ID A0A418URJ9_9ACTO Unreviewed; 899 AA.
AC A0A418URJ9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaX {ECO:0000313|EMBL:RJF41207.1};
GN ORFNames=D4740_09855 {ECO:0000313|EMBL:RJF41207.1};
OS Actinomyces sp. 2119.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=2321393 {ECO:0000313|EMBL:RJF41207.1, ECO:0000313|Proteomes:UP000284680};
RN [1] {ECO:0000313|EMBL:RJF41207.1, ECO:0000313|Proteomes:UP000284680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2119 {ECO:0000313|EMBL:RJF41207.1,
RC ECO:0000313|Proteomes:UP000284680};
RA Li J.;
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC {ECO:0000256|ARBA:ARBA00006360}.
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:RJF41207.1}.
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DR EMBL; QYRR01000007; RJF41207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418URJ9; -.
DR Proteomes; UP000284680; Unassembled WGS sequence.
DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:InterPro.
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 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 DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000313|EMBL:RJF41207.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000284680};
KW Transferase {ECO:0000313|EMBL:RJF41207.1}.
FT DOMAIN 36..184
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 371..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..873
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 91353 MW; 8F04016B42D32537 CRC64;
MTTALYRRYR PDTFQDVIGQ DHVTAPLMAA LRADRVTHAY LFSGPRGCGK TTSARILARC
LNCEQAPTDA PCGECPSCRD LATGGPGSLD VVEIDAASHN GVDDARDLRE RAAFAPARDR
YKVFILDEAH MVTAQGFNAL LKLVEEPPTH VKFIFATTEP DKVIGTIRSR THHYPFRLVP
PDVLEDYLGQ LCDAEGVSVG PGVFPLVVRA GGGSVRDTLS VMDQLIGGAV DGSVDYQRAV
ALLGYTDTTL LDQCVDAVAA ADGSGVFRVV ERVVTSGHDP RRFVEDLLQR LRDLLVIALA
GSQAGPALGS LPADQLARME AQARTLGAAA LSRAADTTAQ ALGSMVGATS PRLQLELLMA
RLLLPGAVPG AAAPSADGQA PAVGQPVRPL PTSTPGTSAP TASPVPPAPT APPSASEAEA
APQAVQGQGT QTSPGAVPGA TEPLSASQPS PPRPGDGQGA PGAAEAEMIR TRWEEVLEAA
KRSRRATWAL VGPNSQPGSL REGALTLLFT APGLVGAFEN GGHGPVLSAA IHQALGLQVD
VHAVLVGGDG PGGGGSRSGH WNSTQAGAGA APVAWDRSQA GAAGPVASRD QGMPRAADQG
AREDQEPPLP PEEPPVRLPE PPGQGWDPVA GADGVQEEPA PAGQGTRGEA YGGAAGAWTP
GPGASVPDPD DGWGPVAVPG GGGAVHSAPE LTGRTRQPVS GVPAGGASSP PPSSVSLPSP
ASSQESALQE PPLAPVRRLH ALPDLPAAVS PGPSGPGPSA ASADVFDQVG ERPSRPPLGL
APATWDGPAQ PAQTFSDGVP LPEEPGDQEE PAAEGALAER DGADDTWAPT GAAGSRLAAA
MAAARAAAQE PDDHSALAED TPSEDDEDAE DAGVVGLEVV KRVLGATVIE EVTVTQEGY
//
