ID   A0A1C9WQ94_9MICC        Unreviewed;      1012 AA.
AC   A0A1C9WQ94;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, 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=ASPU41_08435 {ECO:0000313|EMBL:AOT03364.1};
OS   Arthrobacter sp. U41.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1849032 {ECO:0000313|EMBL:AOT03364.1, ECO:0000313|Proteomes:UP000095776};
RN   [1] {ECO:0000313|EMBL:AOT03364.1, ECO:0000313|Proteomes:UP000095776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U41 {ECO:0000313|EMBL:AOT03364.1,
RC   ECO:0000313|Proteomes:UP000095776};
RA   Fomenkov A., Akimov V.N., Vasilyeva L.V., Andersen D., Vincze T.,
RA   Roberts R.J.;
RT   "Complete Genome and Methylome Analysis of Psychrotrophic Bacterial
RT   Isolates from Antarctic Lake Untersee.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; CP015732; AOT03364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C9WQ94; -.
DR   STRING; 1849032.ASPU41_08435; -.
DR   KEGG; aru:ASPU41_08435; -.
DR   Proteomes; UP000095776; Chromosome.
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:UP000095776};
KW   Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT   DOMAIN          9..157
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          404..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..841
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          897..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..476
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..736
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1012 AA;  103427 MW;  A3D687B735DFF80C CRC64;
     MTALRKNRVN HAYLFSGPRG CGKTTSARIL ARCLNCAEGP TDTPCGRCPS CVELARGGSG
     SLDVIEIDAA SHGGVDDARD LRERATYAPV RDRYKIFIID EAHMVTSAGF NALLKIVEEP
     PEHIKFIFAT TEPDKVIGTI RSRTHHYPFR LVPPEPLMEY LELLCKQEDV PVAPGVLSLV
     IRAGGGSVRD SLSVLDQLMA GAGPAGLDYE LAVALLGYTH ASLLDDVVEA VAASDAATVF
     RAVDRVIQTG HDPRRFVEDL LERFRDLIIV QAMPESAQSI LRGMPADQIA RLQNQAHNLG
     AAELSRAADV TNTALTEMTG ATSPRLHLEL LCARILLPSA DQTERGIAAR IDRVERRLNY
     AGSDVGAPAA VAAVPAAAVP AAAAPAPAAP APMTPVPAAA TPAAAASATP ASPSAAMAPQ
     PETEPARESL TPPRVSTGDW PVDEPAGVQR AAPGKTPESR ATPPAPPAPA AAAPPAPFPS
     GQAQSGPGRT APAQDRRDPA PPAAAPGVAP GAGSGPDVEV LRRAWPEILQ TLSKIKRSTW
     ALVEPNAQVG HFEDHVLTLA FTTSGLAGAF GRADHSENLR QAIHKTIGIE CQINAVASGS
     NSAASSEPNP KAPVSRDVPA TSADADWGLT PAAAPAQSGA PRTEPAPAQT AVPATRTAPM
     APAQATVTPA APVQAPVPPV PAPALATSAS EVPPAPAPAP AAAAAGEQQN SSPESAGSYD
     HPDDDWGPPR DEDAPPLDEE PPMDWDPSAP ALVRAAPPAA APAPARKKAA APARTGAASP
     TAPSGAPAPQ APDTADDPWA RAVEQAPGVW AVGTEPNVGR YPGEASETPE PAPEPEPPHY
     EPAAAQVPQY AAAVSASASY EPVASSSNGW GDPAELVAVG APSVPASANA APIAAPATPA
     NAAPTNAAPT AAPVPPTASP AANPVAPAAT PATGRQSLYQ RLSNSPEAEA GRAKAPARAA
     AVTTTYVQDI PSADDETIEE SGVFGRAAVE RILDGKLIEE RSLDGSPLPP RF
//