ID   A0A374BNQ2_9BACT        Unreviewed;      1237 AA.
AC   A0A374BNQ2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=DW917_15410 {ECO:0000313|EMBL:RGH35266.1};
OS   Prevotella sp. AM42-24.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=2293125 {ECO:0000313|EMBL:RGH35266.1, ECO:0000313|Proteomes:UP000263324};
RN   [1] {ECO:0000313|EMBL:RGH35266.1, ECO:0000313|Proteomes:UP000263324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM42-24 {ECO:0000313|EMBL:RGH35266.1,
RC   ECO:0000313|Proteomes:UP000263324};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-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:RGH35266.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QTXV01000089; RGH35266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A374BNQ2; -.
DR   Proteomes; UP000263324; 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:RGH35266.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RGH35266.1}.
FT   DOMAIN          5..82
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1237 AA;  140573 MW;  D62CB2612DA3A578 CRC64;
     MEDFIHLHVH TQYSILDGQS KIPHLVDKAV KDGMKGMAVT DHGVMFGIKE LTDYCGKVNK
     GRKKEGLEPF KPIIGCEMYV AHRRKEDRDK NRGDMSGYHL IVLAKNYNGY KNLIKLVSNS
     WVDGYYMRPR TDRADLEKYH EDLIVCSACI AGEVPKKILD GDIEGAREAC EWYHHLFGDD
     YYLELQRHKV PDDPRILANR EAYELQQRAN KVLIEFAKEY GIKLICTNDC HFEDKETAEA
     HDHLLCLATG KDLDDPNRMR YSKQEWFKTR EEMNEVFSDI PEALSNTLDI YNKVEIYSID
     HGPIMPFFPI PETFGTEEQL REKVSEEDLY KEFTSDENGE NQLPPEEGQK VIDRLGGYDK
     IYRIKFEAEY LKHLAYEGAK KLYGDPLPEN VDEHVNFELH VMKTMGFPGY FLIVSDFIRA
     AREELGVVVG PGRGSAAGSV VAYCLGITKI DPLKYDLLFE RFLNPDRVNL PDIDTDFDDD
     GRGKVLRWVM DKYGHENCAH IITYGSMATK NSIKDVARVE KLPLDKANAL CKAIPDRLPD
     GAKMNLTNAI KYTPALRDAE FSTDPRESNT IKYAKMLEGT IRGTGIHACG FIICRDPISN
     WVPVSTADDP DFPGLKTAVT QYDGHVIEST GLIKMDFLGL KTLSELKEAC KVVKQTLGED
     VDLDTIPIDD ALTYELYQRG QTIGTFQFES PGMQKYLREL KPTVFEDLIA MNALYRPGPM
     DYIPSFIARK NGQEEIKYDI PCMEKYLKDT YGITVYQEQV MLLSRQLANF TRGESDALRK
     AMGKKKKDIV DAMKPKFIKQ GQENGHDPAI LEKIWGDWEK FASYAFNKSH ATCYSWVAYQ
     TAYMKAHYPA EYMAALMTRR FSQITEITKL MEECQSMNIK TLGPDINESY RAFGVNEHGE
     IRFGLSAIKG MGAPAADAIV AEREKNGAYK DIFDFAQRVD FSNVNRKAFE SLALSGGFDS
     FGIPREDFFA KDSKGNVFLD TLVKYGQLYQ REQQEAVTSL FGGVEAVEIA TPPIPKGEPW
     STIEKLNKER ELVGIYLSAH PLDDYSIVLH SMCNTHCTEL GDKEALSKKA EIVFGGIVTA
     LRSTFTKTGK PCGFVTLEDF EGSGELALFG EDWGQWRGML VEGSTVYVTA RCAPRYANSN
     YLEFKINSID YMQTIKENRI EKLTITLDSD IVDDTVINDF NTMLKDDLAG KTQLYFQIHD
     VESNTFIMFR AQDKTVNVGK ELIQYIEAHP KMSYHIN
//