POLIA_ARATH
ID POLIA_ARATH Reviewed; 1050 AA.
AC F4I6M1; Q8W105; Q9C6J5;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=DNA polymerase I A, chloroplastic/mitochondrial;
DE EC=2.7.7.7;
DE AltName: Full=DNA polymerase PolI-like B;
DE Short=AtPolI-like A;
DE AltName: Full=Polymerase gamma 2;
DE Short=POLGAMMA2;
DE Flags: Precursor;
GN Name=POLIA; OrderedLocusNames=At1g50840; ORFNames=F8A12.8;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION, AND NON-AUG INITIATOR START CODON.
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 [7]
RP FUNCTION.
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).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23167278; DOI=10.1111/ppl.12009;
RA Cupp J.D., Nielsen B.L.;
RT "Arabidopsis thaliana organellar DNA polymerase IB mutants exhibit reduced
RT mtDNA levels with a decrease in mitochondrial area density.";
RL Physiol. Plantarum 149:91-103(2013).
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. May be
CC required for DNA repair in both organelles. {ECO:0000250,
CC ECO:0000269|PubMed:21427281, ECO:0000269|PubMed:23167278}.
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: Plastid, chloroplast. Mitochondrion.
CC Note=Targeted to chloroplast when translation is initiated at the AUG
CC initiator start, and to mitochondrion when it is initiated at a non-
CC canonical CTG leucine codon located 21-bp upstream of the initiator
CC methionine codon. {ECO:0000269|PubMed:16169894}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot apical meristem.
CC {ECO:0000269|PubMed:15993837}.
CC -!- DISRUPTION PHENOTYPE: Retarded growth and reduced levels of DNA in both
CC mitochondria and plastids. Double homozygous mutants polIa and polIb
CC are sterile. {ECO:0000269|PubMed:23167278}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC -!- CAUTION: This sequence can initiate at a non-canonical CTG leucine
CC codon. This non-AUG initiator start codon is located 21-bp upstream of
CC the initiator methionine codon (PubMed:16169894).
CC {ECO:0000305|PubMed:16169894}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50942.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50942.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
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DR EMBL; AB211532; BAE10873.1; -; mRNA.
DR EMBL; AC079284; AAG50942.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32595.1; -; Genomic_DNA.
DR EMBL; AF462826; AAL58915.1; -; mRNA.
DR EMBL; AY091072; AAM13892.1; -; mRNA.
DR PIR; D96545; D96545.
DR RefSeq; NP_175498.2; NM_103965.5.
DR AlphaFoldDB; F4I6M1; -.
DR SMR; F4I6M1; -.
DR BioGRID; 26731; 1.
DR STRING; 3702.AT1G50840.1; -.
DR PaxDb; F4I6M1; -.
DR PRIDE; F4I6M1; -.
DR EnsemblPlants; AT1G50840.1; AT1G50840.1; AT1G50840.
DR GeneID; 841506; -.
DR Gramene; AT1G50840.1; AT1G50840.1; AT1G50840.
DR KEGG; ath:AT1G50840; -.
DR Araport; AT1G50840; -.
DR TAIR; locus:2036361; AT1G50840.
DR eggNOG; KOG0950; Eukaryota.
DR HOGENOM; CLU_004638_0_0_1; -.
DR InParanoid; F4I6M1; -.
DR BRENDA; 4.2.99.B1; 399.
DR PRO; PR:F4I6M1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I6M1; baseline and differential.
DR Genevisible; F4I6M1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
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:TAIR.
DR GO; GO:0033259; P:plastid DNA replication; IMP:TAIR.
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 Chloroplast; DNA damage; DNA repair; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; Mitochondrion;
KW Nuclease; Nucleotidyltransferase; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..91
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 92..1050
FT /note="DNA polymerase I A, chloroplastic/mitochondrial"
FT /id="PRO_0000429309"
FT DOMAIN 312..490
FT /note="3'-5' exonuclease"
FT REGION 202..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..1048
FT /note="Polymerase"
FT COMPBIAS 226..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 79
FT /note="Missing (in Ref. 1; BAE10873 and 4; AAL58915/
FT AAM13892)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1050 AA; 117234 MW; E9C83C875ACA43D7 CRC64;
MAMGVSLTSH NNPLLRHLSP SSSWVSRSSS RLSSSPLPSF LFPCRRTLLQ RKLASTDGNV
GYCTTTVCQG FQHSVHQRSS SVVFNGEWEL RSESNKVRMV PKIIKVGNQT EVAETHQVPG
TVSAWREEAN KLRERNGQIA RNLDDNGYFN GSVPIISSAP SYETSQKIDY EFKPRGTTRS
TTATLNKELI GITQSEPVVS LPRKGLDVGD NMDVNPKGEG IQRPLISDKS SGTANGNKNT
VAISKVERST EPSNVRENLG KIYDKVLIVD NVQAAKDTVA KLVNQFRNHV HSCDTEVSGI
EVKEETPVDH GELICFSIYC GPEADFGNGK SCIWVDVLGE NGREVLAEFK PYFEDSFIRK
VWHNYSFDSH IIRNHGIEIS GFHADTMHMA RLWDSARRIK GGYSLEALTS DPKVLGGTQT
KEEAEFLGKI SMKTIFGKRK LKKDGSEGKI VVIPPVEELQ REDREAWISY SALDAISTLK
LYESMTKKLQ LMDWHLDGKP VLGRTMLDFY HEFWRPFGEL LVKMEAEGIL VDREYLAEIE
KVAKAEQQVA GSRFRNWASK YCPDAKYMNI GSDTQLRQLF FGGISNSHDE VLPVEKLFKV
PNIDKVIEEG KKTPTKFRNI KLHRISDSPL STENFTASGW PSVGGDVLKE LAGKVSAEYD
FMDDVSDISL EEVVEDDDVE TSETQKSKTD DETDTSAYGT AYVAFGGGER GKEACHAIAS
LCEVCSIDSL ISNFILPLQG SNVSGKDGRV HCSLNINTET GRLSARRPNL QNQPALEKDR
YKIRKAFVAS PGNTLVVADY GQLELRILAH LTGCKSMMEA FKAGGDFHSR TAMNMYPHVR
EAVENGQVIL EWHPEPGEDK PPVPLLKDAF GSERRKAKML NFSIAYGKTA VGLSRDWKVS
TKEAQETVDL WYNDRQEVRK WQEMRKKEAI EDGYVLTLLG RSRRFPASKS RAQRNHIQRA
AINTPVQGSA ADVAMCAMLE ISINQQLKKL GWRLLLQIHD EVILEGPIES AEIAKDIVVD
CMSKPFNGRN ILSVDLSVDA KCAQNWYAAK
