ID   A0A398CQ39_9BACL        Unreviewed;      1192 AA.
AC   A0A398CQ39;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, 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=D3H35_19855 {ECO:0000313|EMBL:RIE02878.1};
OS   Cohnella faecalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2315694 {ECO:0000313|EMBL:RIE02878.1, ECO:0000313|Proteomes:UP000266340};
RN   [1] {ECO:0000313|EMBL:RIE02878.1, ECO:0000313|Proteomes:UP000266340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2E09-144 {ECO:0000313|EMBL:RIE02878.1,
RC   ECO:0000313|Proteomes:UP000266340};
RA   Zhu H.;
RT   "Cohnella cavernae sp. nov., isolated from a karst cave.";
RL   Submitted (SEP-2018) 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:RIE02878.1}.
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DR   EMBL; QXJM01000039; RIE02878.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A398CQ39; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000266340; 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd04485; DnaE_OBF; 1.
DR   CDD; cd12113; PHP_PolIIIA_DnaE3; 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:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 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   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:RIE02878.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266340};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RIE02878.1}.
FT   DOMAIN          5..72
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   REGION          1079..1106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1192 AA;  132018 MW;  F10117C40088B14B CRC64;
     MCGFVHLHVH SEYSLLDGAA RIKEMTARAA ELGMTSLALT DHGVMYGAIP FYKACKERGI
     KPIIGMEAYI SAGSRHEKVS RKEQPIYHLT LLAKNEAGYR NLMKLSSIGH LEGFYYKPRI
     DFDALKEHAE GLIVLSGCLA SELSQLLLAG RYEDAKSTAL RYRQLFGDDY YLEIQDHGIL
     DQKKVTADVL RLAEETGIPL VATNDSHYLC EEDSALQDVL ICIGTGKTLE DTDRLKMTTT
     QLYMKSGEEM AALFRHVPEA VANTAAIADK CSLDIDFGRH ILPSFSPLPE GKTAAAYLAA
     LCEEGLAARY EGTEEWRDGK FRDTAVNRLR YELDVIGRMG FDDYFLIVWD FIRFARESDI
     ATGPGRGSAA GSLVAYSLRI TDVDPLKYKL LFERFLNPER VTMPDIDIDF SDERRDEVIR
     YVKTKYGSDH VAQIISFGTL AARAAVRDVG RVLNVPYGDV DKAAKLIPGM PGMSIERAAK
     ESTEFRALSE GGGPTGELVA MARRVEGMPR HASTHAAGIV MSPTPLTDYV PLQEGTDGVP
     LTQYSMEHLE AVGLLKMDFL GLRTLSIIER AMRWIREETG RELRWEDVPY DDPATYALLG
     RGDTTGIFQM ESAGVRKVLK DMKPSTFEDI VSVLALYRPG PMEFIPQFIR AKHGQAEVVF
     PHPSLEPILA DTYGIIVYQE QIMQIASGMA GFSLGEADLL RRAVGKKKRE VLDEQREHFV
     RGSLEQGHGE EAANRVYDLI VRFADYGFCR AHAAAYAVLA FQTAYLRAHY PVPFMASMLT
     AVIGNQRKTA EYVDDCRKMG IPVLPPDVNE SGVLFTPVRG EAIRFGLAAV KNVGTQAIDS
     LLRERSEQPY DSLTDLCRRV DPRACNKRVV ESLLLAGALD TLPGHRAQLL AALDETVEAA
     AAWRKEKEEL QIELFDFGDS PNWIVDLPEV APFTAQQTLE LERELMGLYL SGHPLDAFDG
     LMDELKLDRL MDMTDAQDGA TVLTAGMIVS LKPFVTRKGQ QMAFLEMEDR IMGTELVAFP
     TVWKNASSFV KKGSLVLVRA KVQQGDDDFK LLADDILPLE APDLTRQVER LRQLRGRISG
     VDAGARPSRE GAGAKPSQDG GLESAATSME ADALEGGMQR VYIRIDSTRE QTALLTRLKA
     LLSSHSGPLQ AVLIYERGRR TVALSDDLRV RPSPELFGAI EALMGEGSVR VK
//