ID A0A1H9L861_9BACI Unreviewed; 1429 AA.
AC A0A1H9L861;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN04487944_101137 {ECO:0000313|EMBL:SER07357.1};
OS Gracilibacillus ureilyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=531814 {ECO:0000313|EMBL:SER07357.1, ECO:0000313|Proteomes:UP000199687};
RN [1] {ECO:0000313|EMBL:SER07357.1, ECO:0000313|Proteomes:UP000199687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7727 {ECO:0000313|EMBL:SER07357.1,
RC ECO:0000313|Proteomes:UP000199687};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC also exhibits 3' to 5' exonuclease activity.
CC {ECO:0000256|ARBA:ARBA00003452, ECO:0000256|HAMAP-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|ARBA:ARBA00004496,
CC 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}.
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DR EMBL; FOGL01000001; SER07357.1; -; Genomic_DNA.
DR STRING; 531814.SAMN04487944_101137; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000199687; 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; cd06127; DEDDh; 1.
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 Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR HAMAP; MF_00356; DNApol_PolC; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR024754; DNA_PolC-like_N_II.
DR InterPro; IPR028112; DNA_PolC-type_N_I.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR006054; DnaQ.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR006308; Pol_III_a_PolC-type_gram_pos.
DR InterPro; IPR044923; PolC_middle_finger_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00573; dnaq; 1.
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; PF14480; DNA_pol3_a_NI; 1.
DR Pfam; PF11490; DNA_pol3_a_NII; 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; 2.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000199687};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 329..396
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 414..580
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 185..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 157..184
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 185..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1429 AA; 163304 MW; 2D43B172B92F8AD5 CRC64;
MDSTNRERFN LLMQQIGIPD DMKNKYLQNG MIEKLEVFRQ TKVWQFSFRL EKLLPADVYQ
LFVLKLTDAF SSIAKVSWKF SAENTALEEN EWSKYWFIFL SELINESPKY RVLENKKPLF
NDNNIMLTTS NDIERQSLMQ DLQKRFDEFS RHVGLTKRMI QIDVVEQQDE IERFQQEKAL
EDKKRVEEAF KQQAERSKDN KDEKSSGPVM IGYPVKEEPV QMRDIIEEEK NVVFQGYLFD
AEIRELRSGR HLLMLKMTDY TDSFQIKMFS KGDQDVEKFK QLKQGMWLKT KGMIQTDTFS
NELTMMAKDI QEVKAKSRED HGMDGEKRIE LHAHTLMSQM DSVVSASKLV EQAAKWGHKA
IAITDHAVAQ AFPEAYGAGK KHGVKVIYGV EANIVDDGVP IAYNVQDREL FDETYVVFDV
ETTGLSAVYD TIIELAAVKI KNGEIIDRFE SFANPHKPLT ETIINLTNIT DDMLRDAPEV
EEVLTDFQKW MGDHILVAHN ADFDMGFINT GFKKIGLEEA SNPVIDTLEL ARFLFPDMKN
HRLNTMCKKL DIELTQHHRA IYDTEATSYL LWKFIKLSHE KGITNHNQFN KHMGEGNSYQ
RSRPFHATLL AKNEVGLKNL FKLISLAHID YFYRVPRIPR SKLQQLREGI LVGTACDKGE
VFETMMQKSA DQAEKVAKFY DYIEVQPPAN YVHLVDKELV QNEAQLLDIL RKLVDMAERL
GKICVATGNV HHLDENDQIY RKILIASQSG NPLNRQKLPN TYFRTTNEML DAFSFLGQEK
AIEVVIKNPQ LISDEIDDVK PIKDDLYTPN IDGAEQEIRD LSYNFAKSIY GDPLPEIVEK
RIEKELKSII GHGFAVIYLI SHKLVKKSLN DGYLVGSRGS VGSSLIATFT EITEVNPLPP
HYVCPNCKHN EFFNDGSVGS GFDLPDKNCP ECQTPYKKDG QDIPFETFLG FKGDKVPDID
LNFSGEYQPR AHNYTKVLFG EDNVYRAGTI GTVAEKTAYG YVKGYAGDHD MVIKNAEVDR
LVKGCTGAKR TTGQHPGGII VVPDDMEIYD FTPIQYPADD RNSEWRTTHF DFHSIHDNLL
KLDILGHDDP TVIRMLQDLS GIDPQTIPTD DQETMKIFSG PEVLGVTPDQ IMCKTGTLGV
PEFGTRFVRQ MLEDTKPKTF GELLIISGLS HGTDVWLGNA QDLINDGICK LPDVIGCRDD
IMVYLMHKGL EPSLAFKIME FVRKGKGLQD EWIEEMKKHD VPDWYIDSCK KIKYMFPKAH
AAAYVLMAIR IAYFKVHYPI FFYAAYFTVR ADDFDLDTMV KGSEAIRNRI KDIIAKGNDA
SPKEKNLLTV LELALEMNER GFHFQKVDLY RSSATEFIVE GDSLIPPFNA VDGLGTNAAI
NIAKAREDGE FLSKEDLRER SRISKTVLEY LDQHGCLEGM EEKNQLSLF
//
