UniProt: A0A139A7K7

Database: UniProt
Entry: A0A139A7K7_GONPJ

LinkDB:  A0A139A7K7_GONPJ 
Original site:  A0A139A7K7_GONPJ

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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)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   A0A139A7K7_GONPJ        Unreviewed;      2296 AA.
AC   A0A139A7K7;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN   ORFNames=M427DRAFT_125636 {ECO:0000313|EMBL:KXS12658.1};
OS   Gonapodya prolifera (strain JEL478) (Monoblepharis prolifera).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Monoblepharidomycetes; Monoblepharidales;
OC   Gonapodyaceae; Gonapodya.
OX   NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS12658.1, ECO:0000313|Proteomes:UP000070544};
RN   [1] {ECO:0000313|EMBL:KXS12658.1, ECO:0000313|Proteomes:UP000070544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEL478 {ECO:0000313|EMBL:KXS12658.1,
RC   ECO:0000313|Proteomes:UP000070544};
RX   PubMed=25977457; DOI=10.1093/gbe/evv090;
RA   Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA   Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA   Spatafora J.W., Berbee M.L.;
RT   "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT   Walls of Algal Ancestors of Land Plants.";
RL   Genome Biol. Evol. 7:1590-1601(2015).
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; KQ965786; KXS12658.1; -; Genomic_DNA.
DR   STRING; 1344416.A0A139A7K7; -.
DR   OMA; MLDQCRY; -.
DR   OrthoDB; 5475218at2759; -.
DR   Proteomes; UP000070544; 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:UP000070544};
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          1562..1973
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2296 AA;  260592 MW;  4941C440797090C8 CRC64;
     MFGIPPGRGA KGKARGDRWE NAENIAPRSV GRGSSGHRGQ LRNVPTSRFG SRPTGPASRD
     DLEDFGADLD ADTAFDGFKE LKDASSTVTG FTSPNDELQD LLFVDEIDEK MGFWRYEEGP
     ERIGWLVNMR PTLVRNSDWP GGKSAVDLYF LEDDGGRFKV TLQYEPYFLV CPKEGCAAEV
     EEHLRRLFDR QVHQIQRIEK EDLDLPNHLI GAKRTVVKLA FRNVRDLLSV RKVLLQTVQA
     NREGKQAAEV YENNWNIVGY EDELQQSKGL KDPLDLIDDI REYDVPYYIR VAIDNGFRVG
     HWFAVTADAT SHSVTLSRRS DLLHRAEPVV LAFDIETTKQ PLKFPDQQLD AIMMISYMVD
     GQGYLITNRE VVSEDVEDFE YTPKPEYEGP FTVFNESDEA SVLRRFFAHI LSARPSIIAT
     YNGDFFDFPF VEARARACGM DMYKEIGWKK DSSPGGGDIY QSSYGIHMDC FAWVKRDSYL
     PQGSQGLKAV TSAKLGYNPL ELDPEDMTRF AIERPQTLAQ YSVSDAVATY YLFMKYVNPF
     VFSLCTVIPG CADDVLRKGS GTMCEMLLMV QAFENNILMP NKYVEKRGKT FEGHLVFSET
     YVGGHVEALE AGVFRSDLPT KFRIVPEAVQ GLLDQLDGAL KHTIEVEGKS KVQDVENYDE
     VRSAIASRLL DLRDRPLRSE RPLIYHLDVA AMYPNIMLTN RLQPDSMVDE RTCATCDFNC
     PESDCQREMT WSRRAEFFPA KRNEVNMLRS VLENEKFKAS GRFPSDPSRN WNELSHSEQT
     KALEKRVGDY SVKVYNKKYE NKIVPSKAIV CQRENPFYVD TVRLFRDRRY EYKAQHKQWK
     KKLDDALHNG IASEIDRCKK MVVLYDSLQL AHKCILNSFY GYVMRKGSRW FSMEMAGIVC
     LTGAKIIQMA RQLVERVGRP LELDTDGIWC ILPQTFPENY TFKFKGGKTL PVSYPCAMLN
     HLVHEKFTNH QYQDLDDAET YRYKKHSENS IFFEVDGPYK AMILPASTEE DKLLKKRYAV
     FNEDGSLAEL KGFEVKRRGE LKIIKIFQSE IFKVFLKGDT LETCYGAVAE IANRWLDILY
     SKGADLEDDE LIELISENRS MSKSLEEYGA QKSTSISTAK RLAEFLGDQM VKDKGLNCKF
     IISSKPSGVP VSERSIPVAI FQAESSVKKY HLRAWLKDPA LSNFDIRNIV DWNYYLERFG
     SVIQKLITIP AAMQKVSNPV PRVKHPDWLG KRVAEREETF KQIRITNYIP KSANALMTQP
     DLISPREKAV ILSDEPLSVH SFGGGASMGR SYGAWLIIQK QKWRAQILEQ DILRKQHGPN
     LQNMHGRRDG RSKGTIFGSG NIGGMTSFLR KQADSLVNHS WEVLQIAEGD TPGEFRIWAL
     VNRNLHSLKL HVPRVFYVNS KTPNTFTQLS ATSGVVIRQC VRTLPRSHKC HYLYEMQMTE
     QTFRDNTEAI SSFTSHPNIE GVYELNVPLM YRALISLGAS IGVTPSKRNK IWKSGIEGGF
     ELGDLVPTQS NLGQYLENAA GRLNFIFLYH SSSDSRHLVG LFSTAVNRSH VFVVDRSNQL
     PNLSKAYSDL MTAQANIQHS SSSQLRTGNA KGQQSIFSYH NSLDFQVAIC GSEGEAWKAI
     QRTLVQYNEE RHGPSLLLVQ SQRSIRYLSE RIINLNDFPI VTIPSHKSDN QFTALDWQRP
     AARQMVAHLL NVDEYLKDKI RLAKYIDAPI CNIDADFPIF SADLAFARRL QQQNMILWLS
     LSGQPDLGGR EADENQFVAM ELLNPEINNP GSYRNICVEL EVNQLAVNTL LRSSFINDIE
     GTSSTIGLDA NLHAMNGHLA RATSQLDTDI DDQAVSWQHF NIIKSLVTSW TADLFQTQCQ
     WSEMMVEHCL RWITSPSSKF YDPAMYSLIH GMMHKVFAQL VAEFRRLGAQ PVFASFTKLI
     LVTPKPAMTT AKTYVKYILK AITQHSLFDV LDINATQFWE HFLWMDYANY GGVNGFNNIG
     ESTKAPSIIM KWNIKEYLPP AVQPQFLKIV AELLHSLHLQ KVEWLNKNPL GIIPASRQKN
     LQTEEPSHQD NLNFDDVDEF KRRLIESVLG RQLLTMVKDI DRNISLSHAE TEDDQIAASF
     PRLPGSYLPM NNVALEFIKS VCAVLELDTF VHAEVRRLKK SLLTLIGISD FSEKAQFMNP
     CETIKLSRII CGYCNLCSDL DLCRDPDLLP DAKVGSAKLQ PWHCKGCGME YNKQDIEEEL
     VGTIGRRLLA WQLQDVTCQK CHSVRGDSLA AVCSQCGGGF ATARGAVDVA RRLQVLRGLA
     DLHGFQSLQE MLASVT
//

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