ID A0A1H0A621_9BACI Unreviewed; 1433 AA.
AC A0A1H0A621;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN04488053_101375 {ECO:0000313|EMBL:SDN29242.1};
OS Alkalicoccus daliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX NCBI_TaxID=745820 {ECO:0000313|EMBL:SDN29242.1, ECO:0000313|Proteomes:UP000198778};
RN [1] {ECO:0000313|Proteomes:UP000198778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10369 {ECO:0000313|Proteomes:UP000198778};
RA Varghese N., Submissions S.;
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|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; FNIL01000001; SDN29242.1; -; Genomic_DNA.
DR STRING; 745820.SAMN04488053_101375; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000198778; 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; 1.
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; 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; 2.
DR Pfam; PF00929; RNase_T; 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}; Reference proteome {ECO:0000313|Proteomes:UP000198778};
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 161..188
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1433 AA; 162714 MW; 3E4DB5620A4A514A CRC64;
MALDKEARKA RFQLLMQQIQ MPEDFVSRYA ESAYIEKLEI YQSAQKWHFH FVMPVILPFP
AFELLESRIV QGLNHIAEAD FSIRCEEEAD AGEMIKSYWP YFVEHLRKAT NGLIKRLEAQ
QPKIENNRLY ISVMNEAEAE IIERRVSIPL KALLFKTGFP ELQIATEIKE AKEEIQKFEE
QKQEEDHNKV VEAMLEQKKQ QEQAQELGQN QKVAVGMAIK DDPVPMEQII EEEKRITVQG
YVFSAETREL KSGRVLLTFK ITDYTDSLLI KVFSNDKEDI PLLEAVKKGM WIKARGAVQY
DTFIRDMTMM ARDFHEVKPR LIEDKAPEDE KRVELHVHSN MSSMDAVTSI SDYVKRAKEW
GHQAIGLSDH AVAQSFPEAY AAGKKHGVKI LYGIEANLVD DGVPVAYNAV TRDLQDETYI
VFDVETTGLS AVYNTIIELA AVKIHNGEVI DKFESFADPK EKLSPTIIDL TGITDDMVKG
QPEPGEVLKE FYDWCGNDTL VAHNASFDIG FLNAGYQKIG YDKVKNPVID TLEFARMLYP
HFKNYRLNTL CKKFNIELVA HHRAIYDAEA TAHLLWKMVK DAIEKNIHTH DSLNEQGSSD
DYKKQRPMHC TIYASTKAGL KNLYRLISMS HIDYFYRVPR IPRSVLVKNR DGLLVGSACD
KGEVFDALMQ KGLEESKDTA SFYDFIEVQP PGNYQHLVER EIVRDELALK DILKQLVKLG
EEIDRPVVAT GNAHYLDKED YVYRKILIAS QGGANPLNRQ TLPQVHFRST TEMLEEFSFL
TEDKAKEIVV HNSQAIAERI DEIKPIPDDL YTPHIEGADE EMRQLCYDMA KSIYGEELPQ
LVIDRLEKEL TSIISNGFSV IYLISQKLVK KSLNDGYLVG SRGSVGSSFV ATMTEITEVN
PLPPHYVCPN CKHSYFFNDG SVGSGFDLPD KHCEKCGELY DKDGHDIPFE TFLGFKGDKV
PDIDLNFSGD YQPKAHNYTK ELFGEDFVYR AGTIGTVAEK TAYGYVRGYE SDEALQLRGA
EIDRLVQGCT GVKRTTGQHP GGIIVVPDHL DIYDFSPIQF PADDRESEWK TTHFDFHSIH
DNLLKLDILG HDDPTVIRML QDLSGMDPKK IPIDDPEVFK LFSGTESLGV TEEQILCKTG
TYGIPEFGTR FVRQMLEETK PSTFSELVQI SGLSHGADVW LNNAADLIAA GTCQLKDVIG
CRDDIMVYLM YKGLDHPLAF KIMEFVRKGK GLEEEWIEEM KKHGVPDWYI GSCLKIKYMF
PKAHAAAYVL MAVRIAYFKV HEPMMFYAAY FTVRADDFDL DTMIRGSASI KKQIEEIQAK
GLDASPKEKS LVTVLELSLE MCERGFSFEK VDLYRSKATE FQVDGDKLLP PFNAITGVGT
NAAIAIEKAK EDGEFLSKEN LRERSKITKS VLEKLDDHGC LEGLPDSNQL SLF
//
