ID A0A2K6AY60_MACNE Unreviewed; 1228 AA.
AC A0A2K6AY60;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA polymerase subunit gamma-1 {ECO:0000256|ARBA:ARBA00015350, ECO:0000256|PIRNR:PIRNR000797};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|PIRNR:PIRNR000797};
GN Name=POLG {ECO:0000313|Ensembl:ENSMNEP00000004086.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000004086.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000004086.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Involved in the replication of mitochondrial DNA. Associates
CC with mitochondrial DNA. {ECO:0000256|ARBA:ARBA00025629}.
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 Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|PIRNR:PIRNR000797};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Heterotrimer composed of a catalytic subunit and a homodimer
CC of accessory subunits. {ECO:0000256|PIRNR:PIRNR000797}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|PIRNR:PIRNR000797}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|PIRNR:PIRNR000797}.
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DR RefSeq; XP_011750584.1; XM_011752282.1.
DR AlphaFoldDB; A0A2K6AY60; -.
DR STRING; 9545.ENSMNEP00000004086; -.
DR Ensembl; ENSMNET00000020823.1; ENSMNEP00000004086.1; ENSMNEG00000019045.1.
DR GeneID; 105488334; -.
DR KEGG; mni:105488334; -.
DR CTD; 5428; -.
DR GeneTree; ENSGT00390000000453; -.
DR OMA; LWLWDED; -.
DR OrthoDB; 5403095at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000019045; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0005760; C:gamma DNA polymerase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
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:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IEA:Ensembl.
DR GO; GO:0006287; P:base-excision repair, gap-filling; IEA:Ensembl.
DR GO; GO:0045004; P:DNA replication proofreading; IEA:Ensembl.
DR GO; GO:0006264; P:mitochondrial DNA replication; IEA:Ensembl.
DR CDD; cd08641; DNA_pol_gammaA; 1.
DR Gene3D; 1.20.5.3960; -; 1.
DR Gene3D; 3.30.420.390; -; 2.
DR Gene3D; 3.30.70.370; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
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; IPR047580; POLG_palm_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR PANTHER; PTHR10267; DNA POLYMERASE SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10267:SF0; DNA POLYMERASE SUBUNIT GAMMA-1; 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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR000797};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR000797};
KW DNA-directed DNA polymerase {ECO:0000256|PIRNR:PIRNR000797};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|PIRNR:PIRNR000797};
KW Mitochondrion nucleoid {ECO:0000256|ARBA:ARBA00023271};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|PIRNR:PIRNR000797};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000797}.
FT DOMAIN 860..1134
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 17..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 427..454
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 29..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1228 AA; 138109 MW; 5FEA1C3B02E177D4 CRC64;
MSRLLWRKLA GATVVPGPVP APGRWVSSSV PASDPSDGRR RQQQQLQQPQ VPSSEGGQLR
HNPLHIQMLS KGLHEQIFGQ GGEIPGEAAV RRSVEHLQKH GLWGQPAAPL PDVELRLPPL
YGDNLDQHFR LLAQKQSLPY LEAANSLLQA QLPPQPTGWA WAEGWTRYGP EGEAVPVAIP
EERALVFDVE VCLAEGICPT LAVAISPSAW YSWCSRRLVE ERYSWTSQLS PADLIPLEVP
AGASPTQRDW QEQLVVGHNV SFDRAHIREQ YLIQGSRMRF LDTMSMHMAI SGLSSFQRSL
WIAAKQGKHK VQGSTKQGQK SQRKARRGPA ISSWDWLDIS SVNSLAEVHR LYVGGPPLEK
EPRELFVKGT MKDIRENFQD LMQYCAQDVW ATHEVFQQQL PLFLERCPHP VTLAGMLEMG
VSYLPVNQNW ERYLAEAQGT YEELQREMKK SLMDLANDAC QLLSGERYKE DPWLWDLEWD
LQEFKQKKAK KVKKEPATAS KLPIEGAGAP GDPMDQEDLG PRSEEEEFQQ DVMARACLQK
LKGTTELLPK RPQHLPGHPG WYRKLCPRLD DPAWTPGPSL LSLQMRVTPK LMALTWDGFP
LHYSERHGWG YLVPGRRDNL AKLPTGTTLE SAGVVCPYRA IESLYRKHCL EQGKQQLTPQ
EAGLAEEFLL TDNSAIWQTV EELDYLEVEA EAKMENLRAA VPGQPLALTA PGGPKDSQPN
YHHGNGPYND VDIPGCWFFK LPHKDGNSCN VGSPFAKDFL PKMEDGTLQA GPGGASGPRA
LEINKMISFW RNAHKRISSQ MVVWLPRSAL PRAVIRHPDY DEEGLYGAIL PQVVTAGTIT
RRAVEPTWLT ASNARPDRVG SELKAMVQAP PGYTLVGADV DSQELWIAAV LGDAHFAGMH
GCTAFGWMTL QGRKSRGTDL HSKTATTVGI SREHAKVFNY GRIYGAGQPF AERLLMQFNH
RLTQQEAAEK AQQMYAVTKG LRWYRLSDEG EWLVRELHLP VDRTEGGWIS LQDLRKVQRE
AARKSHWKKW EVIAERAWKG GTESEMFNKL ESIATSDIPR TPVLGCRISR ALEPSAVQGE
FMTSRVNWVV QSSAVDYLHL MLVAMKWLFE EFAIDGRFCI SIHDEVRYLV REEDRYRAAL
ALQITNLLTR CMFAYKLGLN DLPQSVAFFS AVDIDRCLRK EVTMDCKTPS NPTGMERRYG
IPQGEALDIY QIIELTKGSL EKRSQPGP
//
