ID   DPOG_PICPA              Reviewed;        1012 AA.
AC   Q01941;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=DNA polymerase gamma;
DE            EC=2.7.7.7;
DE   AltName: Full=Mitochondrial DNA polymerase catalytic subunit;
GN   Name=MIP1;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SB 1099;
RX   PubMed=8628681; DOI=10.1093/nar/24.8.1481;
RA   Ye F., Carrodeguas J.A., Bogenhagen D.F.;
RT   "The gamma subfamily of DNA polymerases: cloning of a developmentally
RT   regulated cDNA encoding Xenopus laevis mitochondrial DNA polymerase
RT   gamma.";
RL   Nucleic Acids Res. 24:1481-1488(1996).
CC   -!- FUNCTION: Involved in the replication of mitochondrial DNA.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha,
CC       beta, gamma, delta, and epsilon which are responsible for different
CC       reactions of DNA synthesis.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; U49510; AAB17118.1; -; Genomic_DNA.
DR   PIR; S68259; S68259.
DR   AlphaFoldDB; Q01941; -.
DR   SMR; Q01941; -.
DR   GO; GO:0005760; C:gamma DNA polymerase complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; IPR002297; DNA-dir_DNA_pol_A_mt.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR041336; DNApol_Exo.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   PANTHER; PTHR10267; PTHR10267; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF18136; DNApol_Exo; 1.
DR   PRINTS; PR00867; DNAPOLG.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Magnesium;
KW   Mitochondrion; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..1012
FT                   /note="DNA polymerase gamma"
FT                   /id="PRO_0000101276"
SQ   SEQUENCE   1012 AA;  115719 MW;  AA83C9742AF87963 CRC64;
     MIIRRFVRHL STSKSSIRIN AVGIQHLAPS LQNQLFGKSS PRLDEDLINM AKRHLKSNNL
     IGKKSSLNDP IEIQLPSLQG NTLDEHFYKL GSASLEPYNP LIDELLNLNI IEPQFEFAFQ
     SGWTRYAPGE PSEKVPYPLE DSYFFDVETM YKVSQYPVMA VALSDKAWYG WVSPYLTEES
     TTNDHLIPLN TFETEKFIVG HNVSYDRARA LEEYNLKQTK AFWMDTMALH VSVSGMCTRQ
     RGTWIKHNKK EQENTMSVAS IKSKVQNEEL QELLDSTSIE DPMLEDNPWI NKSSLNSLER
     VAEFYCKIKL KKDIRNSFAT EDPDELRGNF DELMQYCAKD VFATGKVFQK VYPKFKKLIP
     HPVTLAALKD ISSCILPTTT KWEDYIETSE RLYQESRRMI EKNLHVICEE TVKLKDDPTK
     PWENDPWLSQ LDWTIDPIRL TKKGEIHKNQ KLPGYPNWYK QLIVKNELKL TTKTRTSPLL
     LKLAWNGNPL YWIQTQGWCF KVPKNKTEEY EKLNFVMVSL KKLSEDPGFE SIRAEDLKNF
     TFVKVPHPDG PSARVTNCMT KSCLGFFEKG FLNSQYPLAK DALQMAVASS YWTSSRERIM
     NQFVVFEDDM GYILPQIIPM GTITRRAVEN TWLTASNAKK NRLGSELKSL IEAPKGYCFV
     GADVDSEELW IASLIGDSVF KIHGGTAIGW MTLEGTKNEG TDLHSKTAKI LGISRNEAKI
     FNYGRIYGAG IKFTTTLLKK FNPALSDAEA KATANALYTA TKGISGRYDK KSIWYGGSES
     IIFNRLEAIA EMAHPKTPVL GAGITAPLQK ANLSTNNFLT SRINWAIQSS GVDYLHLLII
     SMDYLIKLFD IDARLCITVH DEIRYLVKEE DKFRAAYALQ ISNLWTRAMF CQQLGINEVP
     QSCAFFSAVD LDFVLRKEVD LDCVTPSNPD PIPCGKSLDI YQLLQQEDIK GADFPRTMHL
     NDVHYRKRTP VIEMFDKAVD DKTRKFMVSL QIAQDKTEFT KWKRSRGELI VH