ID   DPOG_SCHPO              Reviewed;        1018 AA.
AC   Q12704; Q96WV3; Q9P7I4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   25-MAY-2022, entry version 141.
DE   RecName: Full=DNA polymerase gamma;
DE            EC=2.7.7.7;
DE   AltName: Full=Mitochondrial DNA polymerase catalytic subunit;
GN   Name=mip1; ORFNames=SPCC24B10.22, SPCPB16A4.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SP808;
RX   PubMed=7489897; DOI=10.1016/0378-1119(95)00412-y;
RA   Ropp P.A., Copeland W.C.;
RT   "Characterization of a new DNA polymerase from Schizosaccharomyces pombe: a
RT   probable homologue of the Saccharomyces cerevisiae DNA polymerase gamma.";
RL   Gene 165:103-107(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Involved in the replication of mitochondrial DNA.
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   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases: alpha,
CC       beta, gamma, delta, and epsilon which are responsible for different
CC       reactions of DNA synthesis.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; Z47976; CAA88012.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAB76231.1; -; Genomic_DNA.
DR   PIR; JC4375; JC4375.
DR   PIR; T50429; T50429.
DR   RefSeq; NP_588025.2; NM_001023016.2.
DR   AlphaFoldDB; Q12704; -.
DR   SMR; Q12704; -.
DR   BioGRID; 275671; 2.
DR   STRING; 4896.SPCC24B10.22.1; -.
DR   iPTMnet; Q12704; -.
DR   MaxQB; Q12704; -.
DR   PaxDb; Q12704; -.
DR   EnsemblFungi; SPCC24B10.22.1; SPCC24B10.22.1:pep; SPCC24B10.22.
DR   GeneID; 2539099; -.
DR   KEGG; spo:SPCC24B10.22; -.
DR   PomBase; SPCC24B10.22; -.
DR   VEuPathDB; FungiDB:SPCC24B10.22; -.
DR   eggNOG; KOG3657; Eukaryota.
DR   HOGENOM; CLU_001524_2_1_1; -.
DR   OMA; LWLWDED; -.
DR   PhylomeDB; Q12704; -.
DR   PRO; PR:Q12704; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005760; C:gamma DNA polymerase complex; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; ISO:PomBase.
DR   GO; GO:0003677; F:DNA binding; ISS:PomBase.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; ISO:PomBase.
DR   GO; GO:0006264; P:mitochondrial DNA replication; IMP:PomBase.
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   PRINTS; PR00867; DNAPOLG.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Magnesium;
KW   Mitochondrion; Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..1018
FT                   /note="DNA polymerase gamma"
FT                   /id="PRO_0000101277"
FT   CONFLICT        563
FT                   /note="G -> C (in Ref. 1; CAA88012)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        571..572
FT                   /note="QR -> HA (in Ref. 1; CAA88012)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        832
FT                   /note="T -> Q (in Ref. 1; CAA88012)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1018 AA;  116045 MW;  9B114BC6FBEE63CA CRC64;
     MFYKACPSTL TCSKWIHSII KTKKFLYCRH YSSKSFIDNA PLRINPVGVQ YLSPALQNQV
     FPQQNTQISQ LHLDLAKFHL AKHQLLNKET IKLPSFNFRL PPLQGKTISE HFYNIGLEFA
     EPHLSKAIKF SKIDTPVQPK TWKRQPGWTK YAKDGSISCV PYPDSDCMVF DVEVLYKVSP
     FAVVATAVSE DAWYCWLSPW LLGKSENDRQ LIPSNPKGAL FVGHNVSFDR QRIREEYNIK
     SSRNVFLDTM SLHVATHGMC SRQKPTWFKA RKAYIRSQST ETSEDDDSSS FDDDYQNYLK
     QEPWLAHSSV NSLKDVAKFH CNITLDKSKR DDFASLEKEP ILQKLNELIT YCAHDTYSTH
     QVFKKVFPQF LEVCPHPATF SAMLSLGSVF LPVNHSWTRY INGVEEQYQQ MIQLVDQKLS
     QYAEKAKDLI NTKDTVLKDP WLRQLDWTPC NLYRKLKKAT QEVPVVPKWY KKAYCKTEKR
     AVITAKSRLA PILLRLKWKK HPLAWSDTYG WVFSVERTSK DEIEMLLDQG LVPCSREEDT
     KLDYNNYIFF KVPHKDGPEA RCGSPLSKSY QRYFEEGILQ SDYEVAKKAL EMSASCSYWS
     SARDRIRSQM VVWDKDAELG VPSSVDGFGI ILPCIIPMGT VTRRAVENTW LTASNSKKNR
     LGSELKAMIR APDGYTFVGA DVDSEELWIV ALMGDSQFRL HGATALGMMT LEGKKSEGTD
     LHSKTAAILG VSRDSAKVFN YGRLYGAGLK HTTLLLMQMN PTLKTAEAKE LAKKLYASTK
     GVKSKMSKRL QEMGLPKLTF WSQGTESFVF NKLEAMAQLP SPRTPVLDAG ITQALSSKNL
     SKNSFMTSRV NWAIQSSAVD YLHLLLVSMN HLIKKYYLEA RLSLTVHDEV RYLSSDKDKY
     RVAFALQVAN LWTRAFFCQR LGINELPQSV AFFSSVDIDH VLRKDVKMDC VTPSNKVPIP
     PGEELTIESV LEKLEQSGQS LEPLEQIQCF VDVKATTSAE ITEEDKKNIA YLKAQAFY