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Database: UniProt
Entry: A0A0A6VTB1_9MICC
LinkDB: A0A0A6VTB1_9MICC
Original site: A0A0A6VTB1_9MICC 
ID   A0A0A6VTB1_9MICC        Unreviewed;      1030 AA.
AC   A0A0A6VTB1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=GY22_11795 {ECO:0000313|EMBL:KHD97074.1};
OS   Kocuria polaris.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=136273 {ECO:0000313|EMBL:KHD97074.1, ECO:0000313|Proteomes:UP000030466};
RN   [1] {ECO:0000313|EMBL:KHD97074.1, ECO:0000313|Proteomes:UP000030466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMS 76or {ECO:0000313|EMBL:KHD97074.1,
RC   ECO:0000313|Proteomes:UP000030466};
RX   PubMed=12656171; DOI=10.1099/ijs.0.02336-0;
RA   Reddy G.S., Prakash J.S., Prabahar V., Matsumoto G.I., Stackebrandt E.,
RA   Shivaji S.;
RT   "Kocuria polaris sp. nov., an orange-pigmented psychrophilic bacterium
RT   isolated from an Antarctic cyanobacterial mat sample.";
RL   Int. J. Syst. Evol. Microbiol. 53:183-187(2003).
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:KHD97074.1}.
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DR   EMBL; JSUH01000010; KHD97074.1; -; Genomic_DNA.
DR   RefSeq; WP_035927833.1; NZ_JSUH01000010.1.
DR   AlphaFoldDB; A0A0A6VTB1; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000030466; 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..179
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          389..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..1000
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..517
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..679
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..786
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..867
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1030 AA;  107358 MW;  A03B0FA615EA0110 CRC64;
     MTTALYRRYR PETFEDVIGQ EHVTEPLMTA LRKDRVSHAY LFSGPRGCGK TTSARILARC
     LNCAEGPTAT PCGRCDSCRD LARDGAGSLD VIEMDAASHG GVDHARDLRE RATFAPVRDR
     YKIFIIDEAH MVTREGFNAL LKIVEEPPEH IKFIFATTEP SKVLTTIRSR THHYPFRLVP
     TEPLMHYLEQ LCAEEHVQVA PGVLSLVVRA GAGSVRDTLS VLDQLMAGSD EQGIGYDLAV
     ALLGYTHGAL LDDVVDAFAS GDGTTVFRAV DRVVQTGQDP RRFVEDLLER FRDLIIVNAV
     PESAGNILHG MPQDQIARLR NQASQLGAAE LSRAADITNT ALTEMTGATS PQLHLELLCA
     RILLPSSEDT TRGVTARVDR LERRLSIGRG AAAAGPDETP DAPAASPAAS SAASSSAPTA
     PAGPGAPPGG RSHSQPASQS APAPERPAPP APGGDAQQAV PAVPRGTDPR ERTAQGAGQG
     FGQEPGHAAA APERPSARED SGPERPTGRE APAAAERPDA PRQDAAAQAP RQDTPRAGEQ
     GGNEIDLLRA SWPEIVNALA DIRRVAWFTV QRGTPQSFDG KVLRIMFDAE GDLMNFPRFE
     DDLRQAVQQI LGIDCRAEAV PPGDGGHGRG GGGGGAPRGP EPSTRPPGRP AEPGPGTDGE
     RPERRAPEDR SRGGQDRPGA PRGREQQPTP PRAASTPPDG APGTATDSAP EPPAGAPSPD
     GDGGGQDPWD AHGRPATDAP AEWTDPAWAQ EPVHSWSVAA IPQGGAPAGP PAAPAPRAPA
     QPEARPPGPA RTAEDPAGAQ PADRPAPQPG TQPGAPSDPG RTGRPGPAFP GEAPGARDRD
     VPPSDDDVPP PEEPPYPDEP PYPDDLDAAP PEQWRPAAPA RQSPASAPRS GGGPGNRSTG
     SATPPTAHPA ARPEDPRTAT GASAPAPTAN PAAPAAPAAP QQDAPSAAPA GADRNARLSF
     RERHAAAIAA GRKAPASAAA PQDSGVEWDD SFVPSSDDEA LEDSTLYGRA AIERILGGML
     IEERDLHTGE
//
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