ID A0A3E2H024_SCYLI Unreviewed; 2233 AA.
AC A0A3E2H024;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
DE Flags: Fragment;
GN ORFNames=B7463_g9716 {ECO:0000313|EMBL:RFU26627.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU26627.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU26627.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU26627.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-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|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:RFU26627.1}.
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DR EMBL; NCSJ02000251; RFU26627.1; -; Genomic_DNA.
DR STRING; 5539.A0A3E2H024; -.
DR OMA; MLDQCRY; -.
DR Proteomes; UP000258309; 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:UP000258309};
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 1522..1916
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU26627.1"
FT NON_TER 2233
FT /evidence="ECO:0000313|EMBL:RFU26627.1"
SQ SEQUENCE 2233 AA; 255943 MW; 6020314E1DF37323 CRC64;
MAGTRRPQNG YRRGGKQAYY GPRKTKTFAA TGRSEATSAD ERRESNRLAH SIDEAMGFAR
YESGKKKVGW LVNIHTTSIE DEKIPDGRSA VDCYFIEEDG GTFKATVEYE PYFLVAVRRG
HEPEAEEWLK RSPGGGVVKH IRRIEKEDLK MPNHLLGYKR TFLELRFSNI NDLLAARRDI
MPIAEKNKKN MNAMDTYAEV ASANAGFDLF DDSRDDDRRL NTSVADASDF IVDIREWDVP
YHVRVMIDLD IRTGKWYTVE AKHGTTTVKC IEERLQIADP VVMAYDIETT KLPLKFPDAA
VDQVMMISYM IDGQGFLITN REIVSEDIDD FEYTPKPEFE GPFMIFNEPD EKACIERFFL
HIKEARPTVI ATYNGDFFDW PFMDARASVN GIDMYQEIGW RKNNADDQYM CDYSIHMDCF
HWVNRDSYLP QGSRGLKAVT TAKLGYDPDE LDPELMLPYA SEKPQTLAEY SVSDAVATYY
LYMKYVHPFI FSLCTIIPLG ADAVLRKGTG TLCEMLLMVQ AYQKNIVLPN KHVSPKESFW
DGHLLDSETY VGGHVESIEA GVFRSDIPVN FAVDPKAIDE LLGDLDAALK FSITVEEKKS
LDDVTNYDEI KQKITDQLNN LKATSNRSER PLIYHLDVAS MYPNIMTTNR LQPDSMIQES
DCAACDFNRP GKTCDRRMPW AWRGEYLPAK RDEYNMVRNA LENEKFPGKY PNGPLRTFQE
LSPDEQAALV RKRLQLFSQK IYHKIHDSTT IEREAIICQR ENPFYINTVR DFRDRRYDYK
GKQKVWKGKT EALKAAAAPA AEIENGKKMI VLFDSLQLAH KVILNSFYGY VMRKGSRWYS
MEMAGVTCLT GAHIIQMARQ LVERIGRPLE LDTDGIWCML PATFPENYAF TLKNGKKLTI
SYPCVMLNHL VHAKFTNHQY QTLVDPATFK YETHSDNSIF FEVDGPYRAM VLPTSKEEDK
NLKKRYAVFN HDGSLAELKG FELKRRGELK LIKIFQQQIF KFFLEGSTLA ETYASVAKVA
NQWLDVLYSK GTTLADEELI DLIAENRSMS KTLEEYGSQK STSITTAKRL ADFLGEQMVK
DKGLNCKYII CARPKNAPVT ERAVPVAIFS AEMSVKQHFL RKWLKEDPSD MDPRALLDWD
YYLERLGSVI QKLITIPAAL QKIRNPVPRI AHPEWLQRRI NVKDDKMKQK KMTDLFSKTP
LEDITNLQDP RVGDIEDFGT KLLKPKTVGS QIIASSQKSA QKRKSPEPAV PVSVNPYAAL
PEKMPSPTED YLGFLDYQKQ KWKIQKQARI RRRHLFGESR ANAQSNIGAT FRIQAEQVYR
NTWQVLDIRG TDSPGVVLAF VLIDSKIHTL KINVPRRVFL NLKSKELPDI EVDGCEAQKV
THTLPNGHPS VHLFKLTMSE EVYVNEAQKM SLLFNHPSVE GVYERQVPLN IRAVLQLGSL
CTFDETQPGV LGKGLEHGFD LSGLIRAESK QPYLSQSSLA YLYLYHVVAG DRQIFALFST
TREQAHVIIL QKTKGSEQDI PNISKIYNDL LTRRNQEPDG NSWQSCFKYQ QKLQFKIHQV
TTRRKALLEL SDMVKKVRNE ETKPLLLVIQ SPQRRLLVND APILGEFPIL PLRNDIDDTN
LPPLGWQSFA TKRLVNHYLS LSSWILHLTE LARYGDVPLC NLERDDPRFI IDIAYARRLQ
KNNVVLWWSA GPRPDHAGYE EDDVLGPLDT VQMPSVNNPG TYPSVCIELD VRNLAINTIL
TSSLINELEG SDSISFNPAA PSDEANGDPN NVLYADNAFA SAGVTVLREM VKAWWAEACK
GSNMADIMVQ HLVRWVESPE SFLYDRSLHY YVQIMSRKAF QQLMMDFRRV GSQVVFANAN
RLLLQTTKSE VGNAYAYSQY ILKSIKAKPL FHFLDLEIKE YWDYLVWYDE FNYGGKACQE
VVEAEQQTLD TIMHWQLSKF LPVSLHPIFN DWVVEFIEIM HKSKRPRVLT NGVDSTPRPT
QLPVRNLGDD KEDKIMLGKE FEKPLKRQIA GLIRRQKDEM LHPELAGDYR FPILPGSHLK
LENPILQLVK SLMQVLSLDK NITLEARLLR KELLAMFEVR EFSQEAYFQN PSESLKISQM
ICDNCTMARD LDLCRDEDLI PDLDPDGKPL DSSTRPWKCS FCDSEYKRLD IEERMIASVE
GIIVEWNTQD LKCSKCKTVR VNDFMEHCSC SGEWGGDVNR EDVVRRLKVY RNVARFYGLR
MLDDVTEGVF AGL
//