ID W9ZGT9_9EURO Unreviewed; 2236 AA.
AC W9ZGT9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN ORFNames=A1O1_02122 {ECO:0000313|EMBL:EXJ93729.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ93729.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ93729.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ93729.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) 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:EXJ93729.1}.
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DR EMBL; AMWN01000002; EXJ93729.1; -; Genomic_DNA.
DR RefSeq; XP_007721223.1; XM_007723033.1.
DR STRING; 1182541.W9ZGT9; -.
DR GeneID; 19157022; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_0_1_1; -.
DR OrthoDB; 5475218at2759; -.
DR Proteomes; UP000019484; 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:UP000019484};
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 1516..1908
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2236 AA; 254450 MW; E01B84E0E1BE9044 CRC64;
MPVRKPSRYG SNVRFSKDSS RRPRTKTVDA SSLRATEGTS QDEKIQATRL ANSIDEAMGF
PRYDAGRKRV GWLYNMHSTT IEDSKVPGGR AGVDFYFIGD NGENFKATVE YDPYFLLAVK
RGREAEVEEW CKRMFEGLVK SVSRVSKEDL QMPNHLLGYK RTFLKLTFAN VSDLLSVRRT
IMPIAEKNKE KVNAMDTYAE VASANAGFDI YDEENAGNTR SSGVADASDF ILDIREYDVP
YHVRVAIDKD IRVGKWYTVE AKHGSVSLTC LEERLQRADP VVLAFDIETT KLPLKFPDSV
IDQVMMISYM IDGQGVLITN REIVSEDIAD FDYTPKAEYE GPFIIFNEPN ERAVLERFFA
HIKEARPNVI ATYNGDFFDW PFVEARASVL GIDMYAEIGF RKNGEDIYQS DYCVHMDCFA
WVNRDSYLPQ GSRGLKAVTV AKLGYDPDEL DPELMTPYAS EHPQILAEYS VSDAVATYYL
YMKYVHPFIF SLCTIIPLSP DETLRKGTGT LCEMLLMVQA YQKNIVLPNK HSEPREAFWE
GHLLDSETYV GGHVESIEAG VFRADIPVNF AIDPTAIDEL LRDLDAALKF CITVEEKKSL
DDVMNYEEVR AQISEKLVSL KETPNRNERP LIYHLDVASM YPNIMTTNRL QPDSMKAEAD
CAACDFNRPG KTCDRRLPWA WRGEFLPTKR DEYNMIRRAV ANETFPGKFA KSARRTFQEL
SLDEQAATVR KRLQEYSKKI YHKIHDSKTI EREAIICQRE NPFYVDTVRD FRDRRYDFKG
QQKVWKGKTE ALKSANATAQ EIEEAKKMIV LYDSLQLAHK VILNSFYGYV MRKGSRWYSM
EMAGVTCLTG AHIIQMAREL VERIGRPLEL DTDGIWCMLP ATFPENVVFS LKNGKKMAIS
YPCVMLNHLV HGRFTNHQYQ TLVDPVTFKY ETTSDNSIFF EVDGPYKAMI LPTSKEEDKN
LKKRYAVFNH DGSLAELKGF EVKRRGELKL IKIFQTQIFK FFLEGTTLAE TYGAVARVAN
RWLDVLHQHG STLADEELID LICENKSMTK TLEEYGAQKS TSITTAKRLA EFLGDQMTKD
KGLNCKYIIS ARPRNTPVTD RAIPVAIFSA EEGVKRYFLR KWLKEDPADM DPRTVIDWDY
YLERLGSVIQ KLITIPAALQ KIRNPVPRVA HPEWLQKRIN VKDDKFKQKK VTDLFEKKPL
AERSVNLLDH RLAASGDIED ALNSSLEPTM QLNKPAKRKA DEAAHLSLVD PFATLPPNPP
AIDEDYSGWL DYQKQKWKIQ KQARARRRQL FGERPNAATD SISSFFRNQA ELLYINTWHV
LQLRQGDSPG EVTAFVAIGK KIHALKIKVP RTLYLNLKGD ELPNVEVPGC EVEKVNHTLP
NGHPSVHLFQ LTMAEDVYLR ESESISLLCN HPSVEGVYER QLPLFMRALL KLGNMCSFDE
EQKGVLGKGL ENGFDLSALL RNPSQSTYLE EPSSFAYVYV YHVAAGDRNV FALFSTARSD
AHIVVLSRSR DAQLPNADKI YAEQYRQKSP ENALVDEIFQ YQSNLTFKVS QVTTKRKANL
EIADVLKQWR SDESKPTVLL LQTTSHKQLV HDIRIMKDYP VLSLPTEQAD ADLPSLGWQG
YAFKQLISHY FNVAGWLTHL IELARYGEVP LCNLEKDDPR FLIDLAYARR LKRANVVLWW
SEQPRPDHAG YERDDILGPL TEVVEMPAIN NPGAYTSVCV DVTVQNLTIN TILTSSIIND
LEGSAESVAF NPAGEEDPIA NASMVKSNGG FAQAALEVLR EMVKAWWAEA CRGNRLADVM
VSHLVRWVEA PASCLYDRHL HYYVQMMSKK ALQQLITDFR RVGSQVVFAS STRLLLQTSK
QEVENAYAYS QYILKSIQQK PLFHFLGLEV KDYWDVLLWY DAYNYGGKGT STITEGTSNA
DLETIVHWQL SQFLPVPLQS VFDDWVISFI DLLHSLKRPA NTSSATPRAT QVPSGFLSLT
EDPTSTEVTT VLQDDFSKPL KKQITALIRR QREEMLHPEL ASDWSFPSLP GGTLEATDTR
HSRDPVLELV KGLMQIISLS KPLQLEARLL RKELLALFDV REFGREARFE NPSASLRFEN
LVCDTCTMTR DLDLCRDEDV LPDPESGPED AANKPWRCPA CQSEYNKIAL EENLIARVQA
SLLSWQMQDL KCKKCGTLQG DDSLFHDHCT CGGEWTGTMD RGDIRSNMRV MERVSSAYGL
RMLSGVLEGV KTMCMT
//
