ID A0A0B9AN29_BRELN Unreviewed; 1199 AA.
AC A0A0B9AN29;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=AE0388_2712 {ECO:0000313|EMBL:KHS52162.1};
OS Brevibacterium linens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=1703 {ECO:0000313|EMBL:KHS52162.1, ECO:0000313|Proteomes:UP000031488};
RN [1] {ECO:0000313|EMBL:KHS52162.1, ECO:0000313|Proteomes:UP000031488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AE038-8 {ECO:0000313|EMBL:KHS52162.1,
RC ECO:0000313|Proteomes:UP000031488};
RA Maizel D., Utturkar S.M., Brown S.D., Ferrero M., Rosen B.P.;
RT "Draft Genome Sequence of Brevibacterium linens AE038-8.";
RL Submitted (NOV-2014) 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:KHS52162.1}.
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DR EMBL; JTJZ01000020; KHS52162.1; -; Genomic_DNA.
DR RefSeq; WP_039211089.1; NZ_JTJZ01000020.1.
DR AlphaFoldDB; A0A0B9AN29; -.
DR PATRIC; fig|1703.6.peg.2617; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000031488; 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:UP000031488};
KW Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT DOMAIN 36..737
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 396..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 123877 MW; 908D3A9ECFAA5E0F CRC64;
MSTALYRRYR PETFDEVIGQ EHVTDPLKAA IERGRINHAY LFSGPRGCGK TTSARILARC
LNCEQGPTPV PCGECPSCRD LANGGPGSLD VVEIDAASHN GVDDARDLRE RAVYAPARDR
YKVFILDEAH MVTSQGFNAL LKIVEEPPPH IKFVFATTEP EKVIGTIRSR THHYPFRLVP
PEALGNYLEE LCTREGVQVA KGVLPLVVRA GGGSVRDTLS VLDQLIAGSG PDGVDYGRAI
ALLGYTPDSL LSDIVDAFSA GDGAGVYRAV ERVIESGQDP RRFVEDLLER FRDLIVINAA
PEAAHAFLPE VPPDRLERLT LQANGFGQGE LSRAADLLNV GLTEMSGATS PRLQLELICA
RILLPGSGRS RDAVLSRVER MERRIGMSAT GVAANVPPAQ VSDQGAAAGG AGQGQAPAAG
QGQSTGQPSS GGASASGAGR GAGAPAANAA AGQNQSAAHD DFDDIAAMAA AAESMLNEPA
GQPVHQDQSG QQEQQRQSGQ PEQPGQQGHR TQPEPSSQDA SQARPDQRAQ SDRQGQPTQY
DQQARQEQRT QQEPPSRHEP QAQPVPANDG QQSVEDAPAA GERPSAQNQQ PSSEPSSSTG
RAPETAPQPE QNNQQMPDPA GAPSHGSPRD SAPESAPVNQ PQRQAAEQSQ NQSGPAPTSA
APKGPEEDSQ SEQAAAPEAT SVAGSGDIGG EIEAIRRAWP SILASVEKRS RLTRAIIAAN
AIPQSFSDGV VYLGFNNAGS VQGFQQRDHA AKLAAAINDV LGIQARIDIG DVGRIGGGSA
GGGNQGKGSS APSMNDSGGN HGPASSQRRP SPQEVAAVVG TREVDKPQVD HEKFWEPSGP
TQGPWSSDDE EGEQPGQPTE PTTQGNTAGA AEQADEGSAT AEQSGGAGAS TKSPQDDAGP
ATEAAPDSST PQAPASDSSV PETQAWNAPE PSVPEHDASE SAVPDVVVPD LSDDDFFGPP
ADAGTEPAHT GTDSAGTAPA DEFGHPDPSP QQGSASAGSS GYTDNSPMEY VEPRWEEPNW
NDGPSPIDTS PTGTASTGTD SSDVDETSAG SGAVDVGAVV VPPPDDDLDY PDLSDGPSSF
GGGAFEQPAP AVQSPPPTSA HGGEKPFKSR FAALAEKHGV NTTPPAGSGY GSGPQGNPAG
GSASGAASAP GSNPYPQRSG SDEDEYDPET DLDVSEAPQM GVDVIARVLG GEIIDEREV
//
