UniProt: A0A2G5VSQ4

Database: UniProt
Entry: A0A2G5VSQ4_9PELO

LinkDB:  A0A2G5VSQ4_9PELO 
Original site:  A0A2G5VSQ4_9PELO

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   SMART (2)   
All databases (25)   

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ID   A0A2G5VSQ4_9PELO        Unreviewed;      2157 AA.
AC   A0A2G5VSQ4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN   Name=Cni-pole-1 {ECO:0000313|EMBL:PIC54700.1};
GN   Synonyms=Cnig_chr_I.g3843 {ECO:0000313|EMBL:PIC54700.1};
GN   ORFNames=B9Z55_003843 {ECO:0000313|EMBL:PIC54700.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC54700.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) 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:PIC54700.1}.
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DR   EMBL; PDUG01000001; PIC54700.1; -; Genomic_DNA.
DR   STRING; 1611254.A0A2G5VSQ4; -.
DR   Proteomes; UP000230233; Chromosome i.
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; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000230233};
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          1471..1873
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
FT   REGION          1174..1196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          566..593
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2157 AA;  245927 MW;  6EB31467734CEE81 CRC64;
     MSSKDDLLAQ AVENDANYKE RLSLIKSNDA IDAKLGFVRY TGIQEKKGFL INIQPSELVD
     EQTKVIVSVV DYFFISDMDE RFKISYPFRP YFYIATLDGF EFQVSSYLSK KYGAQAQVEH
     MDKEDLDLKD HLSGLKKTYI KLSFTSTVEM MKIRKDLMPL VRKNTDRIKK ESAYADYLAR
     NLGGKGGNSG TSDAQLDGDI LNQIVDIREY DVPFHMRVSI DEKIFVGLWY DVKGVGPNRV
     PTINRKDLAF FHAKPRVLAF DIETTKLPLK FPDRESDEIM MISYMVDGRG FLIINREIVS
     ADINAFEYTP KAEYKGEFTV WNEKDETALI RKFFDHFLQV RPNIVVTYNG DFFDWPFVEA
     RAKIRGFNME KEIGFSKDSA DEYKSRNCIH MDAFRWVKRD SYLPVGSQNL KAVTKAKLRY
     DPVEVEPELM CKMAREQPQQ LANYSVSDAV STYYLYMKYV HQFIFALCTI IPLGADDVLR
     KGSGTLCEAL LMVEAFHSNI VFPNKYTGPE ETRFSKDGHR VESETYVGGH VEALEAGVFR
     ADIPARFRLS VDALEQLKSE VPETLRKELA REFEVSLDQV ENFEQQCAEV EEAFDGLIAV
     PTRLENPRIY HLDVGAMYPN IILTNRLQPC AMVNEEICMG CSFNKPDAEC KRTMAWEWRG
     ELTPATRGEY QQIMQQLEAE SFGKPPKHFH MLERAEREAI EMKRVKDYSR RVYGKTHLTK
     LEMRETMICQ RENHFYVETV KAFRDRRYEY KDMLKKAKGR FDQAQAENDL ATVATSKLEM
     VLYESLQLAH KCILNSFYGY VMRKGSRWYS MEMAGIVCHT GANIIKEARK LVDKIGKPLE
     LDTDGIWCLI PASFPENVTF KLKNHKRNQV TVSYPGAMLN ALVYEGFTNH QYFTLQKDGS
     YLKSSENSIY FEVDGPYQCM VLPASKEEGK KLKKRYAVFN LDGSLAEMKG FELKRRGELN
     IIKHFQSHVF KTFLNGKTLE ETYKAVAGDA NHWLDILHSH GEEISDEELF DLISENRSMS
     RKLEDYGSQK STSISTAKRL AEFLGDDMVK DAGLACMFII SRHPIGAPVT ERAIPVAIFK
     ADSKVKSHYI RKWTKQQDYD EDTDIRDMLD WDYYIERFGS CIQKIITIPA ALQGVVNPVP
     RVPHPDWLQN KIRNKVDAHK QPRINQIFAA CQKPSTSSTL ENGKRRRSPD VEEGSDDVIV
     EDVDSQEGDK ENLAKRKKAV ETKKNQEAEV LEKKTLVDHG FDDWLGFLKK KWRIQRKERK
     NQLKTARDSD AVDTIVRGAR EAESEREWHI LSVEPTADSS FFNVWLSVQG QMQKLTLKVG
     RKILVDSRAP RGNRETVRRV LPHHKPPGYL YEFKTDEAQL TALMDKLYSE TCSSTIDGIY
     ESEVPTEFRA VLQLGSTVRP DHGVSLGGHQ LTLESLRPME KMSYLPNEQN IRTIFLYKFS
     QDTRHVYSLI DTSGSAAYFY VVNSGDVQLP NMDALYTSAY NKIMSTERGQ LCKTPEKMPF
     TVKRLSSNQE CERQLGRALR AFREFSSKTA VVLLLSDTEP SRLARKIPNL GLFPNVQLHI
     TEPSSLLNQI DWQKVVARRV LQHYFNSFFF LTDYLEWARY LRVPLGNLPA DHALFGLDLL
     YARHLQKSGH ALWATKSSRP DLGGKELDDI RLSIDWNPLS VDDTVLLNRE TFCETACVEL
     QLSAVAVTAL VQRSRVLEAE GADDVVTFDS MNTIAQQSVT GGTQNSIACY DEGAAVDASI
     KILKQMLTEC VRHIAHQGNR HADEVVMTVS RWLNTRSALL FDSALTRSIS VLESKLVLLL
     CAECERIGAK VIHATAQKLV LNTGKMTSEE AKGFVEMLIQ SLSTNVVFAA LHITPVKFFD
     SMLWMDAHNH TGICIVDGDS ESPDVIDDSL PTSSSSSQPQ ATRQFETTAI WKIAEEMPDE
     SNIRDEFLQM IGAFILEFLE TNREVQFDSE SAATFRADVI SQKISHRLYR VVNKLVHNNA
     ESAHCATYLV NAICRALSCD QTSQLAVEGV RDNARRLLHN VVVEVDMTPL RQTTLFVPNV
     FCSSCSQASN VFLSSTDEIL TCTTCQSKLN SDVIDMMICD RLNQLLTAYQ IQDHQCAKCK
     SVRHDSLSLY CECCSPFNPQ ITPTQLKHEA TTVETVANIR NFTLSSELAT WILKMVV
//

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