ID A0A368F407_ANCCA Unreviewed; 471 AA.
AC A0A368F407;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=ANCCAN_27428 {ECO:0000313|EMBL:RCN26844.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN26844.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN26844.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN26844.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCN26844.1}.
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DR EMBL; JOJR01005856; RCN26844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368F407; -.
DR STRING; 29170.A0A368F407; -.
DR Proteomes; UP000252519; 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: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 Gene3D; 1.10.287.690; Helix hairpin bin; 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; 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 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};
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}; Nucleus {ECO:0000256|RuleBase:RU365029};
KW Reference proteome {ECO:0000313|Proteomes:UP000252519};
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 4..87
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 265..446
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:RCN26844.1"
SQ SEQUENCE 471 AA; 54181 MW; 288BE92F0B65203B CRC64;
TATIKRFFDH ILEVRPNVIV TYNGDFFDWP FVETRARIRG INMEDEIGFA KDSADEFKSR
NCIHMDAFRW VKRDSYLPVG SQNLKAVAKA KLRYDPVEVD PEDMCKMARE DPQSLANYSV
SDAVATYYLY MKYVHPFVFA LCTIIPLGPD DVLRKGSGTL CEALLMVEAF HNNIVFPNKF
TGDGGHVEAL EAGVFRADIP CKFRLAPAAL KSLRDSVPET IEKELIREFG IPLENVVDFE
ERCAEVQETF DNLLAIPARM ENPRIYHLDV GAMYPNIILT NRLQPCAMVN EEICMACTYN
RPDAKCKRVM NWEWRGELNY CRRVYGRTHL TRLEMRQTMI CQRENAFYVD TVKAFRDRRY
EYKELLKKAK GSLDEISKDD IAGIKAAQGR VVLYESLQLA HKCILNSFYG YVMRKGSRWF
SMEMAGIVCH TGANIITEAR KLVEQIGKPL ELDTDGKFTF YGCAPFFFSR L
//
