ID A0A0Q5CJM2_9MICO Unreviewed; 1159 AA.
AC A0A0Q5CJM2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=ASF54_02510 {ECO:0000313|EMBL:KQQ27673.1};
OS Frondihabitans sp. Leaf304.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ27673.1, ECO:0000313|Proteomes:UP000051456};
RN [1] {ECO:0000313|EMBL:KQQ27673.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27673.1,
RC ECO:0000313|Proteomes:UP000051456};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ27673.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27673.1,
RC ECO:0000313|Proteomes:UP000051456};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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:KQQ27673.1}.
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DR EMBL; LMNV01000002; KQQ27673.1; -; Genomic_DNA.
DR RefSeq; WP_055958428.1; NZ_LMNV01000002.1.
DR AlphaFoldDB; A0A0Q5CJM2; -.
DR STRING; 1736329.ASF54_02510; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000051456; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07431; PHP_PolIIIA; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF4; ERROR-PRONE DNA POLYMERASE; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000051456};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT COILED 755..782
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1159 AA; 126450 MW; F796207EE08E4A0D CRC64;
MAFTHLHVAS SFSAHFGTAT PMDLVAQAVA SGADAAAITD RDGLYGAIRH VGACRAAGID
PIVGVELGVL SDAEGGSARG RSAADTDRIV VLAHGSPAGG VAAGAGWASL CRLISAAHGR
ATRKTSGTAN SVATIARSRL RAFLLGDDGP AGTVLLGPDS DVGRAVSRGD HAKAMALLDD
WKTLLPGGVV VEVVCHLTEP GESRSLRHAA RMLELADAAR VPAILSNAVR YLEPDGAVTA
DVLDAAGHLA ALGSFEPQPN AQAWLKGPGA MRELAQQIAS VSSLDRRSAE EMLAATEELA
DRCRLDPDAD LGWRRPKVPE LSAIGVEGDP DQVLWRRSEA GITERFGDVS MAKREKLERR
MRDELKTITG FGFASYFLTV ADVSQLMRDM RVRNAARGSG AGSLVTYLLR ISNVDPLEHD
LLFERFLGNK RETLPDIDID VESARRHEIY RAIFDRYGSN RVTLMSMQST YRGRGAVRDA
GLALGLDDEQ IDLVAKNVWR SNARDFRTAL AEKPELREIA DLARENDQIE LLVDLTERLD
RLPRHISMHP CGVILGDSDL LSMTPVQPSG MGLPMSQFDK HDMNDAGLLK LDVLGVRMQS
SMAFALDEIE RINGPRTALA GALPLDVPYV NRQGRIELDA IPHDDEPTYE AIRTTHTLGM
FQIESPGQRE LIGKMQPDQY EDLIADISLF RPGPMKGNMV APYLDTKHGF QQPDYLHPSF
AEFLQDSYGV VIYHEHVLRI LNATMGISLA EADEMRRAMT KRDDLEDEFR QKTRDNRDAQ
GRSKFTEKEI DRIWGVLKGF GSFGFCKAHG AAFALPTYQS AWLKTHYPAE FLAGILTHDP
GMYPKRLLLT EAKRMGIPVL PLDVNASSDV FHVERVKPPR TPVARSYPGE LGIRLSLVDV
QGITEAEVTR ILENRPFTSI ADFYQRATPS RRLFERLGQV GALDSLGGEG RTRGDVLARI
RQLTGRASRP KATDALNQLD FDVDESSSVP IGTPDVSVRE RVSRELDILS LEVGEHVIES
YRPMLDDLGV IRAADLRNNW NGTTVLVAGI RIATQTPPMR SGKRVVFISL DDGSGCSDST
FFEEAQNRAG SLLFGTKLLL IQGRTRRTGE RGISLEADNA WDLKTLWRDW QAGRVAGGSL
GEGVDASVSD GLDAGLVSP
//
