ID A0A3A9JP27_9THEO Unreviewed; 1421 AA.
AC A0A3A9JP27;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-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=DXT63_13690 {ECO:0000313|EMBL:RKL62059.1};
OS Thermoanaerobacteraceae bacterium SP2.
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae.
OX NCBI_TaxID=2292448 {ECO:0000313|EMBL:RKL62059.1, ECO:0000313|Proteomes:UP000271566};
RN [1] {ECO:0000313|Proteomes:UP000271566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|Proteomes:UP000271566};
RA Grouzdev D.S., Krutkina M.S., Patutina E.O.;
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|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:RKL62059.1}.
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DR EMBL; QSNL01000027; RKL62059.1; -; Genomic_DNA.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000271566; 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; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
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 PANTHER; PTHR32294:SF5; DNA POLYMERASE III POLC-TYPE; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 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; SSF160975; AF1531-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53098; Ribonuclease H-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:UP000271566};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 321..388
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 406..571
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1421 AA; 160892 MW; E16EA8C456A67EAC CRC64;
MINLKQILEK EDLIDFDKSE LQAISKVSVK KVLVDLEKRK LEIYFKSENE IAGYLYDKIK
SRLYQKIPGC KHINVISDDS IHNNVDAEEI IKNNWQSILE HVFSHAPSAR IWLLNASMDI
QKNHFVIYVD KSGMEFLERK KCNLIIEKFL RSKDIQVKVT FVQKTDEEEE YDIYEEDREI
VETLLSQNIN GSSEKSNHES DSGILLGKTI SGEPVPIRDA FMETQDITVQ GEIFGVEKRE
LKNKTIMVTF ALTDYTGSLP VKIFLSGEKK VIEDKIKEGL WVKVRGKIES NKYSQEYELM
PYDINEAQKP VRQDPSPEKR VELHLHTRYS AMDAICSPKQ VIKLVKSWGH KAVAFTDHGV
IQSYPEIYEF AHGSGIKPIY GVEAYVFDDE FPVMVNPPDS ELQDVTFVVA DIETTGLSLE
NDEIIEVGAV KLKNGSIIDR FASFVKPSKA LPANIINLTG ITNEMVSSAP PLKEVLSGFI
NFLGDGIFVA HNARFDSGFI RRDCEKLGLP FDNKVLDTLP LCQIIYTDLK NHRLDTVAKK
LDIKMGNHHR AVDDANTAAL ILKEALAHLE KTGIKNLSHI NHIYHSSNGA VHLNSYHATI
LVKNMVGLRN LYELVSRSHL DYFYRHPRIP KSLLKSFREG LILGTGCQAG ELYQSLLHFS
SPEYIKRIVE FYDFLEIQPL QNNAFLVQNG MVSGKEALEK LNLQIYKLGK KFNKPVALTG
DVHFLNPEDE IYRKVLLKSQ GYEDADKDSC LYLKTTEDML KECEYLGKEA AFEVVVANTN
KIADEIEDDI KPVPDELYPP KIEGAEQEII NMTYKRAKEL YGDNLPDIVQ KRIERELNSI
VNHGYSVIYL IAHKLVKKSM EDGYLVGSRG SVGSSLVATM CGITEVNPLP PHYLCPECKN
AIFIQENEGI VGPDLPDKSC PVCGKPMKKE GFNIPFEVFM GFEGDKVPDI DLNFSGEYQA
KAHKFTEELF GRHHVFRAGT ISTIAEKTAF GFVKSYMEEK RINAPACEIK RLASGITGVK
RTTGQHPGGL MVVPRDMEIY DFSPVQYPAD DKESGVITTH FDYHSISSRL LKLDLLGHDD
PTVIKMLEEE TGIDARKIPL DDRDTMEIFS SLKSLKLEPE SVGTTVGTIG VPEFGTRFVR
QMLEDTRPST FAELVRISGL SHGTDVWLNN AQDLIKSKTA TLKDVIATRD DIMIYLLNQG
IEPKIAFTIM ENVRKGKGLK TEFEEILAKN KNIAPWFVES CKRIKYLFPK AHAVAYVIMA
FRIAYFKVHY PEAFYATYFT VRADDFDAEL ILQGPKKIRE TISEIEKKEK DASAKEKNLL
TILEVANEMY MRGIQFVPID LYKSDVKRFK ITDNGILPPL TALQGLGLAA AQSIAEERAK
GRFTSIEDLR QRARITKNVI QILKQNGIIS NLQETNQLCL F
//
