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Database: UniProt
Entry: A0A261EVC2_9BIFI
LinkDB: A0A261EVC2_9BIFI
Original site: A0A261EVC2_9BIFI 
ID   A0A261EVC2_9BIFI        Unreviewed;       934 AA.
AC   A0A261EVC2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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=PSRA_1406 {ECO:0000313|EMBL:OZG50775.1};
OS   Pseudoscardovia radai.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Pseudoscardovia.
OX   NCBI_TaxID=987066 {ECO:0000313|EMBL:OZG50775.1, ECO:0000313|Proteomes:UP000216725};
RN   [1] {ECO:0000313|EMBL:OZG50775.1, ECO:0000313|Proteomes:UP000216725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24742 {ECO:0000313|EMBL:OZG50775.1,
RC   ECO:0000313|Proteomes:UP000216725};
RX   PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA   Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA   Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA   van Sinderen D., Ventura M.;
RT   "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT   family.";
RL   BMC Genomics 18:568-568(2017).
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:OZG50775.1}.
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DR   EMBL; MWWR01000014; OZG50775.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261EVC2; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000216725; 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   Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT   DOMAIN          36..177
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          392..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..783
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..828
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..886
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   934 AA;  95774 MW;  24927B88DFB01732 CRC64;
     MALALYRRYR PDTFDGVIGQ RQVTEPLCRA LDNNRLTHAY LFSGPRGCGK TSSARILARC
     VNCVEGPTSH PCGKCDSCRE LAANGPGSID VMEIDAASHN GVEDARDLRD RVTYGPTRDR
     YKIIILDEAH MVTPQSFNAL LKTVEEPPDN VMFIFATTEP DKVIGTIRSR THHYPFRLVP
     PEIMGPYLEE VCSKESITPE QGVLRLVMRA GGGSVRDTLS VLDQLMVGAD GGTITYDSAV
     RLLGFTPDSL IGEAIDAVID SDGAKLYGIV NKVVVGGYEP KKFVDDLLSR VRDLMVLTLA
     GEQAESVISD DVRVEDDAEL RRQASALGLP KLTWMAETIN EALEQMAGAI SPRMRLELLA
     AKLLVPADYE PAPGAGAPAA APGVSVGAVP GNRGAGSAGP RASAASAGPA NSVAPRQGQG
     DSAGARPNAG ITSSDALTSA LSQMNAESAT LDSALSGAGR QGEGRPAASE AAPQQASRPA
     AQPQRGAASA AAAAPASGAA SVADGNVDEM WDTAVASLPD DAKVFVDRSQ VPTVHLHRDP
     RNPARARLNL TFVHPVAQQA FSLAISGDKP VTRLTAEAVQ KVFGSGTAIA PTPQTADGKK
     SVPLSRMPEQ EQQAARRAAL MYGIQLRGGS ALGSASDLQT PARATEGQSS GSGEGHGAAQ
     GSGAQAGDSS DGSGSGDSDN SDRGHAGASA PSAGGMPHGT GASSAPAGPP AGSSAGSSAA
     QDAVDPWAGQ PSLAQVQPIE PTPEHHQKHV AVPDDSDSVD PWATQAPSQA PARAAQTVTR
     ASQAAMREPA PAGPAHASHA SANPASASPA LAGPAQQSVP QTAGQSFEPV GFGTPAASQG
     AANPGAPAAF AAPARPAPQA PQAQPGPYPA NPYQPGPYPD DAPEGGPGYP DDPGDEYSLD
     DANYDDTLTI DQIAKMLDAK EIRQVTKDGE NGTV
//
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