ID A0A0D3F5K4_9ORYZ Unreviewed; 2230 AA.
AC A0A0D3F5K4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART02G17930.2};
RN [1] {ECO:0000313|EnsemblPlants:OBART02G17930.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART02G17930.2};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART02G17930.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- FUNCTION: DNA polymerase II participates in chromosomal DNA
CC replication. {ECO:0000256|RuleBase:RU365029}.
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 Evidence={ECO:0000256|RuleBase:RU365029};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU365029};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365029}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU365029}.
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DR STRING; 65489.A0A0D3F5K4; -.
DR PaxDb; 65489-OBART02G17930-2; -.
DR EnsemblPlants; OBART02G17930.2; OBART02G17930.2; OBART02G17930.
DR Gramene; OBART02G17930.2; OBART02G17930.2; OBART02G17930.
DR eggNOG; KOG1798; Eukaryota.
DR Proteomes; UP000026960; Chromosome 2.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd05779; DNA_polB_epsilon_exo; 1.
DR CDD; cd05535; POLBc_epsilon; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
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; IPR013697; DNA_pol_e_suA_C.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR029703; POL2.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10670:SF0; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT 1; 1.
DR PANTHER; PTHR10670; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08490; DUF1744; 1.
DR SMART; SM01159; DUF1744; 1.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU365029};
KW DNA replication {ECO:0000256|RuleBase:RU365029};
KW DNA-binding {ECO:0000256|RuleBase:RU365029};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU365029};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365029};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU365029};
KW Metal-binding {ECO:0000256|RuleBase:RU365029};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU365029};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365029};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365029};
KW Zinc {ECO:0000256|RuleBase:RU365029};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU365029}.
FT DOMAIN 1548..1927
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2230 AA; 254177 MW; D428A40D95F130DC CRC64;
MGGGGGGDGR RRRPSAGGGG GGGGRGGGWR SGSSAAKEQR LRLGAEELLE SRLGFAPYAD
SERRLGWLLT FSPSSWEDED TGKIYSCVDL YFVSQDGSTF KVKYKFPPYF YAATKDKMEL
EVEAYLRRRY EGDIADIEII EKEDLDLKNH LSGLKRKYLK IQFDTVQQLM RVRSDLLHVV
EKNEEELNAA EAFESIYGVK SLCSDDLVHY DRVERPQDYI NCIIDLREYD VPYHVRFAID
NDVRCGQWYD VSVSSSDVLL HRREDLLQRA EVHVCAFDIE TTKLPLKFPD AEYDTVMMIS
YMIDGQGYLI INRECVGEDI EDLEYTPKPE FEGHFKVKNV ANELDLLKAW FSHMQEVKPG
IYVTYNGDFF DWPFLEKRAA HHGIKMNEEI GFQCDNNQGE CRAKFSCHLD CFAWVKRDSY
LPQGSHGLKA VTKAKLGYDP LEVNPEDMVR FAMEQPQTMA SYSVSDAVAT YYLYMTYVHP
FIFSLATIIP MSPDEVLRKG SGTLCEMLLM VQAFKANIIC PNKHQADLEK FYNNRLLESE
TYIGGHVECL ETGVFRSDLP TKFQLEPSAC EQLIANLDRD LQYAISVEGK LDIDSVTNYD
EVKDAIKQKL VSLRDHPIRE ECPLIYHLDV AAMYPNIILT NRLQPPSIVT DVDCTACDFN
RPGKNCLRTL EWVWRGETYM AKKSDYHHIK RQIESEMIQA GGVTPSKPFL DLSKPEHLLK
LKDRLKKYCQ KAYKRVVDKP ITEVRNAGIC MRENSFYVDT VRSFRDRRYE YKGLNKSWKG
KLAEAKANGN SIKIQEAQDM VVLYDSLQLA HKCILNSFYG YVMRKGARWY SMEMAGVVTY
TGAKIIQNAR LLVDKIGKPL ELDTDGIWCV LPGSFPENFT FKTNAGKKLT ISYPCVMLNV
DVARNNTNDQ YQTLNDPVNK LYTTHSECSI EFEVDGPYKA MILPASKEEG VLLKKRYAVF
NEDGTLAELK GFEIKRRGEL KLIKVFQAEN QGIDISDNEL LDFISESSTM SKSLVDYGEQ
KSCAVTTAKR LAEFLGDSMV KDKGLHCQYI VAQEPQGTPV SERAIPVAIF ETDAEIAKFY
LRKWCKISSE ASIRSIVDWS YYKQRLSSAI QKIITIPAAM QKAIYFLLIS NPVPRVLHPD
WLHKKVREKD DRFRQRKLRD MFNPLEKDRG VQNLDGTGDM EDLLTLDGGM RKSHVPNGFG
KENKPNDAPS TEAGSKHSKN KQKSITRSNE PLAVHIQNDA ADEQVDRSTD YQGWLDAKKR
KWKYVREQKK RQRLGAAVTS DGPTNDLFSA RNVGQLHGNA RNRSTFFQKQ ELALFRSHWQ
ACYFCYSIML CNMCYDINLS VIYSFTLMPD KLIYCPHQII QLASSTLPGH FFAWVVAEGI
MFKIPINVPR VFYLNSKAPV TEEFPGRRVK KILPHGRPCF NLIEVVTSEE QFRVEGKKLA
AHLAEPDVEG IYETKILPEL NAILQIGCVC KVDKSAKRRS IQDGWDLAEL QMKTTAECSY
LEQTVSFFYL YHSLSEGRGV YVMYFPTSFR IHAVVVNPFR NKELSPSFLE KQYRDACQAL
GSLHENITFL VDYHTSIDAG SKHVQRMLLE YRQQHPGPVI GIIECPKLQA LKSAVRALDD
FPCVTIPCNA RDNNYQALGW QATAGRTSMQ RCAASTQWFN ERISLARYAH VPLGNFELDW
LLFTADVFFS RALRDQQQVL WISDDGIPDL GGTYEGDTCF ADEVIQPALT YPGAYRRVAV
ELKIHHLAVN SLLKSSQVDE MEGGPIGSFA NDMPAGPNGT ETEFDDATLC LPAFQVLKQL
IQRCISDAVS SGNVFADAIL QHLYRWLCSP RSKLHDPALH RLLHNVMKKV FALMLAEFRK
LGANVIFANF SKIIIDTGKV DLSSACEYCD SLLKTLQTRD IFEWVELEPL HYWHSLLFMD
QYNYGGIQAK MQNATSEGSS DGDNDIDIVS SWNIAEYLPK ATQDHFVLIV SEFLYVPWKY
MKEQVALRST TRDETSCTPS ITIMAAENLE VQVIGYLRDQ ISNYFADKLL RIVSDILHHF
KGKGKSESVE LTNREPDPHT HKGDAALEFI KHICAVLALD QNVQHDILEF APEAQFQDPC
ASFTLPNVIC SYCNDCRDLD LCRDSTLQGQ EWRCAVPQCG QPYHREQMEN ALLQVVRQRE
RLYHLQDLVC LRCRQVKAAH LSEQCSCGGA FRCKEESSQF LSKMRVFLNV AVSQKFELLQ
DVVQWILEVR
//
