ID A0A1G6H7M9_9BACI Unreviewed; 1432 AA.
AC A0A1G6H7M9;
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 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=SAMN05421737_10335 {ECO:0000313|EMBL:SDB90221.1};
OS Shouchella lonarensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1464122 {ECO:0000313|EMBL:SDB90221.1, ECO:0000313|Proteomes:UP000242662};
RN [1] {ECO:0000313|Proteomes:UP000242662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=25nlg {ECO:0000313|Proteomes:UP000242662};
RA Varghese N., Submissions S.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC responsible for most of the replicative synthesis in bacteria. This DNA
CC polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC is the DNA polymerase. {ECO:0000256|ARBA:ARBA00025611}.
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. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
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; FMYM01000003; SDB90221.1; -; Genomic_DNA.
DR STRING; 1464122.SAMN05421737_10335; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000242662; 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; 2.
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; IPR016195; Pol/histidinol_Pase-like.
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; SSF89550; PHP domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
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:UP000242662};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 332..399
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 417..583
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1432 AA; 161184 MW; B5810F828261C6DD CRC64;
MDARKQTGQE RFQLLLEQLN MPATSLPYFK HGAIEKLAIL KAERTWHFYI TLEKLIPAEH
YAAFRSRLIT TFKEIAYTQC TITYKHAPSL AEAWPGYWSL LVEDLVKQTP SLANTWRKQT
PTVTNRALQL VAAHEAEAGM MNRKLKELAR PLCQSLGLAE MPFQITVKSS EADYEAFAEQ
RAQEDYSKVV EAMLEKKRRE EEGAKEEVVT SVSIGYPIKE EATPLEGIVD EERRITIQGY
VFSADIRELR SGRTLLTFKI TDYTDSILVK MFSRDKEDVP AMKAIKKGMW LKVRGGIQND
TFVRDLVMIA NDIAQYTPQL RKDTATEDEK RIELHAHSTM SQMDGMVSVE RYVKRAAEWG
HKAFAITDHG VVQAFPEAYA AGKKHGVKIL YGMEANLVDD GVPIAYNLAH RSLEDEVYVV
FDVETTGLSA VYNQIIELAA VKIKNGEIIE RYESFADPKE PLSAKIIELT GITDDMVQGA
KDPLDVLKEF RAFAGDATIV AHNASFDVGF VNVGYKKLGY DEVQNPVIDT LELGRFLYPE
FKNHRLNTLC KKFGIELTSH HRAIYDTEAT AYLLWRMVKD AAEKDIHYHD ALNDHMGKGN
FYRGRPSHCT LLVTSQEGLK NLYKLVTLSH VDYYFRTPRI PRSQLNRHRA GLLVGSACDK
GEVFEAMMQK SADEVTEIAR FYDYFEVQPP VCYQHLIEKE LVKDKETLQD IIANIVQLGK
ELEKPVVATG NVHYLDEEDA VYRQILIASQ GGANPLNRQT LPPVHFRTTA EMLAAFQFLG
EETAKDVVIT ATHDMASRIA DIKPIPDDLY TPKMAGADDE IRDMTYTRAR EIYGDPLPEI
VEARIQKELK SIIGHGFAVI YLISQKLVKK SLDDGYLVGS RGSVGSSFVA TMTEITEVNP
LPPHYVCPGC CHSQFFNDGS VASGYDLPEE NCPKCGTTYV KEGQDIPFET FLGFKGDKVP
DIDLNFSGEY QARAHAYTKE LFGAEYVYRA GTIGTVAEKT AYGFVKGFQS DHEFMMRGAE
IDRLVSGCTG VKRTTGQHPG GIIVVPDDMD IHDFSPVQYP ADDKNAEWKT THFDFHSIHD
NLLKLDILGH DDPTAIRMLQ DLSGIDPKTI PMDDPKVMEI FSGPEVLGVT AEQIMCKTGT
LGIPEFGTRF VRQMLEETKP KTFSELLQIS GLSHGTDVWL GNASELIANG TCELKDVIGC
RDDIMIYLIY KGLESSLAFK ITEFVRKGKG LQPEWIEEMR KHNVPDWYID SCMKIKYMFP
KAHATAYVMM AVRIAYFKVH YPALYYATYF SVRASDFDLD TMVKGEAAIK AKIEEINEKG
LDASPKEKSV LTVLELALEM CARGLSFQKV DLYRSQATEF IVDGETLLPP FSALNGVSTN
AGLGIVRERE AGHFLSKEDL QQRARLTKTV IEHLNDHGCL TDLPETNQLT LF
//
