ID A0A0N1D1V9_9MICO Unreviewed; 839 AA.
AC A0A0N1D1V9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=AEQ27_11020 {ECO:0000313|EMBL:KPG81400.1};
OS Frigoribacterium sp. RIT-PI-h.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1690245 {ECO:0000313|EMBL:KPG81400.1, ECO:0000313|Proteomes:UP000037934};
RN [1] {ECO:0000313|Proteomes:UP000037934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-h {ECO:0000313|Proteomes:UP000037934};
RA Tran P.N., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-2015) 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:KPG81400.1}.
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DR EMBL; LHOZ01000076; KPG81400.1; -; Genomic_DNA.
DR RefSeq; WP_054146684.1; NZ_LHOZ01000076.1.
DR AlphaFoldDB; A0A0N1D1V9; -.
DR PATRIC; fig|1690245.3.peg.1047; -.
DR Proteomes; UP000037934; 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:UP000037934};
KW Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT DOMAIN 36..177
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 385..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 86171 MW; 3F8A361E0C0B8B99 CRC64;
MVTALYRRYR PENFAELIGQ TQVTDPLRTA LRTNRVNHAY LFSGPRGCGK TTSARILARC
LNCAQGPTDT PCGVCASCVE LSRDGGGSLD VIEIDAASHN GVDDARDIRD RAVFAPARDR
FKIFILDEAH MVTPQGFNAL LKVVEEPPEH VKFIFATTEP DKVIGTIRSR THHYPFRLVP
PAQMLEYVHE LCESESVEAA PGVLPLVVRA GGGSVRDTLS LLDQLMAGSE NGAIEYERAV
ALLGYTHASL LDDVVEALGA RDGAAAFAAV DRVVQTGQDP RRFVEDLLER LRDLIVVGAT
VEGASAVLRG VTADELDRLV HQSHAFGAAE LSRSADVVNR ALTDMTGATS PRLHLELMIA
RVLVPESDQT GRGALARVER LERRVGVEGP GSASSSASGP STAAHPTEVG PASGRSAPAV
VSSAPVSTAP AVTSPSAAPV EATPSTEAAG GPSAVESATA SWATAAPSAP VEPVGSAAPA
TTEPAPPSAP HSAAWAQTPD SGQGAGSGAA PVTLQQMRDS WPEIVEVVQK ARRTAWMVVV
TATVVDFADD VLTLAFPSAN DVESFKRPQG AAEGVSEYLR RAIVDVLGVK VKYIARVEGD
GPAGPTPTGA PPVDASVPTA ASTPRRDTGR SAAPATDGGR QASAPSPQGS TPAETGRTTA
AAAEPAAPDD SAAPAASPPR TPAPATRSAS AERSSAPASA SVARPGAPAP VTGWDVATIP
QAPPPEPDEP EHITEEPPGG VPTVDAAPPP PEADASPVGR SVAGAPSSAA TASTPAPAAP
AASTSAGPSV AERRAATGDP RRGIPTGSRY GEAVVREILG AQFIEEETIA PRVTPQRSE
//
