UniProt: A0A2T0FNJ4

Database: UniProt
Entry: A0A2T0FNJ4_9ASCO

LinkDB:  A0A2T0FNJ4_9ASCO 
Original site:  A0A2T0FNJ4_9ASCO

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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   A0A2T0FNJ4_9ASCO        Unreviewed;      2170 AA.
AC   A0A2T0FNJ4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN   ORFNames=B9G98_04182 {ECO:0000313|EMBL:PRT56562.1};
OS   Wickerhamiella sorbophila.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trichomonascaceae; Wickerhamiella.
OX   NCBI_TaxID=45607 {ECO:0000313|EMBL:PRT56562.1, ECO:0000313|Proteomes:UP000238350};
RN   [1] {ECO:0000313|EMBL:PRT56562.1, ECO:0000313|Proteomes:UP000238350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS02 {ECO:0000313|EMBL:PRT56562.1,
RC   ECO:0000313|Proteomes:UP000238350};
RA   Ahn J.O.;
RT   "Genome sequencing of [Candida] sorbophila.";
RL   Submitted (APR-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:PRT56562.1}.
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DR   EMBL; NDIQ01000022; PRT56562.1; -; Genomic_DNA.
DR   STRING; 45607.A0A2T0FNJ4; -.
DR   OrthoDB; 5475218at2759; -.
DR   Proteomes; UP000238350; 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: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; 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:UP000238350};
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          1499..1874
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
SQ   SEQUENCE   2170 AA;  247056 MW;  67062D48C05DEDE4 CRC64;
     MAHYRRNDAP TNLAIDATSQ IRREHAVALT DTIDASMGFE RFDSGPPRVG WLVNFQATSQ
     SDPNIPNGKA AVDFYFIDDE GGCFKSTIRY DPYFLVKCSP GKEADVEEYI RKNLEGVVKE
     TRRVIKDDLS LPNHLIGRKQ SLIEVRFWNV TNLLAARKTL APFAEANQKK LAQYADYGAD
     YAQSALNKSF SAKSDASDYI LDIREYDVPY HVRVSIDLDV RVGKWYTVTA VEGVVSLTEF
     ARIERADPVV LAFDIETTKQ PLKFPDAAID CVMMISYMIN GEGYLITNRE VVSKDIDDFE
     YTPKPEFKGE FTIFNEANER DLLTRFFDHI KEEKPTVIVT FNGDFFDWPF VDARANVHGI
     NMYEEIGFRK DMEDEYKSAH CAHMDAFRWV KRDSYLPQGS QGLKAVTSAK LGYNPLELDP
     EKMTPYASEK PQVLAEYSVS DAVATYYLYM KYVHPFIFSL CNIIPLKPDE VLRKGTGTLC
     EMLLMVQAYQ KGILLPHKHQ DPLERFYNGH LVESETYVGG HVESLEAGVF RNDIPTHFSV
     DQNAIEQLLQ ELDEALKFTI QVEAKMDLQK VTNYDEIKQQ ITEKLISLKE APSRTETPLI
     YHVDVASMYP NIMTTNRLQP DSMVSERDCA MCDFNRPGKD CDRRLPWAWR GEFYPAEKSE
     YLMIRKTLEQ ETFPRPNRDR NGKKTFRTFD ELPPFEQAQL IKKRVSDYSR KVYHKIKQTE
     TVEREAIICQ RENPFYVNTV RDFRDRRYEF KGLQKVWKRK LDEVPKSDIP SVEEAKKMIV
     LYDSLQLAHK VILNSFYGYV MRKGSRWYSM EMAGVTCLTG ATIIQLARSR VEQLGRPLEL
     DTDGIWCILP SSFPGDFMFT FSDGKKLPIA YPCVMLNHLV HAKFTNHQYQ ILVDPGTFQY
     ETISDNSIYF EVDGPYKAMV LPTSTEEGKN LKKRYAVFNM DGSLAELKGF ELKRRGELRI
     IKAFQSQIFK EFLEGVSLEE CYGAVAKVAN AWLDVLDTRG KHLEDADLMD LISENKVMSK
     SLKDYAGQKS TSICTARRLA EFLGSQMIKD SGLACHYVIS KLPYGAPVTD RAIPVEVFSA
     EYEVKRKFLR AWLKSPGLEN FDPREIIDWD YYRARLASTI QKIITIPAAL QSVSNPVPRV
     AHPDWLNKRV AAMNDRFKQK KITGFFTMPS EKSELLKPKQ TLVDIEDVLS TGLGVEVNGQ
     KRAVVHKRKA GEDDSVGADD LAVLEISNDT VAPDPEDDYS AWLRYQKVIW QKKYEQRETR
     RKLFGDKVSL RYNRGVTGML RNQAEQAFSG RSWHIVQVTA SPGKLGQVQA FIWVNSRIQK
     IKINVPRRFF VQFTDVPNLT LPSGITMEKS SKSLPHGVSN DNLYEVVMSE EAYQDELARG
     GGLLKQQTVK GVYETQLEPR DRVLLEIGTL CSLDSSRPGI LGKGLESGFE LEWLRPYRPR
     KGAEHEPIPY LKSTNLGYIF LQHYEISNQV FIAVTTSWSS KAYLVHYSAS NVNANEPLRV
     GAMYGDSFTS LQSSDVSQPY FNFQENLEFD TINCSSLSKV YTHTNNILSD ILAERGTHAV
     LTLQSARIER LYNRIRAIDD FASFEIKSRD GVLPSVGWQP ALSKRIVKSY FRLQYWIEQL
     HSKAIFSNIP IGNLNSGDSN DLIDILFARK LLNDNVVLWW SNRPLPDLGG GEAGNVLANN
     EETVIPSFNN PGFYGKVCID IDVSNLSVNS ILTAVLFNAA DGLDFSENNS LFGQNKLSAS
     ALSALSSLVK EWWSTAAKGD VVADNLIQHF ITWVSSPQSK MYDPPLLYYV QNLSRKALLQ
     LIGELHNFGA RVVFADMNRL LVVTSNAHAV NTLAFGSFVI KSIKSNPLFT YLDVSIREYW
     DYLMWLDNAN YCGRVCKPSL SETPELSHVS DWNIAHYLPK ILEQEFQEWI FQLMQHVGEA
     KDLFHKDETR ATQIAGTVKE NAEESFTTGI LKALEAPLVN RMKHLNRRYI DGRAIADVSK
     EFEFPKLAGS VANLKNPILE LIKYICAVYG LGSSNEPEYL QLRRKLLEVV RVGEFDPDAQ
     FRNPSADLVL NGIVCHNCGY TESINICRPE LEHEFGWSCS LCRASLDRVF LEEKLVELVV
     KAVCLYQIQD LKCSKCSRIR ADDMAYYCEC SGAFVGTIPI STLRKDLAVY NHVSEFFDLK
     LLQSVLSGLN
//

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