ID   POLIB_ARATH             Reviewed;        1034 AA.
AC   Q84ND9; Q9LJU4;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 130.
DE   RecName: Full=DNA polymerase I B, chloroplastic/mitochondrial;
DE            EC=2.7.7.7;
DE   AltName: Full=DNA polymerase PolI-like B;
DE            Short=AtPolI-like B;
DE   AltName: Full=Polymerase gamma 1;
DE            Short=POLGAMMA1;
DE   Flags: Precursor;
GN   Name=POLIB; OrderedLocusNames=At3g20540; ORFNames=K10D20.8;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15993837; DOI=10.1016/j.bbrc.2005.06.052;
RA   Mori Y., Kimura S., Saotome A., Kasai N., Sakaguchi N., Uchiyama Y.,
RA   Ishibashi T., Yamamoto T., Chiku H., Sakaguchi K.;
RT   "Plastid DNA polymerases from higher plants, Arabidopsis thaliana.";
RL   Biochem. Biophys. Res. Commun. 334:43-50(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RA   Elo A., Lyznik A.M., Gonzalez D.O., Kachman S.D., Mackenzie S.A.;
RT   "Nuclear genes encoding mitochondrial proteins for DNA and RNA metabolism
RT   are clustered in the Arabidopsis genome.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12837951; DOI=10.1105/tpc.010009;
RA   Elo A., Lyznik A., Gonzalez D.O., Kachman S.D., Mackenzie S.A.;
RT   "Nuclear genes that encode mitochondrial proteins for DNA and RNA
RT   metabolism are clustered in the Arabidopsis genome.";
RL   Plant Cell 15:1619-1631(2003).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16169894; DOI=10.1105/tpc.105.035287;
RA   Christensen A.C., Lyznik A., Mohammed S., Elowsky C.G., Elo A., Yule R.,
RA   Mackenzie S.A.;
RT   "Dual-domain, dual-targeting organellar protein presequences in Arabidopsis
RT   can use non-AUG start codons.";
RL   Plant Cell 17:2805-2816(2005).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21427281; DOI=10.1104/pp.111.173849;
RA   Parent J.S., Lepage E., Brisson N.;
RT   "Divergent roles for the two PolI-like organelle DNA polymerases of
RT   Arabidopsis.";
RL   Plant Physiol. 156:254-262(2011).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 5'-3' exonuclease activity (By similarity). Required for DNA
CC       replication and accumulation in plastids and mitochondria.
CC       {ECO:0000250, ECO:0000269|PubMed:21427281}.
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   -!- ACTIVITY REGULATION: Not inhibited by aphidicolin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Plastid, chloroplast.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According EST sequences.;
CC       Name=1;
CC         IsoId=Q84ND9-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in shoot apical meristem.
CC       {ECO:0000269|PubMed:15993837}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants have reduced levels of DNA in both
CC       mitochondria and plastids. Double homozygous mutants polIa and polIb
CC       are sterile. {ECO:0000269|PubMed:21427281}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB01162.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB211533; BAE10874.1; -; mRNA.
DR   EMBL; AY195962; AAO34128.1; -; mRNA.
DR   EMBL; AP000410; BAB01162.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE76392.1; -; Genomic_DNA.
DR   EMBL; AK226811; BAE98907.1; -; mRNA.
DR   RefSeq; NP_188690.3; NM_112946.5. [Q84ND9-1]
DR   AlphaFoldDB; Q84ND9; -.
DR   SMR; Q84ND9; -.
DR   STRING; 3702.AT3G20540.2; -.
DR   iPTMnet; Q84ND9; -.
DR   PaxDb; Q84ND9; -.
DR   PRIDE; Q84ND9; -.
DR   ProteomicsDB; 226311; -. [Q84ND9-1]
DR   EnsemblPlants; AT3G20540.1; AT3G20540.1; AT3G20540. [Q84ND9-1]
DR   GeneID; 821600; -.
