ID A0A1S3ESF9_DIPOR Unreviewed; 1331 AA.
AC A0A1S3ESF9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA polymerase subunit gamma-1 {ECO:0000256|ARBA:ARBA00015350};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE AltName: Full=Mitochondrial DNA polymerase catalytic subunit {ECO:0000256|ARBA:ARBA00031966};
GN Name=Polg {ECO:0000313|RefSeq:XP_012867331.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012867331.1};
RN [1] {ECO:0000313|RefSeq:XP_012867331.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012867331.1};
RG RefSeq;
RL Submitted (NOV-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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705}.
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DR RefSeq; XP_012867331.1; XM_013011877.1.
DR STRING; 10020.ENSDORP00000013295; -.
DR GeneID; 105982304; -.
DR KEGG; dord:105982304; -.
DR CTD; 5428; -.
DR InParanoid; A0A1S3ESF9; -.
DR OrthoDB; 5403095at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005760; C:gamma DNA polymerase complex; IEA:InterPro.
DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006264; P:mitochondrial DNA replication; IEA:InterPro.
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; IPR018247; EF_Hand_1_Ca_BS.
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 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.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion nucleoid {ECO:0000256|ARBA:ARBA00023271};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 963..1237
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 136..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 539..566
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 150..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1331 AA; 147129 MW; 57E268311DCB95CA CRC64;
MPRAPVNRVF CLSGQAHLYK DLKIGLNKMT VARGRRWQGS GDTGGRARRT PGWLAPWDLA
HRLTVPSSES AHGALTSATV SLVLLVGEGT IGPHHGLGLH LPRAHTADCL QVCLSVCPSV
CQSQVSAGVR AGHSFSAARS RASIPSGGAP GSKGRSSSPH CITKPGSRQP PLRPWLRSLT
SPGDCGGPGG RRAQRRLGPA EVKGTGQEER CHTGLELWNG GVRTPTHPES LSKSEGETIL
PSSLRARGTG TRTSSIRANW YKSPPRPRSW AWAPGWTRYG PGGEAEPVAI PEERALVFDV
EVCLAEGTCP TLAVAISPSA WYSWCSRRLV EERYSWTSRL SPADLIPLEA PGEGSSAPTD
GQGQLVVGHN VCFDRAHIRE QYLIQGSRLR FLDTMSLHTA ISGLSGFQRS LWIAAKQGRH
KAQQLAQRGR KTRGKANGHG PVISSWDWMD LSSANNLADV HSLYVGGPPL EKEPRELFVK
GSMQDVRQNF QELMEYCARD VWATHEVFQQ QLPLFLERCP HPVTLAGMLE MSVSYLPVNQ
NWERYLEEAQ STYEELQREM KKSLMGLADD ACGLLSGERY KDDPWLWDLE WDLQEFRQKK
TKKVKKEPAL ASRPPAEAAR APGAPLDQED PGPPSEEEEV QRDGAIRSCL QQLKATAQLL
PKRSQHLPGH PGWYRKLCPR LDDPAWAPGP SLLSLQMRIT PKLMALTWDG FPLHYSEQHG
WGYLVPGRQD NLASVPAGTG LESGVECPSR AIESLYRKHC AAQGKPRPTG LAPDPLPPDS
SAEWHTMEEL VCLDVEAEAR LENLDACEPG QPPALPAASS QPSFHHGNGP YNDVNVPGCW
FFKLPHKDGN SYNVGSPFAK DFLPKMEDGT LQAGPGRASG PRALEINKMI SFWRNAHKRI
SSQMVVWLPR SALPRAVTRH PGYDEEGRYG AILPQLVTVG TITRRAVEPT WLTASNARAD
RVGSELKAMI QAPPGYVLVG ADVDSQELWI AAVLGDAHFA GMHGCTAFGW MTLQGRKSMG
TDLHSKTATT VGISREHAKV FNYGRIYGAG QPFAERLLMQ FNHRLTRQEA AEKAQQMYAV
TKGLRRYRLT EEGEWLVRQL GLSVDRSEDG WISLQDLRKI QREASRKSRR KKWDVVAERA
WIGGTESEMF NKLESIATSD TPQTPVLGCR ISRALEPAAV GGEFMTSRVN WVVQSSAVDY
LHLMLVAMKW LFEEFAIDGR FCISIHDEVR YLVREEDRYR AALALQITNL LTRCMFSYKL
GLKDLPQSVA FFSAVDIDQC LRKEVTMDCK TPSNPMGMER GYGVPQGEAL DIYQIIELTK
GSLEKQSQPG P
//
