ID   DPOD1_SOYBN             Reviewed;        1088 AA.
AC   O48901;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=DNA polymerase delta catalytic subunit;
DE            EC=2.7.7.7;
GN   Name=POLD1;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Corsoy;
RA   Collins J.T.B., Cannon G.C., Heinhorst S.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This polymerase possesses two enzymatic activities: DNA
CC       synthesis (polymerase) and an exonucleolytic activity that degrades
CC       single-stranded DNA in the 3'- to 5'-direction.
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   -!- SUBUNIT: Heterodimer with subunits of 125 kDa and 50 kDa. The 125 kDa
CC       subunit contains the polymerase active site and most likely the active
CC       site for the 3'-5' exonuclease activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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-B family. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other DNA polymerase delta proteins, does not
CC       contain the Cys-rich regions at the C-terminus that coordinates zinc
CC       and 1 4Fe-4S iron-sulfur cluster. {ECO:0000305}.
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DR   EMBL; AF020193; AAC18443.1; -; mRNA.
DR   PIR; T05731; T05731.
DR   RefSeq; NP_001238693.1; NM_001251764.1.
DR   AlphaFoldDB; O48901; -.
DR   SMR; O48901; -.
DR   STRING; 3847.GLYMA04G38800.4; -.
DR   PRIDE; O48901; -.
DR   GeneID; 548092; -.
DR   KEGG; gmx:548092; -.
DR   eggNOG; KOG0969; Eukaryota.
DR   InParanoid; O48901; -.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0043625; C:delta DNA polymerase complex; IBA:GO_Central.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006287; P:base-excision repair, gap-filling; IBA:GO_Central.
DR   GO; GO:0045004; P:DNA replication proofreading; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   2: Evidence at transcript level;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Metal-binding; Nuclease; Nucleotidyltransferase; Nucleus;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1088
FT                   /note="DNA polymerase delta catalytic subunit"
FT                   /id="PRO_0000046451"
SQ   SEQUENCE   1088 AA;  123188 MW;  69559CDF5BE7598D CRC64;
     MTQEEEFMDE DVFINETLVS EDEESLILRD IEQRQALANR LSKWTRPPLS AGYVAQSRSV
     LFQQLEIDYV IAESHGELLP NSSGPVAIIR IFGVTKEGHS VCCNVHGFEP YFYICCPPGM
     GPDDISHFHQ TLEGRMREAN RNSNVGKFVR RIEMVQRRSI MYYQQSNSQP FLKIVVALPT
     MVASCRGILD RGIQLDGLGM KSFLTYESNV LFALRFMIDC NIVGGNWIGI PAGKYKKTAK
     SLSYCQLEFD CLYSELISHA PEGEYSKMAP FRILSFDIEC AGRKGHFPEP THDPVIQIAN
     LVTLQGEDQP FIRNVMTLKS CSPIVGVDVM PFETEREVLL AWRDFIREVD PDIIIGYNIC
     KFDLPYLIER ALNLKIAEFP ILGRIRNSRV RVKDTTFSSR QYGTRESKEV AVEGRVTFDL
     LQVMQRDYKL SSYSLNSVSS HFLSEQKEDV HHSIISDLQN GNAETRRRLA VYCLKDAYLP
     QRLLDKLMFI YNYVEMARVT GVPISFLLSR GQSIKVLSQL LRRARQKNLV IPNAKQAGSE
     QGTFEGATVL EARAGFYEKP IATLDFASLY PSIMMAYNLC YCTLVIPEDA RKLNIPPESV
     NRTPSGETFV KSNLQKGILP EILEELLTAR KRAKADLKEA KDPLEKAVLD GRQLALKISA
     NSVYGFTGAT IGQLPCLEIS SSVTSYGRQM IEHTKKLVED KFTTLNGYEH NAEVIYGDTD
     SVMVQFGVSA VEEAMNLGRE AAEHISGTFT KPIKLEFEKV YYPYLLISKK RYAGLFWTKP
     DNFDKMDTKG IETVRRDNCL LVKNLVNDCL HKILIDRDIP GAVQYVKNAI SDLLMNRMDL
     SLLVITKGLT KTGDDYEVKA AHVELAERMR KRDAATAPNV GDRVPYVIIK AAKGAKAYER
     SEDPIYVLEN NIPIDPHYYL ENQISKPILR IFEPILKNAS KELLHGSHTR SISISTPSNS
     GILRFAKKQL PALVVKLYLA RVITLSVHIA KEGRLSCTVK QYLKCLSWRC FLGGCGHSVR
     SAKVHFIRMF SAPVGIVQFS IDEKRHRKIW VKQSCNWTDG TSKFCQEFDL ADLFEPMDTN
     TIWCLPQS