ID   DPO3A_MYCGE             Reviewed;         874 AA.
AC   Q49405;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=MG261;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
CC   -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC       responsible for most of the replicative synthesis in bacteria. This DNA
CC       polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC       is the DNA polymerase (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the PolIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III complex
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L43967; AAC71482.1; -; Genomic_DNA.
DR   PIR; H64228; H64228.
DR   RefSeq; WP_009885893.1; NZ_AAGX01000009.1.
DR   AlphaFoldDB; Q49405; -.
DR   SMR; Q49405; -.
DR   STRING; 243273.MG_261; -.
DR   EnsemblBacteria; AAC71482; AAC71482; MG_261.
DR   KEGG; mge:MG_261; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_1_14; -.
DR   OMA; HTNSYYN; -.
DR   OrthoDB; 561611at2; -.
DR   BioCyc; MGEN243273:G1GJ2-316-MON; -.
DR   Proteomes; UP000000807; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; PTHR32294; 1.
DR   Pfam; PF07733; DNA_pol3_alpha; 1.
DR   Pfam; PF17657; DNA_pol3_finger; 1.
DR   Pfam; PF02811; PHP; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..874
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103326"
SQ   SEQUENCE   874 AA;  100435 MW;  9B27C96A28A74909 CRC64;
     MFVNLHTNSY YNFLNSALSP KKLVNLAIND QQKAVAITDP NLFGAVEFFI TCKQNNIKPI
     IGLNLTVEYQ KNDVKLLLIA KSNKGFQTLN KIALIQQKLE INSLVDQLTD IAVIICSLTT
     WKSTYKDVYQ AKGIEINQTP IAILANAVNC EKTNSDQVVL TVLKQMKQNQ TGKITTFDWD
     LKQKLNQISI NENLKVKSEI QPFLDQKTAQ QLFSETELNN LNDLVNRCEL DLEHLKAASL
     SLTDNDAAVL ESLCQTNLKQ FLDKNQDLNK KAYQLRLEKE LNVINKLNFA SYFLVVNDLV
     NYAFKKDILI GSGRGSAVGS LVAFLLNITK IDPVQHQLIF ERFISTHRQD LPDIDIDIME
     NKRAEMINYL FEKYGKENCA QIVTFQRFKT RSAVKEVAKL FNDYGISDMI LGVLPKDQTI
     TFTDLKATED SALQLCLQQF GLIVELALAI VDFPRQSSIH ASGIVIASNS LIKTIPLLQL
     DNNHFLTQVS MEWLSFFNLN KFDLLGLINL TMISDVITQI KPSNQTVNQF LNTISWTDQN
     TFINLVNEDT LGIFQLESFG MKKLLVQIKP KTINQLAIVL ALYRPGAQDN INLFINRLHN
     GYDQSDIDPR ILPIVKNTYG VLIFQEQIIN IVKVVANYSL EEADSFRRAI SKKDVKLIQK
     NKRNFFERAV QNNFDLKTTT KIFSYIERFA NYGFNLSHAL GYALLSYWTA WLKTNYPVYF
     YLWLLNHFQS SKDKQKLIIR TLEKSGIEIY PPLLNKAQPN SVIENKKIYL GLNLIKGIND
     RYIQNLQKVQ HLIQTQNNLQ LTDVVSWCLD KTIGDIPLKD LLLLKTMGCF DFFEYTYDFN
     DAKDFWIKSD HLLFTRMPLE KKDSNFWIKQ FFTN