ID A0A0M4QZE5_9PSEU Unreviewed; 829 AA.
AC A0A0M4QZE5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=XF36_23475 {ECO:0000313|EMBL:ALE85743.1};
OS Pseudonocardia sp. HH130629-09.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1641402 {ECO:0000313|EMBL:ALE85743.1, ECO:0000313|Proteomes:UP000062082};
RN [1] {ECO:0000313|EMBL:ALE85743.1, ECO:0000313|Proteomes:UP000062082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH130629-09 {ECO:0000313|EMBL:ALE85743.1,
RC ECO:0000313|Proteomes:UP000062082};
RX PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT "Variable genetic architectures produce virtually identical molecules in
RT bacterial symbionts of fungus-growing ants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011868; ALE85743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4QZE5; -.
DR KEGG; pseh:XF36_23475; -.
DR PATRIC; fig|1641402.3.peg.5034; -.
DR OrthoDB; 9810148at2; -.
DR Proteomes; UP000062082; 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; IPR048448; DnaX-like_C.
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 Pfam; PF20964; DnaX_C; 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:UP000062082};
KW Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT DOMAIN 34..178
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 383..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..611
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..764
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 85651 MW; B83983934DC8C76E CRC64;
MALYRKYRPA KLADVVGQEH VTEPLATALT AGRINHAYLF SGPRGCGKTS SARILARSLN
CEQGPTPDPC GVCNSCIALA PEGSGSIDVV ELDAASHGGV EDARELRDRA FYAPAESRYR
VFVVDEAHMV TTQGFNALLK IVEEPPEHLV FVFATTEPEK VLPTIRSRTH HYPFRLIPPG
TMRSLLEKIC GEEQVTVAPP VFPLVIRAGG GSARDTLSVL DQLLAGAGPQ GVTYEHAVAL
LGVTDSGLID DTVDALAAAD GAAVYGAVDR LVEAGHDPRR FASDLLQRFR DLMLVQAVPD
AAEQGLVDGA EDELARMADQ AARLGPATLT RYGEILHQGL IEMRGATAPR LLLELLVARM
LLPAATTSDG GLLERLERIE RRNAIAPDPA GPSDDGAAKR FVRPSERPPA PTSDGAAPGA
GGGVPARSAE RDAGAPAAVP APAPARPDES APRPAVTRAA DGPRSAERDD EAAGPAAPAR
SGDRTEADPR SAEHAPASVP DVPVPDAPVP DSSVPAVSAP AESDPVAPEV GDGPVPADGP
AADAPATGTG HTDGEPARQA DGPGDGARRA DDPGPGGAGA GGTEEPAAQA APSRSPAPPR
DGAPPDAVPP ESAQPVSSAS SLDATAVRRV WPEILAAVRQ RSRSTEALLV NATVRAVDGD
TLVLAIGAPP LARRLSEARN TDVIADALRA VLGVQWRVHC DTGEAATARR AAAPDRAQRA
VPQRPSQRDA PQREQGGRPA RRPAGDSDVP LPPEPPPEDA PPDPRDAGPQ GGDGPGARPA
PVRNQAAEEE DMLAEAAAEA ASPGARRDPE AAALEILTSH LGARKLDPR
//
