ID A0A2N6PIR8_9MICO Unreviewed; 1103 AA.
AC A0A2N6PIR8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=CJ198_04410 {ECO:0000313|EMBL:PMB98580.1};
OS Brevibacterium luteolum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=199591 {ECO:0000313|EMBL:PMB98580.1, ECO:0000313|Proteomes:UP000235703};
RN [1] {ECO:0000313|EMBL:PMB98580.1, ECO:0000313|Proteomes:UP000235703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0680 {ECO:0000313|EMBL:PMB98580.1,
RC ECO:0000313|Proteomes:UP000235703};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-2017) 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:PMB98580.1}.
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DR EMBL; PNFZ01000002; PMB98580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6PIR8; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000235703; 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:0000256|ARBA:ARBA00022932};
KW Reference proteome {ECO:0000313|Proteomes:UP000235703};
KW Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT DOMAIN 46..190
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 397..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 113485 MW; A46FE82A5689B95E CRC64;
MSAVRSRVGD VSTALYRRYR PETFDEVIGQ DHVVTPLMAA IANDRINHAY LFSGPRGCGK
TTSARILARC LNCVEGPTAQ PCGQCPSCRD LANDGPGSLD VVEIDAASHN GVDDARDLRE
RAVYAPARDR FKVFILDEAH MVTPQGFNAL LKLVEEPPAH VKFVFATTEP EKVIGTIRSR
THHYPFRLVP PEVLTGYLEE LCTRENVPVS KGVLPLVVRA GGGSVRDSLS VLDQLMAGAG
PDGVDYHTAI ALLGYTPDSL LGDIVDAFSA GDGAAVFRVV DRVIESGQDP RRFVEDLLER
FRDLVVVGAA PEAAASFLPE VPSDRLERLV QQARSFGQAE LSRAADLFNT GLSEMSGATS
PRLQLELICA RVLLPAAEKS RRSTLSRVER IERRIGMGAT GTLPPGAVPA AVPEGTDNGP
GAAEAGSTAG VAAQTESAQP AKPAPAPARS VDDDLDEFAA AAAAAESMLS DEPDAGQSAE
SAPAADPSSP EPTSAAPEAT APEPTAPAVP EAAATAARRA ADSSAPAAAD AGQQTGAQQP
TESQQPAQLQ PSARLEQAGP QSAPAAQTSQ PGQVSQPSQT QGMQQPSQPQ HASEPAQPPT
PASGTGQPGA EIDAIRRAWL DILDALGRTA KLARAIVSNS AVPYGFTDGV FYLGFDNPGA
LNSFNRGNNA QKLSEALNDV LGIQARVEVG PATGNVPGGH SGSTPAANPG NPGGGAGGPQ
SSRGPEQQNT INRPRPTQEE IDSVVGPREA DREPIDHERF WKSPGDTAVA ESAADDAEEG
QSLDQPAAQT PDSAGEKPNA EQSAPEPPAN AGSRSTAEEP TADESTEERS AARQPAAEEP
AAPQQHPARQ APIAHDVEEP DDGPEPPPED DYYAGADFAD PYEADTSAGS GAVDMPAVVV
PPPAAIDDEP DSFGADSGDP GTTDAADSDA ATTDAGAPDA SAPSATGSAS DSDDDLDFLG
AYADPNIAFT TNDGPEAPLP KGEKPAESAN PYASFAQRAQ QNGNGSTPGH DANPGAAEQA
AHTSGPADPA DPGPAAGSGP AMAGAANGDG LEAQRQQTGA GRPDDGYEDF DPDTDMDITE
APDVGVPVVE RILGGVVIKE TDA
//