DR   Gramene; AT3G20540.1; AT3G20540.1; AT3G20540. [Q84ND9-1]
DR   KEGG; ath:AT3G20540; -.
DR   Araport; AT3G20540; -.
DR   eggNOG; KOG0950; Eukaryota.
DR   HOGENOM; CLU_004638_0_0_1; -.
DR   OMA; VNDDIKP; -.
DR   PhylomeDB; Q84ND9; -.
DR   BRENDA; 4.2.99.B1; 399.
DR   PRO; PR:Q84ND9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q84ND9; baseline and differential.
DR   Genevisible; Q84ND9; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   GO; GO:0006264; P:mitochondrial DNA replication; IMP:UniProtKB.
DR   GO; GO:0033259; P:plastid DNA replication; IMP:UniProtKB.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10133; PTHR10133; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chloroplast; DNA damage; DNA repair; DNA replication;
KW   DNA-binding; DNA-directed DNA polymerase; Exonuclease; Hydrolase;
KW   Mitochondrion; Nuclease; Nucleotidyltransferase; Plastid;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..55
FT                   /note="Chloroplast and mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           56..1033
FT                   /note="DNA polymerase I B, chloroplastic/mitochondrial"
FT                   /id="PRO_0000429310"
FT   DOMAIN          270..468
FT                   /note="3'-5' exonuclease"
FT   REGION          700..1030
FT                   /note="Polymerase"
SQ   SEQUENCE   1034 AA;  115563 MW;  9BD3F52F98B0EAFE CRC64;
     MGVSLRHLSP SSFWVSRRPR VSSSILSFLV PRRRILCTRK VAIIKGNAGY STATDCGGSH
     GFHHSGHQRS SSVEFSGEWK LNLGSKTARM VPPTVKQAGA VSAWREEVNN KLRGRNREYA
     NNQDDAFGNG SYILKGFVPK IDDVHSYGNG QNFDYNLKPG TDITTLGREL NGFMQTNSIR
     GSVVALPSKD IEVGETTDVT LKPLNSDTTL DNASYKKTAT ISKVEKCTNL SQVRANLKKI
     YNRVRVVDNV SSAKETVALL MNQYRNLVHA CDTEVSRIDV KTETPVDHGE MICFSIYCGS
     EADFGDGKSC IWVDVLGENG RDILAEFKPF FEDSSIKKVW HNYSFDNHII RNYGIKLSGF
     HGDTMHMARL WDSSRRISGG YSLEALTSDP KVLGGTETKE EAELFGKISM KKIFGKGKLK
     KDGSEGKLVI IPPVKELQME DREAWISYSA LDSISTLKLY ESMKKQLQAK KWFLDGKLIS
     KKNMFDFYQE YWQPFGELLA KMESEGMLVD RDYLAQIEIV AKAEQEIAVS RFRNWASKHC
     PDAKHMNVGS DTQLRQLFFG GISNSCNDED LPYEKLFKVP NVDKVIEEGK KRATKFRNIK
     LHRISDRPLP TEKFTASGWP SVSGDTLKAL AGKVSAEYDY MEGVLDTCLE ENIGDDDCIS
     LPDEVVETQH VNTSVESDTS AYGTAFDAFG GGESGKEACH AIAALCEVCS IDSLISNFIL
     PLQGSNVSGK DGRVHCSLNI NTETGRLSAR RPNLQNQPAL EKDRYKIRQA FIASPGNSLI
     VADYGQLELR ILAHLASCES MKEAFIAGGD FHSRTAMNMY PHIREAVENG EVLLEWHPQP
     GQEKPPVPLL KDAFASERRK AKMLNFSIAY GKTAIGLSRD WKVSREEAQD TVNLWYNDRQ
     EVRKWQELRK KEAIQKGYVL TLLGRARKFP EYRSRAQKNH IERAAINTPV QGSAADVAMC
     AMLEISNNQR LKELGWKLLL QVHDEVILEG PSESAENAKD IVVNCMSEPF NGKNILSVDL
     SVDAKCAQNW YAGK