ID A0A401Y5H3_9ACTN Unreviewed; 704 AA.
AC A0A401Y5H3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=NLS1_18580 {ECO:0000313|EMBL:GCD89852.1};
OS Nocardioides sp. LS1.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1027620 {ECO:0000313|EMBL:GCD89852.1, ECO:0000313|Proteomes:UP000288271};
RN [1] {ECO:0000313|EMBL:GCD89852.1, ECO:0000313|Proteomes:UP000288271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS1 {ECO:0000313|EMBL:GCD89852.1,
RC ECO:0000313|Proteomes:UP000288271};
RA Morimura H., Sato I., Uesaka K.;
RT "Draft Genome sequence of the deoxynivalenol-degrading actinomycete
RT Nocardioides sp. strain LS1, isolated from wheat leaves in Japan.";
RL Submitted (NOV-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:GCD89852.1}.
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DR EMBL; BIFF01000002; GCD89852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401Y5H3; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000288271; 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; 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; 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; PR01217; PRICHEXTENSN.
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:UP000288271};
KW Transferase {ECO:0000256|RuleBase:RU364063}.
FT DOMAIN 38..182
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 420..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..462
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 73982 MW; 08A77944EF9842A0 CRC64;
MESPLALYRR YRPETFAEVI GQDHVTTPLR AALANNRVNH AYLFSGPRGC GKTTSARILA
RALNCELAPV ADPCGECDSC RDLARGGPGS IDVIEIDAAS HGGVDDARDL REKAFFAPVR
SRYKVYIIDE AHMVTTQGFN ALLKLVEEPP PHLRFIFATT EPDKVLPTIR SRTHHYPFRL
IPPRLLSSYL SELCEKEQVS IEPAALPLVV RAGAGSARDT LSVLDQLLGG AGPEGVTHQL
ATGLLGYTPD SLLDEVVDAF AAGDGSAVFG VVDKVIETGQ DPRRFTEDLL RRLRDLVIVD
AVPDAPATGL IDCSEDQGER LVAQAARFGS AELSRAADLV ASGLTEMRGA TAPRLLLELI
VARVLLPGAD HSTDGLAARL DRIEKRIAIT GVPSATAAPQ PAVPQQDRPA QVHVTSDVVA
PTPAPVRPEP VAEPAPIPER TPEPEPVRAP APPEPEPTAP AAAPAAAPAA APAAGGGLSL
IDVRRLWPDI VDATKLRRRV TWMHLTQNCQ VVSIEGNVLT LGFPNAGARE SFDNGGSAEI
VRQAAIDVVG ADWRIVTIVD PGAQADAGQR PPAPAPAAPD PAPAAPAVSD APEQAAAPVS
PPAWVSDEPE TPTAQAPTSP APEAGAPEAP PAREKAGPEA IAAAKAAIQS TRQSGEEAAR
SDDAAERDAD ASLDDVDADH QGLAGAELLQ RELGARVIEE IRHQ
//
