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Entry: A0A1V2TDQ0_9NOCA
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ID   A0A1V2TDQ0_9NOCA        Unreviewed;       947 AA.
AC   A0A1V2TDQ0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=B0T46_18115 {ECO:0000313|EMBL:ONM47471.1};
OS   Nocardia donostiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1538463 {ECO:0000313|EMBL:ONM47471.1, ECO:0000313|Proteomes:UP000188836};
RN   [1] {ECO:0000313|EMBL:ONM47471.1, ECO:0000313|Proteomes:UP000188836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X1655 {ECO:0000313|EMBL:ONM47471.1,
RC   ECO:0000313|Proteomes:UP000188836};
RX   PubMed=26914251; DOI=10.1007/s10482-016-0667-8;
RA   Ercibengoa M., Bell M., Marimon J.M., Humrighouse B., Klenk H.P.,
RA   Potter G., Perez-Trallero E.;
RT   "Nocardia donostiensis sp. nov., isolated from human respiratory
RT   specimens.";
RL   Antonie Van Leeuwenhoek 109:653-660(2016).
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:ONM47471.1}.
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DR   EMBL; MUMY01000015; ONM47471.1; -; Genomic_DNA.
DR   RefSeq; WP_077118812.1; NZ_MUMY01000015.1.
DR   AlphaFoldDB; A0A1V2TDQ0; -.
DR   STRING; 1538463.B0T36_14930; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000188836; Unassembled WGS sequence.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
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-LIKE 2; 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:UP000188836};
KW   Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT   DOMAIN          34..177
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          387..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   947 AA;  97304 MW;  B1D5F623F4D866CD CRC64;
     MALYRKYRPA TFAEVVGQEH VTDPLSTALD SGRISHAYLF SGPRGCGKTS SARILARSLN
     CVEGPTSTPC GQCPSCMALG PGGAGNLDVI ELDAASHGGV DDTRELRDRA FYAPAESRYR
     VFIVDEAHMV TTAGFNALLK IVEEPPAHLI FVFATTEPDK VLPTIRSRTH HYPFRLLPPA
     TMRGLLGRIC EQEHVPVEEA VYPLVIRAGG GSPRDSLSVL DQLLAGAGPE GVTYSRAVAL
     LGVTDIALID DAVDALATTD GAALFGTVDR VMEAGHDPRR FAVDLLERLR DLILLRAVPD
     AADRGLVAAP ADQLERMSDQ ASRIGPASLT RYAELLHAGL GEMRGATAPR LLLEVVCARM
     LLPAASDAEA ATLQRLEQLE RQVATGAVSA PAAATDSSER TAPASSPSPA SGPPRRRGAE
     ALAAVRESRA AKAAVPDVVD AAAREKPQEE PQHGGSASGA PGRPAQPSDT EPVPSAGPGN
     RPDETRPDHA AEQYEPTPPE TSRSREGSTE RADVADGRAR TEPVHPDPAT HGGGRESRRD
     AGAFRSASGT SDAGVPMSSE RAASAEGGAP GDSPMSPRRS GQGEGSTGSH DPGRPAPGGS
     GHELGAKGPD QPTDPTQVPY GRADANAASS PSAAGYEGPD NRAPAHGPAA RGSASVSRGG
     TDHAADLSGP APSPAADPLA EIEAAWGDIK TRVREFSVAV AAMLASGASV VRVEGEVIVF
     AHQHAALVQR LSNQQSLDAV RSAVGAVLGR DYQVKWVTAA AAGGRQAVGG PGNRGRGGGR
     EAGGRRSGSA DGTGGPDAER GKTVDGPIAP PGRGAEPEGY GTRPSGGDGE PAGHGSRGRG
     RRGSAGAPPR FSRPSQARSG GSGGNGGSVY PDDDIPPPDY PDFPDDPGPA DYGYDSGPAA
     VPPSTPEEEQ EMLAESARPV APGDRRDPDE VALELLASEL GAVRLDG
//
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