ID U2T0D9_9FUSO Unreviewed; 1436 AA.
AC U2T0D9;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=HMPREF1984_00696 {ECO:0000313|EMBL:ERK68207.1};
OS Leptotrichia sp. oral taxon 215 str. W9775.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1321779 {ECO:0000313|EMBL:ERK68207.1, ECO:0000313|Proteomes:UP000016640};
RN [1] {ECO:0000313|EMBL:ERK68207.1, ECO:0000313|Proteomes:UP000016640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9775 {ECO:0000313|EMBL:ERK68207.1,
RC ECO:0000313|Proteomes:UP000016640};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERK68207.1}.
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DR EMBL; AWVR01000022; ERK68207.1; -; Genomic_DNA.
DR RefSeq; WP_021767860.1; NZ_KI272873.1.
DR STRING; 1321779.HMPREF1984_00696; -.
DR PATRIC; fig|1321779.3.peg.671; -.
DR eggNOG; COG2176; Bacteria.
DR HOGENOM; CLU_003297_2_0_0; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000016640; 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; 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; PF07733; DNA_pol3_alpha; 1.
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 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}; Reference proteome {ECO:0000313|Proteomes:UP000016640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 327..393
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT DOMAIN 411..576
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 1436 AA; 164314 MW; CF517C2D132087FB CRC64;
MSAKYLKLKP SNDFTAKYDM KSFKIEHINL FSKKRAMEIH VKVNDYNANE ELADLRKLLY
KSLGTALQLS IKITVEPETL ERDVQGFIRF IIDNYKSESA RHQYIFANYE VDNIEDNIFI
KLPSEHLIEH GRNSDILREL KQRIYNATGK NFNLEFTSGD FEKIHKMIEE KKKNLEKAVK
VEELPVFEPP KEETKEKWNG NKGNTLHSDY RKKVSDRKAS DFSVLDSLNL NEEIALEGHI
FHIDISETKN GNTKCDFIIT DYADSIGCRI FLKKSEDVKI GLNDWVKVIG RLEADRFNGE
YYINTKKIDK IEPKMKARKD NAEKKRIELH AHTNMSEMSG VVSAKDLAKR AKEFGHEAIA
VTDFGVVHSF PFAYKESNDN FKIIFGVEAY VVDDEQDMIT KPSDKLIEEE VYVVFDIETT
GLDPYNDKII EIGAIKLKGK EIIDEFSVFV NPEMNIPEEI TRLTNITNDM VKDADNIEKV
LPEFLEFCKD TTVVAHNAKF DVGFINQKAK NQGLEYSPSV IDTLHWARVL LPDQKRFGLK
NVANYFNISL DNHHRAVDDA KATAEIFQKF LNMVLSRGIL KLTEISRELE TNIQNAETLN
TMILVKNQAG LRDLYELISR SHIEFFGNRK PRIPKSLLNE KRENLLIASS ASAVFGNNGE
LANMFIRGSD LKDIEERAKF YDYIEIHPMT NYVDLEGTGD IESLDKIVEM NNYFYNLGKK
LGKIVVATGD AHYLEEREAV NRSVLILGSG MGRRIFSYDK RLFFRTTEEM LEEFSYLGED
KAYEVVVENT HKINDMIEKV RPIPTGFYPP KIEGAEEEVR QMTYAKLHEL YGENVPEHLK
ERIEKELNSI IGNGFAVLYL IAQKLVKKSL DNGYLVGSRG SVGSSIVAYL MGITEVNGLY
PHYRCPNCKH TEFMEFEGSG PDLPDKVCPE CGTKYIKDGH AIPFEVFMGF NGDKVPDIDL
NFSGEYQGEI HKYTEELFGS DNVFRAGTIA TLAEKNAFGY VRKYFEEIEG SPEISKRKAE
LTRIAKGCEG ARKTTGQHPG GMIVVPSDKS IYDFCPIQRP ANDMNAESKT THFDYHVMDE
QLVKLDILGH DDPTTLRILQ DLTGVDIYSI PLDDEKVMSL FSGTEALGVE PADIDSKTGS
SGIPEFGTSF VKQMLMDTKP KTFAELVRIS GLSHGTDVWL NNAQEYVRQG IATLSEIITV
RDDIMNYLID NGLDKSVAFT IMEFVRKGQP TKNPEKWKEF SEIMKKHKVK QWYIDSCEKI
KYMFPKGHAV AYVMMAVRIA YFKVYYPLEF YTAFLNRKAA DFKMTAMFKP VDELKRSKKE
LDAKGNLNAK EKQELFLYEI LIEMHYRKIE LMQIDIYKSE ATSFTIEDGK IRMPLIAMDG
LGESVAVNVV NERKKGEFLS MEDLVKRTKL NKTVMDLLKT YECVPELSAT NQQTLF
//
