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DPO3_MYCPU
ID   DPO3_MYCPU              Reviewed;        1435 AA.
AC   P47729; Q79E72;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=DNA polymerase III PolC-type {ECO:0000255|HAMAP-Rule:MF_00356};
DE            Short=PolIII {ECO:0000255|HAMAP-Rule:MF_00356};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_00356};
GN   Name=polC {ECO:0000255|HAMAP-Rule:MF_00356}; OrderedLocusNames=MYPU_6750;
OS   Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KD735-15;
RX   PubMed=7815943; DOI=10.1111/j.1365-2958.1994.tb00476.x;
RA   Barnes M.H., Tarantino P.M. Jr., Spacciapoli P., Brown N.C., Yu H.,
RA   Dybvig K.;
RT   "DNA polymerase III of Mycoplasma pulmonis: isolation and characterization
RT   of the enzyme and its structural gene, polC.";
RL   Mol. Microbiol. 13:843-854(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT   pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1408-1435.
RC   STRAIN=KD735-16;
RX   PubMed=7934878; DOI=10.1111/j.1365-2958.1994.tb01041.x;
RA   Dybvig K., Yu H.;
RT   "Regulation of a restriction and modification system via DNA inversion in
RT   Mycoplasma pulmonis.";
RL   Mol. Microbiol. 12:547-560(1994).
CC   -!- FUNCTION: Required for replicative DNA synthesis. This DNA polymerase
CC       also exhibits 3' to 5' exonuclease activity.
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:0000255|HAMAP-
CC         Rule:MF_00356};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00356}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. PolC
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00356}.
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DR   EMBL; U06833; AAA18178.1; -; Genomic_DNA.
DR   EMBL; AL445565; CAC13848.1; -; Genomic_DNA.
DR   EMBL; L25415; AAA65635.1; -; Genomic_DNA.
DR   PIR; C90596; C90596.
DR   PIR; S54697; S54697.
DR   RefSeq; WP_010925476.1; NC_002771.1.
DR   AlphaFoldDB; P47729; -.
DR   SMR; P47729; -.
DR   STRING; 272635.MYPU_6750; -.
DR   EnsemblBacteria; CAC13848; CAC13848; CAC13848.
DR   KEGG; mpu:MYPU_6750; -.
DR   eggNOG; COG2176; Bacteria.
DR   HOGENOM; CLU_003297_2_0_14; -.
DR   OMA; YYAAYFT; -.
DR   OrthoDB; 561611at2; -.
DR   BioCyc; MPUL272635:G1GT6-689-MON; -.
DR   Proteomes; UP000000528; Chromosome.
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   Gene3D; 1.10.150.700; -; 2.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00356; DNApol_PolC; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
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; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR006308; PolC_gram_pos.
DR   InterPro; IPR044923; PolC_middle_finger_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
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   SMART; SM00479; EXOIII; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
DR   TIGRFAMs; TIGR00573; dnaq; 1.
DR   TIGRFAMs; TIGR01405; polC_Gram_pos; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Nuclease; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1435
FT                   /note="DNA polymerase III PolC-type"
FT                   /id="PRO_0000204584"
FT   DOMAIN          404..562
FT                   /note="Exonuclease"
FT   CONFLICT        786..787
FT                   /note="NP -> S (in Ref. 1; AAA18178)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1233
FT                   /note="R -> KE (in Ref. 1; AAA18178)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1435 AA;  166375 MW;  9E6527A88725503F CRC64;
     MQESFLNFCQ EINFDIPEYL KNTKIANPYH DEEKSFFSCE IDFLETPKFE DFKSFYLKTK
     NFLNQLVKEQ KLLFKIENIF YEKSEIKKYL DWIAEHFFKN FDFKNTFRID DLKVNLDGKI
     FLTAHSKHSF DLYKDFVEFA NKKMQSFGFE NFLLKLELNQ IEITNNQPLV SSINSQVKTQ
     ASSENQSFKK SNFYNKKRHI QLSLKELIKT QEMFVSVVGM VFKKEIITTN SKTKIFKISI
     TDFQEATRAQ KFSYLEKDQE IFDSIQINDW VNVCGEIQLE KMSLKQFIKI EKIEKIRSPI
     KDRQDNEKEK RIELSFRSKM STMDGILSPL DIVKQAKKFN HSSIAILDHN SVQAFPDFHN
     LTYKDKDFKV IYGMTLSVIS KRNKIFVEPL KDKFFDYKIL DQEYVVYDIE TTGLSPMLNE
     LIQFGASVIK NGRIIETHHF FIKPKSKLDS FTTKLTGITQ EHLEKGYELQ EALEKISSIF
     KARIMVAHNA AFDHNFLKQK FIDNNIEFEE MISIDTLNLA KVLNPIYRSY RLGEVASKLS
     VVYDPSIAHR ADYDSSVLTN IFILQMSHLK EKGINLFKEL NSLSSEKFYS KMFAKDISII
     AKNQAGLKEL FKINSDVLTK YYFANPKMFW EDIKRSKNLL IGSGGLNSPL IDKLLFSTQE
     DVLNEIDKYD YIEIPSPNNF SHFWTTKFSD QQIKIQLQKL IKWAKEKNKI IVAIGEPRYN
     EKWQKIIHEI YINSTGIENS LHPLFIIKKD MDTFYPEQIY KTTNEMKQEF SFLYDPELIE
     EIVVKNPNLI SSQIEKIQVI KDKLYTPKFD DSHIKLKKLV YENAWKKYGK NLPEIIEQRI
     EKELTPILNY GFDVIYWISS ILVQKSLSDG YLVGSRGSIG SSLVATLSGI TEVNPLAPHY
     ICSKCQYFEL VKDPMTNSGF DLDDKKCPKC NSFLDKDGQT IPFETFLGFK ADKVPDIDLN
     FSGEYQGKIH DEVKRLFGSK HTFRAGTIST VAEKTAYGYI KKYLETASLD YSDNFVDFLT
     EKSTGVKRTT GQHPGGIIII PKEFDVEDFT PVNFPANDTE SSWKTTHFDF HAIHDNVLKL
     DILGHDDPTA LKMLEKLTGV NVKDIPKKDE KIISIFTSPK ALGISSEEIL GEKTGALGIP
     EFGTNFVRQM LSEAKPKTFA DLVSISGLSH GTDVWINNAH YIIQSLGKTL DQVISCRDDI
     MVDLIKKGVP IDLSFTIMEQ VRKGKGLSLE QKRKLIEHGI ENWYIESMEK IKYMFPKAHA
     TAYVLMAWRV AFYKVYYPLE YYATYFSTRT EFFDIEIMSK DKLTLESKIK ELAYRENLRN
     DNQLTTKEKN TLPTLYIANE MKARGFNIQN INLKISLAND WIIDKNSKSL IPPFNVIDGL
     GETLAQKIVD SRNEKEFLSV EDFINRTGIN STLVEKFKSM GIFEQIPETN QIFLI
 
 
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