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Database: UniProt
Entry: A0A2U1ZUV6_9MICO
LinkDB: A0A2U1ZUV6_9MICO
Original site: A0A2U1ZUV6_9MICO 
ID   A0A2U1ZUV6_9MICO        Unreviewed;       938 AA.
AC   A0A2U1ZUV6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-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=C8046_08810 {ECO:0000313|EMBL:PWD50730.1};
OS   Serinibacter arcticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC   Serinibacter.
OX   NCBI_TaxID=1655435 {ECO:0000313|EMBL:PWD50730.1, ECO:0000313|Proteomes:UP000245166};
RN   [1] {ECO:0000313|EMBL:PWD50730.1, ECO:0000313|Proteomes:UP000245166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCH200 {ECO:0000313|EMBL:PWD50730.1,
RC   ECO:0000313|Proteomes:UP000245166};
RA   Thakur V., Kumar V., Singh D.;
RT   "Genome assembly of novel Miniimonas species PCH200.";
RL   Submitted (MAR-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:PWD50730.1}.
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DR   EMBL; PYHR01000002; PWD50730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1ZUV6; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000245166; 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   Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT   DOMAIN          36..184
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          387..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..407
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..707
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..744
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   938 AA;  95770 MW;  B6251854BC246BAB CRC64;
     MTTALYRRYR PDSFADVIGQ EHVTDPLRAA LRADRATHAY LFSGPRGCGK TTSARILARC
     LNCAEGPTDT PCGVCESCVE LARGGPGSLD VVEIDAASHG GVDDARDLRE RAVFAPARDR
     YKVFIIDEAH MVTPQGFNAL LKLVEEPPAH VKFVFATTEP EKVIGTIRSR THHYPFRLVP
     PAVLQGYLGT LCEAESITVD SGVLPLVVRA GGGSVRDSLS VLDQLMAGAA EEGVSYDLAS
     SLLGFTPVTL LDDAVGALAA GDGAALFRVV DHVVESGRDP RRFVEDLLDR LRDLIVISAS
     GSEAETVLRA LPADEVERMR PQASALGAHR LSTVADIVNA GLTDMVGATS PRLLLELVLT
     RAMLAIGGLG DAPAAASHAT PVATIPAPIP APVQASTPEP TTPPVVTQPA TPSRASEAPQ
     SRPAASATTA PPAQPAAAAI PGAGPLGGPR EGAPTPTRRP AERPATERQQ PAAEQTTTPA
     PRSEERPAAR DEAPREPAAP ASPAAPAADQ PAAEPTSSAG AVDGTELRRR WPEVLETLAA
     SSRATWTLIS QHAQPGEVTA DSMTLLFPTP GLISAFTGRD GGAVLSQAIF ETVGLRLRVQ
     VDVAGPDGPG GPGGDGGPAG PGGGQGVGQG VGQGVGQGQR DGGGRNERAP QGGARADGQG
     RGPLAQVPGA TAQAGPAHDF GPEPDEDPYG AHDPYLASEH AARAEPEPER APASPAPTAA
     SPRIVTQPTA TTPRPSTTPT TRQPAPSEAQ PPAAAETAEP EAPARQVSEA VARALADWDD
     APVAVPGRSS SATGGTAATP ADDSADDVPH VRSHLSVVAP MAPDAPDVAP DAEPAPEAEH
     APETLRAPAH RSTPAGPSRL APVIDLQARG AARALAATPP APAAPDLPPA PWEDADDDDV
     ANSVAASSSG LMGATLVAKM LGGVVIDEIL DGVSDVRR
//
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