ID   A0A1H1PV65_9ACTN        Unreviewed;       985 AA.
AC   A0A1H1PV65;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=SAMN04489717_1782 {ECO:0000313|EMBL:SDS15152.1};
OS   Actinopolymorpha singaporensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Actinopolymorphaceae; Actinopolymorpha.
OX   NCBI_TaxID=117157 {ECO:0000313|EMBL:SDS15152.1, ECO:0000313|Proteomes:UP000198983};
RN   [1] {ECO:0000313|EMBL:SDS15152.1, ECO:0000313|Proteomes:UP000198983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22024 {ECO:0000313|EMBL:SDS15152.1,
RC   ECO:0000313|Proteomes:UP000198983};
RA   de Groot N.N.;
RL   Submitted (OCT-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; LT629732; SDS15152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1PV65; -.
DR   STRING; 117157.SAMN04489717_1782; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000198983; Chromosome i.
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:UP000198983};
KW   Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT   DOMAIN          38..186
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          392..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..966
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        834..869
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        943..966
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   985 AA;  100021 MW;  BF04469534220D5D CRC64;
     MEAPLALYRR YRPQTYAEVI GQDHVTEPLQ QALRNNRVHH AYLFSGPRGC GKTTSARILA
     RCLNCEVGPT PEPCGECQSC RDLARGGPGS IDVIEIDAAS HGGVDDARDL RERAFFAPVS
     SRYKIYIVDE AHMVTTQGFN ALLKLVEEPP EHLKFVFATT EPEKVIGTIR SRTHHYPFRL
     VPPKVLQEYL SDLCEREGVP VEPAVLPLVV RAGAGSVRDT LSVLDQLIGG AGDDGVTYAR
     AVGLLGYTHE SLLDEVVDAL AAGDGGSVFT VVDKVIESGQ DPRRFAEDLL RRLRDLVIVS
     AVPDAIERGL LEGPADQAER LTAQAARFGT AELTRAADLV NDGLNEMRGA TAPRLHLELI
     CARILLPAVD DSEQGLHARL DRLERRLSIA GGENVPSAAG PSGSGGSAGS ARSAGPAGGA
     AAARDQLGRG QAGQRPSGGG GREAARNTLN TERPSRSGSG EPAGRDTDIS AAPSASPQRP
     SARPPAAGSA GSAGSVPVET SPPESPTQGP DAGGAGPESA PPDGPRPSAA EAAAADWGTP
     QAPHEPSDAS AAGTSVDQAG WSAPAPPAEP TARSAPGRAA PGGSGAGGSA PTESDSDAAV
     SGGAAPDGTG SPGALGITDV RRLWPDVLEA VKGKRRFSWV MLSQNAHVAD LHGNTLTVAL
     VNAGARDSFT RSGSDELLRQ ALRDVLGVDW RVEAIIDPSG GAGGSGGSGG SGPGGPGSGG
     SGSGRGGHGP PAGGAEPRGG ASGGGPSGGR AAADRGGGDS PGSARTRQGG DAADDGRGEP
     AATNGRSYNS FAGAPPEARD PAGQDDGWPS PAPVPGSTPD REPASVRSAD EGFPADTPAD
     EDRSAGDRSP GDRTRGERAR GEDRGGADRP NPPDQAGTSA RDNGSGWADV AVSTPGGSAA
     VDRNAGAEQP RAAGSQGNGS RPMSSARARA AAAAGSTPRP AEPTHDPDSD VDPDTDNSLS
     DDPRSHTALL EREFGAQLIE EIPLN
//