ID   A0A183PFG1_9TREM        Unreviewed;       985 AA.
AC   A0A183PFG1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN   ORFNames=SMTD_LOCUS13097 {ECO:0000313|EMBL:VDP62724.1};
OS   Schistosoma mattheei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=31246 {ECO:0000313|WBParaSite:SMTD_0001309601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMTD_0001309601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP62724.1, ECO:0000313|Proteomes:UP000269396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Denwood {ECO:0000313|EMBL:VDP62724.1}, and Denwood, Zambia
RC   {ECO:0000313|Proteomes:UP000269396};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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|RuleBase:RU365029};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365029}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|RuleBase:RU365029}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; UZAL01033151; VDP62724.1; -; Genomic_DNA.
DR   STRING; 31246.A0A183PFG1; -.
DR   WBParaSite; SMTD_0001309601-mRNA-1; SMTD_0001309601-mRNA-1; SMTD_0001309601.
DR   Proteomes; UP000269396; 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: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   InterPro; IPR013697; DNA_pol_e_suA_C.
DR   InterPro; IPR029703; POL2.
DR   PANTHER; PTHR10670:SF0; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT 1; 1.
DR   PANTHER; PTHR10670; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR   Pfam; PF08490; DUF1744; 1.
DR   SMART; SM01159; DUF1744; 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|RuleBase:RU365029};
KW   Iron {ECO:0000256|RuleBase:RU365029};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU365029};
KW   Metal-binding {ECO:0000256|RuleBase:RU365029};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU365029};
KW   Nucleus {ECO:0000256|RuleBase:RU365029};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269396};
KW   Transferase {ECO:0000256|RuleBase:RU365029};
KW   Zinc {ECO:0000256|RuleBase:RU365029};
KW   Zinc-finger {ECO:0000256|RuleBase:RU365029}.
FT   DOMAIN          253..731
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
SQ   SEQUENCE   985 AA;  111575 MW;  B629AF69E6218FCF CRC64;
     MLNYRPSHDI PNSNLQLRFT NFQVIEIVPD PGRIGHYTLW VLINSPDSGL VPSLNAVDVT
     VSRNFYVNMR TPKPKDSGPL FRKVSGNVSM GNETRSASGL ILPRNHTVYH LYEYNVPESV
     YTEHAPEIAT DLARPDVEGV YELGVPSLFR ILMKVGCLCT VDREAFRNNQ HGPVSDEGSF
     NLDQLCFCSL AQHPYLSGCG LRHLFLFHYQ LPSVGQAITR KDSQRQLYLL IVPWTRCGYV
     CVIDSARINQ LPDLNVLYLR QRTKCFPQYE NEDFPPDTLN FEVRTESDAV IGRRIVQRWI
     TGLCKSMGAR EANSKEANIT SSQSAAPIVI LLHSSLSATQ QDISSGSNEV NWPLNGEIIG
     RRRSPQLPVL SEFPVIQLGG TMDDGESQIG DVEYSMDAYS LLNWQQAAVK RGIRYFLQSE
     ARLERQLELA RYLHIPVGNI PVSEAPLPVS LTPPSQDIQP PASSINAIEL GCDLFYARHL
     VKHNHVLWCS SSGRPDLGGK ETDDQRLLLE MEESGVVEIN RPGLYPYVNV ELEFTNLAVN
     TLIIANRIPE LEGATLLSFD RLSAADRTLE EQLNQGVNLG THITSYDETA ACSAAFRILR
     NMVLAWVRDV TQYQNPLADE QIIYFYQWLR SPRSLFYDPA LRRTVQKLMK KVFLKLVDEI
     SHFHVDVIYA NFSRLIMSTH RIELSEALAR VDYFTQLLRT RQGTLFTHLD LQYVTSWRQL
     IWMDSANYAG IKASVENLVD GKDVEWGKVL TIQHQSHTHT EDKENNIEGQ PNLPDPEVDM
     HWHLARYLPE TRGLRSKFQS LLAGYLLAIY NAVRNEHRRL IESISCSLNE PHGSLEFDAD
     MNKDPNCIHE AETTPYKSDA TVSPGVKEYE ERLFRDQLAP ELYNLIIRLQ RKAAWIDPEL
     VRKTDPSIGN NRTCQLNNGS NIPRNNDLVS AYLAEKSIGS GIEFDATNNN KNSSPNLVLP
     LLPAHQAIYT LNFTPLLDFI KSLCE
//