ID A0A0C2G9X4_9BILA Unreviewed; 871 AA.
AC A0A0C2G9X4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
DE Flags: Fragment;
GN ORFNames=ANCDUO_16110 {ECO:0000313|EMBL:KIH53751.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH53751.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH53751.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH53751.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KN740458; KIH53751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2G9X4; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
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:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide 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 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; 2.
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; 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; 2.
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|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}; Exonuclease {ECO:0000313|EMBL:KIH53751.1};
KW Hydrolase {ECO:0000313|EMBL:KIH53751.1};
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 Nuclease {ECO:0000313|EMBL:KIH53751.1};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU365029}; Nucleus {ECO:0000256|RuleBase:RU365029};
KW Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365029};
KW Zinc {ECO:0000256|RuleBase:RU365029};
KW Zinc-finger {ECO:0000256|RuleBase:RU365029}.
FT DOMAIN 62..269
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 276..329
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 694..756
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIH53751.1"
FT NON_TER 871
FT /evidence="ECO:0000313|EMBL:KIH53751.1"
SQ SEQUENCE 871 AA; 99729 MW; E331B3637156F390 CRC64;
AELIEEQTKA IISAVDFYFI QGNGERFKNS YPFRPYFYIS ASDGAEHQVA SFLTKKYGGS
LVVDIMDKED LDLKNHLSGL KKTYLKLSFP STSELAKVKR DLMPHIRKNK ERVKKESQYC
SYLARNMGGS KYDTQNGDVF SDILDIREYD LPYHMRVAID EKYFVGKWYT VRGISSNRKP
SIVNHPTLID PIDPVVLAFD IETTKLPLKF PDSSTDEIMM ISYMIDGKGF LIINRDIVSA
DIESFEYTPK EEYKGKFFIF NEPDETATIK RPFVETRARI RGINMEDEIG FAKDAADEFK
SRNCIHMDAF RWVKRDSYLP VGSQNLKAVA KAKLRYDPVE VDPEDMCKMA REDPQSLANY
SVSDAVATYY LYMKYVHPFV FALCTIIPLG PDDVLRKGSG TLCEALLMVE AFHNNIVFPN
KFTGDGEAKS TKDGHRIESE TYVGGHVEAL EAGVFRADIP CKFRLAPAAL KSLRDSVPET
IEKELIREFG IPLENVVDFE ERCAEVQETF DNLLAIPARM ENPRIYHLDV GAMYPNIILT
NRLQPCAMVN EEICMACTYN RPDAKCKRVM NWEWRGELTP ATRGELQQII QQLEGETFGK
PPKAFHQLER AERQSIEKKR VQDYSRRVYG RTHLTRLEMR QTMICQRENA FYVDTVKAFR
DRRYEYKELL KKAKGSLDEI SKDDIAGIKA AQGRVVLYES LQLAHKCILN SFYGYVMRKG
SRWFSMEMAG IVCHTGANII TEARKLVEQI GKPLELDTDG IWCLLPASFP ENITFKLQNH
KRKSITVSYP GAMLNAVVNA GFTNDQYHNL QPDGSYTISK ENSIFFEVDG PYQCMVLPAS
KEEGKKLKKR YAVFNLEGSL AELKGFEVKR R
//
