ID R7M806_9CLOT Unreviewed; 1462 AA.
AC R7M806;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=BN712_00576 {ECO:0000313|EMBL:CDE96526.1};
OS Clostridium sp. CAG:567.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262820 {ECO:0000313|EMBL:CDE96526.1, ECO:0000313|Proteomes:UP000018055};
RN [1] {ECO:0000313|EMBL:CDE96526.1, ECO:0000313|Proteomes:UP000018055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:567 {ECO:0000313|Proteomes:UP000018055};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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}.
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:CDE96526.1}.
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DR EMBL; CBJZ010000020; CDE96526.1; -; Genomic_DNA.
DR STRING; 1262820.BN712_00576; -.
DR Proteomes; UP000018055; 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; 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; 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; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 356..425
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 443..608
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 188..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1462 AA; 164848 MW; 950F5C36930AD311 CRC64;
MEELKTVKQV FRDYNSNSFA LSEAKVVCVN IYKKTNILEI KLKVASSILM KDLADFEKYL
AKRFNFKDID IKIESDGTDE NVNNKIHTEW TDIVEYMAYK HPLTKALLKN SAISIEDNRI
NVKLAMKGKM VLEARGFEKI LSSKLADLYH KNYVVSYQEE ITQEMIEQYQ EHARELEKQA
IMLAQKEAME QAEEKRQEKE KKIQGESAPI PDAPMPTDAD IPFEPEQEEN SPLIYGRSLK
IKEELSKVID LSVDSGKVLL DGEILNTDSR ELKSGKFLVT FDLYDGSSTI TCKAFVEAHK
HDAVIKRLKS ASGVKVNGTA QFDPFAKELG VIANVIIEST GIKREVRKDE AKVKRVELHM
HTQMSQMDGM TAAKDLLKRA VKWGMKSIAI TDHGVVQAFP DAHKYLEKDH PDLKVIYGVE
AYLAPDKTPC VSFSKNQPLD DTTYCVLDLE TTGFSFRTEK ITEIGIMKVR NGEVIDELST
FVNPEKPIPQ RVVEVTNITD DMVKDAPKIE EILPKVIEFV GDSVLVAHNA DFDIGFLKYN
CTLLGLKLGN TYLDTLRLAK DLFPEYKKYK LGIIAENLGI KVDVAHRALD DVDTTVKVLN
VMFDMLREKG VKTLDDIDEK LSGKADYKSL PTYHAIILAK DYVGLRNLYK LISVSHLHYF
YKKPRILKSL YKKYSEGLIL GSACEQGEIY RAIIAGKTDE EIEEIAADYD YLEIQPLGNN
MFMVRNETVK SVEDLKDINR KIVALGEKLQ KPVVATCDVH FMDPQDEIYR RILMAGQGYD
DADDQAPLYL RTTEEMLKEF DYLGEEKAYE VVVTNTNKIS DMCEKISPIS PEKCPPHIDG
CEETIKNIAY SKAHELYGDP LPEIVQARLD KELHSIITNG FSVMYIIAQK LVWKSNEDGY
IVGSRGSVGS SFVANMTGIT EVNSLPPHYR CPKCKYSDFT DYGVKNGFDL PDKICPNCGE
KLAKDGMDIP FETFLGFDGD KEPDIDLNFS GEYQAKAHRY TEVIFGKGTT FKAGTVGTVA
DKTAYGYVKK YYEEKGIPIS NAEVVRLSQG CTGIKRTTGQ HPGGIIVVPK GREIYEFTPV
QHPADDPNSD IITTHFDYHS IDQNLLKLDI LGHDDPTMIR MLFDLTGIDP TKVPLDDKDT
MSIFSSTKVL GVTPEQIHSE VGTFGIPEFG TKFVRGMLVD TKPTTFNELI SISGLSHGTD
VWLNNGQELV NQGIVTLSEA IGCRDDIMLY LIKKGLPPKP AFKIMEFVRK GKASKDPEKW
KEHEAMMREY NIPEWYIGSC QKIKYMFPKA HAAAYVTNAF RIAWFKVHKP AAYYTAFYTI
RADEFDSDIM CYGVEKVKNK MKEIDLQGNS ASTKDKNMYA ILELVLEMYE RGITFLPIDL
YKSHATKFIM ESDTEIRPPL NSIPGLGTVA AEGIDTAKKD GKFMSIDDMK IRSKIGTSVI
EMLQKVGCLK GMSQSNQLSL FG
//
