ID   DPOG1_XENLA             Reviewed;        1200 AA.
AC   Q91684;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=DNA polymerase subunit gamma-1;
DE            EC=2.7.7.7;
DE   AltName: Full=Mitochondrial DNA polymerase catalytic subunit;
GN   Name=polg;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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. Associates
CC       with mitochondrial DNA (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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBUNIT: Heterotrimer composed of a catalytic subunit and a homodimer
CC       of accessory subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion matrix,
CC       mitochondrion nucleoid {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; U49509; AAB17117.1; -; mRNA.
DR   PIR; S68258; S68258.
DR   RefSeq; NP_001081464.1; NM_001087995.1.
DR   AlphaFoldDB; Q91684; -.
DR   SMR; Q91684; -.
DR   ComplexPortal; CPX-2095; Mitochondrial DNA polymerase gamma complex.
DR   GeneID; 397851; -.
DR   KEGG; xla:397851; -.
DR   CTD; 397851; -.
DR   Xenbase; XB-GENE-865213; polg.L.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 397851; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005760; C:gamma DNA polymerase complex; IPI:ComplexPortal.
DR   GO; GO:0005759; C:mitochondrial matrix; IC:ComplexPortal.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
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:0006264; P:mitochondrial DNA replication; IC:ComplexPortal.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
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   PIRSF; PIRSF000797; DNA_pol_mt; 1.
DR   PRINTS; PR00867; DNAPOLG.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   2: Evidence at transcript level;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Magnesium;
KW   Mitochondrion; Mitochondrion nucleoid; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1200
FT                   /note="DNA polymerase subunit gamma-1"
FT                   /id="PRO_0000101274"
FT   REGION          471..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1200 AA;  137244 MW;  176F7028CAD1C3C5 CRC64;
     MNRLLQKGTS LVPSWRTRGC RYRRCSYAPQ LHAKPLEMET SQRRMNPLNI QMLSKGFHEQ
     IFRGKQVQHA EEDVQRSITH LKNHELWGQE TSTVPDVELQ LPKMYGNNIE EHFQILAQKQ
     SLPYLEAAND LLNCQLPAMP QTWAWQSGWT RYTATGEKEL VDFPDEKAMV FDVEVCVTEG
     CCPTLAVAAS PQNWYSWCSR RLIEGRYTWS KELLLSDLFP LETSMNCNYM TKNNWTERLV
     VGHNVSFDRA HIKEQYLIKG SKTRFMDTMS MHMAISGLTG FQRTLWMASK YGKKKGLQEV
     KQHIKKTRSN FSGSPISSWD WVNISSINNL ADVHALYVGG PPLEKEAREL FVKGSMSDIR
     TEFQELMRYC ALDVQATHEV FQEQFPLFME RCPHPVTLSG MLEMGVSYLP VNQNWERYLD
     EAQTSYEELQ KEMKKSLMKL ANDACQLLTK DAYKEDPWLW DLEWDIQESK QKKTKISKKQ
     KKANEAAESV GNKLVEDHNE DPGPPTEKEE SRPSMGKLYL EDLKLKTLPL LPKRNQHLPG
     HPGWYRKLCP KLEDPDWLPG PGLISLQMRL TPKLMRLTWD GYPLHYSEKH GWGYLVPGRK
     NNKLNNEEEE EIIPCPYRAI EDIYAEYSKN KTKDGCLSQH STIPEEFMLT DDNSMWQKVE
     ELSRTEMDLS SEVPATAKAK KRNNSSEHPV KLEMEFDSLP DNHHGNSPCG DVNVSGCWFY
     KLPHKDGNAN NVGSPFAKDF LPKMEDGTLQ ASTGDSSATR ALEINKMISF WRNAHKRISS
     QMVVWMKKNE LHRTITRDPE FDEENKYGAI LAQVVSAGTI TRRAVEPTWL TASNARADRV
     GSELKAMVQV PPGYHLIGAD VDSQELWIAA ILGEAHFAGI HGCTAFGWMT LQGKKSSGTD
     LHSKTASTVG ISREHAKVFN YGRIYGAGQP FAERLLMQFN HRLTQEQAAE KAKQMYAVTK
     GIRRYILSKE GEWLVEELGI SVERGEENSV NLQDLRKIQK DATKRSRRKW NLVSRRIWTG
     GTESQMFNKL ETIAMSPSPK TPVLGCRISR ALEPTAVKGE FITSRVNWVV QSSAVDYLHL
     MLVAMKWLFE AYDIDGRFCI SIHDEVRYLV HSKDRYRAAL ALQITNLLTR CMFASRLGIQ
     DVPQSVAFFS AVDIDKCLRK EVTMDCSTPS NPNGMEKRYG IPQGEALDIY QILKVTKGVL