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
//