POLIB_ORYSJ
ID POLIB_ORYSJ Reviewed; 1035 AA.
AC Q6Z4T3; Q0J7N8;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA polymerase I B, mitochondrial;
DE EC=2.7.7.7;
DE AltName: Full=DNA polymerase PolI-like B;
DE Short=OsPolI-like B;
DE AltName: Full=DNA polymerase gamma 2;
DE Flags: Precursor;
GN OrderedLocusNames=Os08g0175600, LOC_Os08g07850;
GN ORFNames=OJ1134_B10.10, OSJNBa0054L03.41;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 5'-3' exonuclease activity. May be required for DNA
CC replication and accumulation in mitochondria (By similarity).
CC {ECO:0000250}.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF23027.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP003882; BAD05229.1; -; Genomic_DNA.
DR EMBL; AP005164; BAD05556.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF23027.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015650229.1; XM_015794743.1.
DR AlphaFoldDB; Q6Z4T3; -.
DR SMR; Q6Z4T3; -.
DR STRING; 39947.Q6Z4T3; -.
DR PaxDb; Q6Z4T3; -.
DR PRIDE; Q6Z4T3; -.
DR GeneID; 4344791; -.
DR KEGG; osa:4344791; -.
DR InParanoid; Q6Z4T3; -.
DR OrthoDB; 931773at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q6Z4T3; OS.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
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 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; Mitochondrion;
KW Nuclease; Nucleotidyltransferase; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..1035
FT /note="DNA polymerase I B, mitochondrial"
FT /id="PRO_0000429312"
FT DOMAIN 317..478
FT /note="3'-5' exonuclease"
FT REGION 100..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..1032
FT /note="Polymerase"
SQ SEQUENCE 1035 AA; 116210 MW; BEBCBA9412AB1F29 CRC64;
MAVAPPLPPA PARLLRRWQG SSPWLSSSFG RTRYFSRPAF AAGGRQDYSP SSGMGVSKTG
AFRLGLHGNL NVQSSVQEWV DETKRLFFLR TTNNVRNNIT NGTTPLRVGN LRHDPSEDIR
SSNYPSLYNQ RERGPSNSIV NRHVDTDLAK HRVMYQSAHA VPAPFSVANN DIKPLNLLDG
SKEEIPWHDS VTVESSLPKV SKSETTLVVD KAIPNKKEHK RITRKVTLNI PDKASLSTES
KNARKLLATI YDKVLVVDNV ESARSVVKLL TTKYKGFIHA CDTEVANIDV KEETPVGHGE
VICFSIYSGN SDGEADFGNG KTCIWVDVLD GGRDVLMEFA PFFEDPSIKK VWHNYSFDSH
VIENCGIKVA GFHADTMHLA RLWDSSRRAD GGYSLEGLTN DHRIMNAVLK DIHKTGKVSM
KTIFGRKNVR KNGSEGKTIS IEPVKKLQRE DRELWICYSS LDSMSTLKLY ESLKNKLEAK
EWIFDGCPRG TMYDFYEEYW RPFGALLVKM ETEGMFVDRA YLSEIEKTAV VERKLAADKF
RKWASKHCPD AKYMNVNSDN QIRQLFFGGI KNRNKPGETW PQSKAFKVPN DESIATEGKK
IPKSRTIKLF TIVEDLKLFT TEGKKTTKTG WLKVRGDVLW SLAGKIPTDH IYKIDDDGQE
FDEDGSSVEL PEQDIEDTSP YGTAYEAFGG GKKGREACHA IAALCEVFSI DKLISGFIVP
LQGDHISCKE GRIHCSLNIN TETGRLSART PSLQNQPALE KDRYKIRQAF VAAPGNTLIV
ADYGQLELRI LAHLTNCKSM LEAFKAGGDF HSRTAMNMYQ HVRDAVEEKK VLLEWHPQPG
QDKPPVPLLK DAFGAERRKA KMLNFSIAYG KTAVGLSQDW NVEVREARDT LKLWHRDRKE
ISAWQKKQKA LAFEKCEVYT LLGRSRQFPN MTHAGPGQKS HVERAAINAP VQGSAADVAM
CAMLEIERNA RLKELGWRLL LQVHDEVILE GPTESAEEAK AIVVECMSKP FYGTNILKVD
LAVDAKYAKS WYAAK
