ID A0A415E4J9_9FIRM Unreviewed; 1274 AA.
AC A0A415E4J9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=DNA polymerase III PolC-type {ECO:0000256|HAMAP-Rule:MF_00356};
DE Short=PolIII {ECO:0000256|HAMAP-Rule:MF_00356};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_00356};
GN Name=polC {ECO:0000256|HAMAP-Rule:MF_00356};
GN ORFNames=DW099_09225 {ECO:0000313|EMBL:RHJ88550.1};
OS Emergencia timonensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Eubacteriales Family XIII. Incertae Sedis; Emergencia.
OX NCBI_TaxID=1776384 {ECO:0000313|EMBL:RHJ88550.1, ECO:0000313|Proteomes:UP000284841};
RN [1] {ECO:0000313|EMBL:RHJ88550.1, ECO:0000313|Proteomes:UP000284841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM07-24 {ECO:0000313|EMBL:RHJ88550.1,
RC ECO:0000313|Proteomes:UP000284841};
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 -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC also exhibits 3' to 5' exonuclease activity. {ECO:0000256|HAMAP-
CC Rule:MF_00356}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00356};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00356}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00356}.
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:RHJ88550.1}.
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DR EMBL; QRMS01000002; RHJ88550.1; -; Genomic_DNA.
DR RefSeq; WP_067542842.1; NZ_QRMS01000002.1.
DR AlphaFoldDB; A0A415E4J9; -.
DR STRING; 1776384.GCA_900086585_04203; -.
DR GeneID; 83006474; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000284841; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd07435; PHP_PolIIIA_POLC; 1.
DR CDD; cd04484; polC_OBF; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.30.1900.20; -; 2.
DR Gene3D; 6.10.140.1510; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.150.700; PolC, middle finger domain; 1.
DR HAMAP; MF_00356; DNApol_PolC; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR006308; Pol_III_a_PolC-type_gram_pos.
DR InterPro; IPR044923; PolC_middle_finger_sf.
DR NCBIfam; TIGR01405; polC_Gram_pos; 1.
DR PANTHER; PTHR32294:SF5; DNA POLYMERASE III POLC-TYPE; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 2.
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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00356};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00356};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_00356};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_00356};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00356};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00356};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00356}; Reference proteome {ECO:0000313|Proteomes:UP000284841};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 356..431
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 194..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 143063 MW; 00AD00823DFD00FA CRC64;
MRELIDKHIN WQGIGNHETG EYHYDITEAV ISKETGVLTI KLRLNFIMPS LDMEKLRGII
LHSIDHLSDV KFEYIYADMI LDEKETVKLF IPHMIEIING KYAAITKTIQ TDKFTFDGEH
LKIYALGKLS TEQLNEKVAH LFQQLLNDNF GINTQVTFLN DEEVYSKAAE SWKASEESDI
KASLAAATRA AAEVRKSQPD KPAFDGGGNS QGGGFGGGQQ KGGWKRREKE APAEGNRIMG
KDIMGQSVSL SSLSADSGVV IVEGILFKKD SRPIKNEKKL VTLLITDKKT SVCLKAFCSN
NKWDEIDSLL KSGDYIKVRG ETEWDRYDNC LVVMLKDINK SKIKKREDTF EGGKRVELHA
HTKMSAMDGL NEVENLVKTA AYWGQPAVAI TDHGVVQSFP DAAKTAKKLA GNKDNPIHIN
IIYGMEGYVF DDSDCHNADG TIDFKKKPTN HIILLARTQE GLKNIYKLVS YSHLNYFYKR
PRLPKSLIEE HREGLIIGSA CEAGEVYRAI AGGKSQEEIE EIASFYDYLE IQPLINNQFM
IDNGMVSGKE ELKEHNRQIV ALADKMGKLV VATTDAHYDE PESAIYRNIL MAGMGFKDAE
NGQGLYMRTT DEMMEEFSYL GEETAYKVVI ENTNKIADMI DEGILPVPKG KFPPKIQGAE
ETLRTTCMEK AYSIYGDPLP DRIGERLEKE LSSIIDNGYA VMYVSAQMLV HKSMEDGYLV
GSRGSVGSSF AATMAGITEV NPLEPHYICP NCKKLIWGDM ELYDCGIDMP ELDCPECATP
MHRDGYTIPF ATFLGFNGDK EPDIDLNFAG EYQATAHKYV GEIFGEKNVF KAGTVGTVAD
KTAYGYVMKF ADEFNRPINK FEADRLTQGC TGVKRTTGQH PGGIIIVPDD HEIYEFCPVQ
HPANDVKSDI ITTHFDYHKI DENLLKLDIL GHNIPSMIRQ LQDMTGIDPM KADLTDRKVL
SIFNGIEALD IKDPDYKFTH GSYAIPEFGT GFVRQMLDDT KPDKFADLVR ISGFSHGTDV
WLNNAQDYIR SGVATMREVI STRDDIMNYL ILKGIENKTS FQIMEDVRKN RPLKDEQLAV
MKEHGVPDWY IDSCIKIQYM FPRAHAVAYV MMSFRMAWYK VYYPVEFYAT YFTSTVANFD
ADTILKGPQA CLDRIEMINA MGNNATAKEQ SDILILEVAY EMYSRGYEFA MARLGKSQAL
KFWSDEGKVL LPFVALDGVG DTAAKAFADA YEEKPFGTIE EAVHRSKLNK TAVEALRTHG
VFEGLPETDQ LSLF
//
