ID H1VNL9_COLHI Unreviewed; 1080 AA.
AC H1VNL9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN ORFNames=CH063_11984 {ECO:0000313|EMBL:CCF41823.1};
OS Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF41823.1, ECO:0000313|Proteomes:UP000007174};
RN [1] {ECO:0000313|Proteomes:UP000007174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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|RuleBase:RU365029};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365029}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|RuleBase:RU365029}.
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DR EMBL; CACQ02004959; CCF41823.1; -; Genomic_DNA.
DR AlphaFoldDB; H1VNL9; -.
DR STRING; 759273.H1VNL9; -.
DR EnsemblFungi; CCF41823; CCF41823; CH063_11984.
DR VEuPathDB; FungiDB:CH63R_01400; -.
DR eggNOG; KOG1798; Eukaryota.
DR HOGENOM; CLU_000556_2_0_1; -.
DR Proteomes; UP000007174; 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: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 InterPro; IPR013697; DNA_pol_e_suA_C.
DR InterPro; IPR029703; POL2.
DR PANTHER; PTHR10670:SF0; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT 1; 1.
DR PANTHER; PTHR10670; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR Pfam; PF08490; DUF1744; 1.
DR SMART; SM01159; DUF1744; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {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|RuleBase:RU365029};
KW Iron {ECO:0000256|RuleBase:RU365029};
KW Iron-sulfur {ECO:0000256|RuleBase:RU365029};
KW Metal-binding {ECO:0000256|RuleBase:RU365029};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU365029};
KW Nucleus {ECO:0000256|RuleBase:RU365029};
KW Transferase {ECO:0000256|RuleBase:RU365029};
KW Zinc {ECO:0000256|RuleBase:RU365029};
KW Zinc-finger {ECO:0000256|RuleBase:RU365029}.
FT DOMAIN 371..762
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 78..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCF41823.1"
SQ SEQUENCE 1080 AA; 122624 MW; E1E4DA124EE57A48 CRC64;
KLITIPAALQ KVRNPVPRVA HPDWLQRRIN IKDDKMKQKK LTDLFAKGPL EDITNPTVIS
AADMEDFGSQ LLKPKPVTSV VASSQPAAPT SQKRKSPGPA ENADPFAALP KEMPSPSDDY
VGFLQYQKQK WKIQKQARIR RRQLFGDRRG NNQNNIQNTF MKQAHMTFMN TWQLLHLKPT
ETPGIVNAHV LIDAKIHSLK IKVPRQVFLN LKSGEMPDVD IPGCEVEQVN HTLPNGHSSV
HLFKLTVPED VYFAEADKFS LLFNHPSVEG VYEKHLPLNI RAVLQLGNQC AIDERQHAVL
GKGLEQGFDL LGLKRPLKPR TYLETSPLAY IYMSHVTAGD RQIFGVFSTL KDEAHVIILQ
KGRDSGQDLP NISRIYTELL ARRGEEAAGT NWQDCFTYQE KLNFKITQVT TRRKAHLELS
DVVKKMRKDE LRPLMMVIQS SQRNMLINDV PILGEFPVLP LKYDPADSSL PPLGWQAVVA
RRLVGHYLGL GSWIVHLNTL ARYGEVPLCN LEREDPRFLI DIAYARRLQN NNVVLWWSAG
PRPDHAGHEK DDITGPLETV QMPATNNPGT FSSVCIDLEV RNLAINTILT SSLINDLEGS
ESISFNPAGD GNAAGDEVIS SEGTFANAGV LVLREMVKSW WQEACKGSAM ADVMVQHLVR
WVENPDSFLY DRALHYYVQM MSRKAFQQLM ADFRRVGSQV IFANSNRLLL QTTKAEVGTA
FAYSQYIIKS IKSKPLFHFI DLEIKEYWDY LVWYDEFNYG GKACQEVVEA EQQTLDTVMH
WQMATFLPIR LQPTFQDWVI EFIQLMHNLK RPLNGDPSST PRLTQLPQKS LAEGAEGQII
LGKAFEKPLK KDIANLINLQ KRELLHPELA EDYSFPHLPG SHLTHLSSRN AVLELVKALM
QVLSLDKNIT LEARLLRKEL LAMFDVREFS KEGAFQNPSE SLKVIQLSCD SCTMARDLDF
CRDEDLLPEM GPDGKRLSPE TRPWRCTFCE AEYDRNAIEE MLLARVEAFV VEWTTQDLKC
GKCGALRMNE LMDHCTCSGE WVESVRRADI VRRLGVFWNV AKFYGLKMLL EVTEGLRKGL
//
