ID   DPOG1_CHICK             Reviewed;         647 AA.
AC   Q92076;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=DNA polymerase subunit gamma-1;
DE            EC=2.7.7.7;
DE   AltName: Full=Mitochondrial DNA polymerase catalytic subunit;
DE   Flags: Fragment;
GN   Name=POLG; Synonyms=POLG1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8884268; DOI=10.1006/geno.1996.0490;
RA   Ropp P.A., Copeland W.C.;
RT   "Cloning and characterization of the human mitochondrial DNA polymerase,
RT   DNA polymerase gamma.";
RL   Genomics 36:449-458(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 (By similarity). Interacts with TTC3 (By
CC       similarity). {ECO:0000250|UniProtKB:P54098,
CC       ECO:0000250|UniProtKB:Q27607}.
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; U60297; AAC60018.1; -; mRNA.
DR   AlphaFoldDB; Q92076; -.
DR   SMR; Q92076; -.
DR   STRING; 9031.ENSGALP00000037807; -.
DR   PaxDb; Q92076; -.
DR   VEuPathDB; HostDB:geneid_404292; -.
DR   eggNOG; KOG3657; Eukaryota.
DR   InParanoid; Q92076; -.
DR   OrthoDB; 86850at2759; -.
DR   PhylomeDB; Q92076; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005760; C:gamma DNA polymerase complex; IEA:InterPro.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IBA:GO_Central.
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; IDA:AgBase.
DR   GO; GO:0000731; P:DNA synthesis involved in DNA repair; IDA:AgBase.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IDA:AgBase.
DR   GO; GO:0006298; P:mismatch repair; IDA:AgBase.
DR   GO; GO:0006264; P:mitochondrial DNA replication; IBA:GO_Central.
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   PANTHER; PTHR10267; PTHR10267; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   PRINTS; PR00867; DNAPOLG.
DR   SMART; SM00482; POLAc; 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..647
FT                   /note="DNA polymerase subunit gamma-1"
FT                   /id="PRO_0000101273"
FT   REGION          116..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   647 AA;  72855 MW;  8B0AE46621BC293B CRC64;
     EEGWVPGPSL ISLQMRVTPK LMRLAWDGFP LHYSEKHGWG YLVPGRQDNL PAASAEPEGP
     VCPHRAIERL YRQHCLQRGQ EQPPEEAGVE DELMVLEGSS MWQKVEELSQ LELDMERPGR
     AEQSQMQDED GLPELVEESS QPSFHHGNGP YNDVNIPGCW FFKLPHKDGN ENNVGSPFAK
     DFLPRMEDGT LRAAVGRTHG TRALEINKMV SFWRNAHKRV SSQVVVWLKK GELPRAVTRH
     PAYSEEEDYG AILPQVVTAG TITRRAVEPT WLTASNARAD RVGSELKAMV QVPPGYSLVG
     ADVDSQELWI AAVLGEAHFA GMHGCTAFGW MTLQGKKSDG TDLHSKTAAT VGISREHAKV
     FNYGRIYGAG QPFAERLLMQ FNHRLTQQQA REKAQQMYAV TKGIRRFHLS EEGEWLVKEL
     ELAVDKAEDG TVSAQDVQKI QREAMRKSRR KKKWDVVAHR MWAGGTESEM FNKLESIALS
     ASPQTPVLGC HISRALEPAV AKGEFLTSRV NWVVQSSAVD YLHLMLVSMK WLFEEYDING
     RFCISIHDEV RYLVQEQDRY RAALALQITN LLTRCMFAYK LGLQDLPQSV AFFSAVDIDR
     CLRKEVTMNC ATPSNPTGME KKYGIPRGEA LDIYQIIEIT KGSLEKK