ID   DPOG2_XENLA             Reviewed;         463 AA.
AC   Q9W6G7;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=DNA polymerase subunit gamma-2, mitochondrial;
DE   AltName: Full=Mitochondrial DNA polymerase accessory subunit;
DE   AltName: Full=MtPolB;
DE   AltName: Full=PolG-beta;
DE   Flags: Precursor;
GN   Name=polg2; Synonyms=mtpolb;
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], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=10330144; DOI=10.1128/mcb.19.6.4039;
RA   Carrodeguas J.A., Kobayashi R., Lim S.E., Copeland W.C., Bogenhagen D.F.;
RT   "The accessory subunit of Xenopus laevis mitochondrial DNA polymerase gamma
RT   increases processivity of the catalytic subunit of human DNA polymerase
RT   gamma and is related to class II aminoacyl-tRNA synthetases.";
RL   Mol. Cell. Biol. 19:4039-4046(1999).
CC   -!- FUNCTION: Mitochondrial polymerase processivity subunit. It regulates
CC       the polymerase and exonuclease activities promoting processive DNA
CC       synthesis. Binds to ss-DNA. {ECO:0000250|UniProtKB:Q9UHN1}.
CC   -!- SUBUNIT: Heterotrimer composed of a catalytic subunit and a homodimer
CC       of accessory subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
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DR   EMBL; AF124606; AAD32572.1; -; mRNA.
DR   RefSeq; NP_001081904.1; NM_001088435.1.
DR   RefSeq; XP_018089639.1; XM_018234150.1.
DR   AlphaFoldDB; Q9W6G7; -.
DR   SMR; Q9W6G7; -.
DR   ComplexPortal; CPX-2095; Mitochondrial DNA polymerase gamma complex.
DR   GeneID; 398112; -.
DR   KEGG; xla:398112; -.
DR   CTD; 398112; -.
DR   Xenbase; XB-GENE-6251937; polg2.L.
DR   OMA; AFREHIF; -.
DR   OrthoDB; 1183820at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   GO; GO:0005760; C:gamma DNA polymerase complex; IPI:ComplexPortal.
DR   GO; GO:0005759; C:mitochondrial matrix; IC:ComplexPortal.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006264; P:mitochondrial DNA replication; IC:ComplexPortal.
DR   CDD; cd00774; GlyRS-like_core; 1.
DR   CDD; cd02426; Pol_gamma_b_Cterm; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR027031; Gly-tRNA_synthase/POLG2.
DR   InterPro; IPR033731; GlyRS-like_core.
DR   InterPro; IPR027030; POLG2.
DR   InterPro; IPR042064; POLG2_C.
DR   PANTHER; PTHR10745; PTHR10745; 1.
DR   PANTHER; PTHR10745:SF8; PTHR10745:SF8; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA replication; DNA-binding; Mitochondrion;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..44
FT                   /note="Mitochondrion"
FT   CHAIN           45..463
FT                   /note="DNA polymerase subunit gamma-2, mitochondrial"
FT                   /id="PRO_0000007316"
SQ   SEQUENCE   463 AA;  52283 MW;  91399264C9087BA8 CRC64;
     MLLTLKNTGQ LLVAACSKVA RSLAKYHPRV NHHRHCVWCS KRGLTTGGTA QKQDILFHLC
     QQRHFLSGET LTCTSLVQGC HNLGPLGVEL KRNLVAQWWN SVVVYREQVL GIDTLHHLST
     PSSAPEKPLL AICTQHLKEL PRDQLVKWLE DPAGKLEFLR HELLYGALLE YVPSMELLNK
     KMPFGLAEIG KCFHSIPEER NKGTILPRIG ERTVASLVWF SSPKSSGQWQ DYWLRQRLQW
     WQKFAQSPSG FSCNDIQDGQ GRKSSLIQYE FPWGRETIET LCNMDDSALF QMHPGCTTKL
     QARDGRKSVV PHVVWVSGDL DRGILAYLSD ALQQTEAPAV RGQYHQREVL KLHPTLAPIK
     VAVDMGKGPT GELRLVCQGL SSELREQGVY VWPGYQETLH GSLEQLYTKY DKMGVLFTVL
     VSESTLENGL LQVRSRDTTL KETIHVSKVK DFLVRYIAAA GNL