|Proteomes:UP000240912};
KW   Transferase {ECO:0000256|RuleBase:RU364063}.
FT   DOMAIN          38..186
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          372..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..436
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  67626 MW;  EC02387A8CD168D4 CRC64;
     MENFIVSARK YRPATFETVV GQQHITGTLK NAIRNNQLAQ AFLFCGPRGV GKTTCARILA
     KTINCSNPGA DMEACASCDN CLSFQNGHSF NIHELDAASN NSVEDIRSLI EQVRIPPQSG
     KFKIYIIDEV HMLSQSAFNA FLKTLEEPPA YAIFILATTE KHKILPTILS RCQIFDFNRI
     QVEDISGHLA KIAGRESIAY EPDGLHIIAQ KADGGLRDAL SMFDQIASYS GKNITYKAVI
     DNLNILDYDY FFKLTDNLTA GRVSETLLLF DEVLNNGFDG NNFINGLASH FRNLLVGKDP
     ATLRLLEVSN NIRQKYMEQA RQTELSFLLT ALNLANQCDL NYKSSKNQRL QVELALIKMC
     HIRNVVHLAQ HPSSALQPAT DAAQDKKKTE LSAVNQAPAA PYKEPAATAA PVAQEPPAIP
     HMPAPRDEPP RQAPAEPASP QGSIRIGLPV KDQVIPSLIP SLTDLERVAN GEEDGPKKVT
     GDARQPFTYE TLLELWNKYA ERLKADGKIN VFTLMTTNAP VLKTPEHIVV LTENKIQEHL
     LQDESVELLN YLRNGLQNFG IEISHEQTER KQVKRLYTNT EKYAYLAAKN PKLEEMRRRF
     NLDVIP
//
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