ID A0A2T4U8A3_9BACI Unreviewed; 1433 AA.
AC A0A2T4U8A3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 ECO:0000313|EMBL:PTL39624.1};
GN ORFNames=C6Y45_04710 {ECO:0000313|EMBL:PTL39624.1};
OS Alkalicoccus saliphilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX NCBI_TaxID=200989 {ECO:0000313|EMBL:PTL39624.1, ECO:0000313|Proteomes:UP000240509};
RN [1] {ECO:0000313|EMBL:PTL39624.1, ECO:0000313|Proteomes:UP000240509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6AG {ECO:0000313|EMBL:PTL39624.1,
RC ECO:0000313|Proteomes:UP000240509};
RA Zhao B.;
RT "Alkalicoccus saliphilus sp. nov., isolated from a mineral pool.";
RL Submitted (MAR-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.
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}.
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:PTL39624.1}.
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DR EMBL; PZJJ01000005; PTL39624.1; -; Genomic_DNA.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000240509; 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; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.150.700; PolC, middle finger domain; 2.
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; 2.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
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; SSF50249; Nucleic acid-binding proteins; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 333..400
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 418..584
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT COILED 168..210
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1433 AA; 163196 MW; 9404E92D7807CDE4 CRC64;
MSIELQNRQE RFRLLMEQVQ MPDDFMKKYA EGAYIEKLEI HQKDHKWNFF IAMPKPLPFP
AFELLQTRIV QGLSHIAEVS LFLRYEENFQ AEELIESYWP YFIERLRSST NGLIQRLEAQ
VPRIDNNRMY LAVMNETEAE ILERRVKAPL KQLLAGAGFP DFIIATEVRE AKEEIKRFEE
QKQEEDHNKV VEAMLEKKKQ ESKAKELQDE QKVSVGMAIK DDPVAMEQII EEEKRITVQG
YVFHAETKEL KSGRMLLTFK ITDYTDSLLI KMFSNDKEDV PVMEAVKEGM WIKARGSVQY
DTFIRDLTMM ARDFHEIKPY VRTDEAKEES KRVELHVHST MSQMDAVTSI SDYVKQAGKW
GHPAIGLTDH AVAQSFPEAY AAGQKHGVKI LYGLEANLVD DGVPIAYNAS RRELKDETYI
VFDVETTGLS AVYNTIIELA AVKIKNGEVI DKFESFADPK EKLSPTIIEL TGITDDMVEG
QPDPGEVLKQ FYEWCGNDIL VAHNASFDIG FLNAGYEKIN YSKVKNPVID TLEMARMLYP
HFKNYRLNTL CKKFNIELVS HHRAIYDAEA TGHLLWKMVK DALEKNITVH EQLNEQGSAE
DYKKQRPVHC TIYAKTKEGL KNLYRLISMS HINYFYRVPR IPRSVLVKNR EGLIVGSGCD
RGEIFEGLMQ KGLEETKEAA AFYDFIEIQP PGNYAHLIEK EIVRDELALK DILKQLVKLG
EETGKPVAAT GNVHYLDPED YVYRKILIAS QGGANPLNRQ RLPQVHFRST DEMLNEFSFL
PEEKAEEIVV TATREIADSI DDIKPIPDDL YTPHIEGADE EMRQLCYDMA KSIYGEELPQ
LVIDRLEKEL TSIISNGFSV IYLISQKLVK KSLDDGYLVG SRGSVGSSFV ATMTEITEVN
PLPPHYVCPN CKHSYFFNDG SVGSGFDLPD KNCEKCGELY AKDGHDIPFE TFLGFKGDKV
PDIDLNFSGA YQPVAHNYTK ELFGEDYVYR AGTIGTVAEK TAYGFVRGYE NDEEMQLRGA
EIDRLVQGCT GVKRTTGQHP GGIIVVPDHL DIYDFSPIQF PADDRESEWR TTHFDFHSIH
DNLLKLDILG HDDPTVIRML QDLSGRDPKT IPVDDPEVFK LFSGTESLGV TEEQIMCKTG
TYGIPEFGTR FVRQMLEETK PSTFSELVQI SGLSHGADVW LNNAADLIAA GTCELKDVIG
CRDDIMVYLM YKGLDHPLAF KIMEFVRKGR GLEEEWIEEM KKHGVPDWYI GSCLKIKYMF
PKAHAAAYVL MAVRIAYYKV HEPMMFYAAY FTVRADDFDL DTMIRGSATI RKKIEEIHAK
GLDASPKEKS LVTVLELSLE MCERGFSFQK VDLYRSKATE FLVEGDTLIP PFNAITGVGT
NAALAVEKAR KDGEFLSKEN LRERSKITKS VLEKLDEHGC LDELPDSNQL SLF
//
