ID A0A452YAX3_AEGTS Unreviewed; 1558 AA.
AC A0A452YAX3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET1Gv20359000.6, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET1Gv20359000.6}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) 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 EnsemblPlants; AET1Gv20359000.6; AET1Gv20359000.6; AET1Gv20359000.
DR Gramene; AET1Gv20359000.6; AET1Gv20359000.6; AET1Gv20359000.
DR Proteomes; UP000015105; Chromosome 1D.
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; cd05535; POLBc_epsilon; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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; IPR042087; DNA_pol_B_thumb.
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:UP000015105};
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 1179..1538
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 869..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1558 AA; 177242 MW; 1DF13E0F06626111 CRC64;
MQEVKPGIYV TYNGDFFDWP FLEKRAAHHG IKMNEEIGFQ CDSNQGECRA KFSCHLDCFA
WVKRDSYLPQ GSQGLKAVTK AKLGYDPLEV NPEDMVRFAM EQPQTMASYS VSDAVATYYL
YMTYVHPFIF SLATIIPMSP DEVLRKGSGT LCEMLLMVQA FQANIICPNK HQADLEKFYN
NRLVESETYI GGHVECLETG VFRSDLPTKF QLEPSAFEQL IENLDRDLQY AIAVEGKLDI
DSVTNYDEVK DAIKQKLVSL RDHPTREECP LIYHLDVAAM YPNIILTNRL QPPSIVTDVD
CTACDFNRPG KNCLRTLEWV WRGETYTAKK SDYHHIKRQI ESEMIQTGGV TSSKPFLDLS
KPEHLLKLKD RLKKYCQKAY KRVVDKPITE VREAGICMRE NSFYVDTVRS FRDRRYEYKG
LNKTWKGKLS EAKASGNSIK IQEAQDMVVL YDSLQLAHKC ILNSFYGYVM RKGARWYSME
MAGVVTYTGA KIIQNARLLV DKIGRPLELD TDGIWCVLPG SFPENFTFKT KAEKKLTISY
PCVMLNVDVA RTNTNDQYQT LKDPVSKLYT TNSECSIEFE VDGPYKAMIL PASKEEGILI
KKRYAVFNED GTLAELKGFE IKRRGELKLI KVFQAEVFDK FLHGSTLEEC YAAVASVANR
WLDLLDNQGI DISDSELLGF ISESSTMSKS LVDYGEQKSC AVTTAKRLAE FLGDSMVKDK
GLHCQYIVAR EPQGTPVSER AVPVAIFETD AEVAKFYLRK WCKVSTEANI RFILDWSYYK
QRLSSAIQKI ITIPAAMQKI SNPVPRVLHP DWLHKKVREK DDRFRQRKLR DMFSPLNKDM
GMHNLNGTGD IEDLLTSDKG LRKTTASHGF NIGKENHPNG SPSAKASLGH CKNQQKSVIR
SNEPLRDDSA DEIVDRSTDY QGWLEARKRK WKYVREQKKR RRLGAAASSE GPSNNLFSAR
NVSQLHGNSR NRSTFFQKQE LSLFRSHWQI IQLAPSTLPG RFFAWVVAEG IMFKIPINVP
RVFYLNSKAP ITDEFPGRRV KKILPHGKPS FNLIEVVTSE EQFRAEGRKL AAHLAEPDVE
GIYETKIPLE LNAILQIGCV CKVDKSAKKR NIQDGWDLAE LQMKTTAEFS YLEQTVSFFY
LYHSVSEGRA VYVMYFPTSL RVHAVVINPF RNKELSPVFL EKQFRDACQT PDPLHENLTF
QVDYHTSMDA GSKYVQRMLL EYRQQHPGPV IGIIECPKLQ AIRESVRALD DFPCVTIPCN
ARDNNYQALG WQATAGRTSM QRCAASTQWF NERISLARYA HVPLGNFELD WLLFTADVFF
SRALHDQQQV LWISDDGIPD LGGTYEGDIC FADEVIQPAL TYPGAYRRIS VELKIHHLAV
NSLLKSSQVD EMEGGSIGNF ENDIPPGPNA TETDYNDASL CLPAFQVLKQ LIQRCISDAV
SSGNVFADAI LQHLYRWLCS PRSRLHDPAL HRLLHNVMKK VFALFLAEFR KLGANVIFAN
FSKIIIDTGK VDLPSARAYC DSLLKTLQTR YCLTSCCRYV CHLSETKSIC VLGIFLSG
//
