ID A0A1M4VVS1_9FIRM Unreviewed; 896 AA.
AC A0A1M4VVS1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN02745190_00997 {ECO:0000313|EMBL:SHE72832.1};
OS Schwartzia succinivorans DSM 10502.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Schwartzia.
OX NCBI_TaxID=1123243 {ECO:0000313|EMBL:SHE72832.1, ECO:0000313|Proteomes:UP000184404};
RN [1] {ECO:0000313|EMBL:SHE72832.1, ECO:0000313|Proteomes:UP000184404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10502 {ECO:0000313|EMBL:SHE72832.1,
RC ECO:0000313|Proteomes:UP000184404};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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. {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; Evidence={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; FQUG01000004; SHE72832.1; -; Genomic_DNA.
DR RefSeq; WP_072935103.1; NZ_FQUG01000004.1.
DR AlphaFoldDB; A0A1M4VVS1; -.
DR STRING; 1123243.SAMN02745190_00997; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000184404; 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; cd07435; PHP_PolIIIA_POLC; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.30.1900.20; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 1.10.150.700; PolC, middle finger domain; 2.
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; 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 PANTHER; PTHR32294:SF5; DNA POLYMERASE III POLC-TYPE; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 2.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000184404};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00356}.
FT DOMAIN 19..88
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT COILED 208..235
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 896 AA; 102080 MW; 87262B5DA2B95BFA CRC64;
MSDNVCAQSR NDNAKVKRVE LSVHTKMGPM DSVVPVRELI RTASHWGWDA IAITDHGSVQ
AFPDAMYAAE YNPFDIKVIY GMEGALTEDH YQHLCANHIT ILAKNMDGLH NLYRLVSLSH
LFFGRCIVSQ SDLYSNRYAP RIPRSILKEH REGLLLGSSG AEGELIRAIA SCHYEDEELI
TVARFYDYLE IQPIGNYAHL LRSNEFPHIN TEEDLRDINR KVAALAKKLD KLLVATGDVH
FLHPEDAICL EVLTAHNDSD ETIPQPSLFL HTTEEMLKAF EYLGEEAAYE AVVTNSRRIA
DMIERIKPIP YDLFDSILPN ADEEIKTMAY KRAHELYGEN LPEIVQNRLD QELTPILKHG
FSSLYLIAHK LVKKSNDDGY SVFVRGSVGA SFVATIAGIT EVNPLAPHWH CTKCHYSEFI
TDGTYNSGFD LPEKNCPNCG EPLIKDGHDI PFAAFLGYDG DKVPDIDINY SDEERPELCK
YIERLFGKDK VYAAGTIETL SEPEMRRYIQ KYFDKKGETP SENFIQYIVN RCVGVKKTTG
VHSAGIYIVP QEIDVNWVTP VQHPEDRLEF SDVVTTHFDY HSISHCLVKF DIIPHKVPTC
LKLLEEYTHR NHRTIPFNDP ETLSIFRSTE ALGVSPEELG TKIGTFGIPN FYSLNTRQIL
DETKPTYFSD IVKISGFCHG TEIWENNMQD ALRDGICTMH DAISVRDDIM MYLIHKGIEP
SIAFKAMEST RKGKGLKPDV VEQLKTSGVP EWYIEACQKV KYLFPRAHAT SYVMMAYRIA
YYKVHYPAAF YAAYFSVYDE AFDADVITVG KEAVKKRISE LSAKYPDLEE DSRKLSWERY
EELKPVLAKF FALQVALEML LRGFTIEPIN PNHSDTEQFI IFDKYMKPLF AVHGKS
//
