ID A0A165RCQ0_9APHY Unreviewed; 2225 AA.
AC A0A165RCQ0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN ORFNames=DAEQUDRAFT_688848 {ECO:0000313|EMBL:KZT70582.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT70582.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT70582.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT70582.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV429050; KZT70582.1; -; Genomic_DNA.
DR STRING; 1314783.A0A165RCQ0; -.
DR OrthoDB; 5475218at2759; -.
DR Proteomes; UP000076727; 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:UP000076727};
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 1518..1908
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1249..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2225 AA; 254614 MW; ADB6850A6CA99865 CRC64;
MARGSFSGAR TRGRGTSRFG NRGTAHFRGG RGRGRGRGGA PSEPRPQREE DGTQLAERFE
QVELNDEVDE KLGFPRVSEG PRREGWLINM HPTLVKDADW PSGKAAVDYY FIQDDGGMFK
CTLQYEPYFY IACKGGMETI IEEWLMKRYE AHICRITRER KEDLQLPNHL MGHRRLYLQL
HFRNVSDLLA VRRDIMPLAL ANSAKLDAVD AYAEVVNSTA SATTSIEIEG EWDAEAGPSR
GKTGRDKDPR EGIIDIREFD VPYYLRVAMD NEIRVGLWYA VTFTAGQPVF AQIAERVKRA
DPVIMAFDIE TTKAPLKFPD QQMDQVMMIS YMIDGQGFLI TNREIVSEDI EDFEYTPKEG
YEGPFTVFNE PDEAATIQRF FSHVQDVKPT VVATFNGDFF DFPFLCARAK VHGVDMFLET
GFAKDSEDEF KSRGCVHMDC FRWVKRDSYL PQGSQGLKAV TTAKLGYDPI ELDPELMTPY
AMEQPQTLAQ YSVSDAVATY YLYMKYVHPF IFSLCNIIPL CPDEVLRKGS GTLCETLLMV
EAFRGQIIMP NRHEEEHGNM YEGHLLASET YVGGHVEALE AGVFRSDIPS HFKVEPSAAQ
KLIDELDAAL TFHVVEESKL SLEEVTNYDE VKGQIQAALE EMRDNPMRMD KPLIYHLDVA
AMYPNIMLSN RLQPDSVVDE AVCAVCDFNR PGKTCDRRMT WAWRGEFFPA RRDEFNMIKH
ALNQETFPPK KPGGPQRKFI DLLPSEQTAL LHKRLGDYSR KVYKKIKDTR VENREAIICQ
RENPFYIDTV RRFRDRRYEY KGLHKTWKKN LDNVLTEQRS IAEVDEAKKM IVLYDSLQLA
HKCILNSFYG YVMRKGARWH SMEMAGITCL TGATIIQMAR QLVEQIGRPL ELDTDGIWCM
LPGVFPENFN FKLANGKTLG ISYPCTMLNH LVHAQFTNHQ YHDLHPETGE YKVHSENSIF
FELDGPYKAM ILPSSKEEDK LLKKRYAVFN DDGSLAELKG FEIKRRGELQ LIKIFQSQIF
ERFLLGETTE ECYAAVAQVA DRWLDVLFSK AENLPDEELV ELIAENRSMS KTLAEYAGQK
STSISTAKRL AEFLGDQMVK DKGLACKFII SARPQGAPVT DRAVPIAIFS AEESVKQTYL
RKWLKDNSLT NFDIRSILDW EYYIERLGSV IQKLITIPAA MQKVANPVPR IKHPDWLHRR
VVAMDDKFHQ HKVTDFFRTK TDGVATSHDI EDVDMQAATN GRARFAVVTR KPPPREDTPE
PTEETLDLPH PSVDYRGFVT RLGVAWRRRA RGETTASVPK MFKSIHPKTR TNSRWDIIQI
RPTRIPGRFA MWLSVGGELF SIPLRIPREF YIHLRTPAKA DQFNRDVYTC DKVIRGLPRD
RPCVNLYKIS VREDTYVDGQ EHFIDLTNDP NVDGVFEMQL PLDIRALLRL GKTCMTNVLG
MTLNRAEAVG FDLAELNRVI TTSTKHKYLN EGRDGKYIFL YHACSSSAPV HVFALFSPGA
DVRLHIVDPA TRRQPIPRLT EVYRDQFSKR QQTIGGNISY SYPVSCQFSS TYHGTDAAAL
KAISRELGLT ENLSYTVVIS SSKEQAYFDA YVPKLSKFPV LSMPKTKIAH TLDVFPWQTN
VAQKMVNRYL ALGTWLDRTV ALADYYDVPI GHIDGDQPLL LADVDFARRL MEHDFVLWWS
PGNCPDLGGS EEDARPTEEL PKTEFISPGC YSNVCLEITV RNLAVNSVLH SLMVNELEGA
GGATAFDSSR TLDEYSADTQ RDLTLGDSSV SPQMFSILRN MVKTWLLDKI QGNFESPATI
AIDHFWRWIS SKASCMYDPS LHRFIHGLMR KTFIQMLAEF KRLGSHVVYA DLSKILLVTS
KPPGTAHAYA TYITTAVTSH ELFQHVYLRT ERFYDFLLFM DQANLGGVVC EDPLAIELPE
EICIEMRWNI ETFLPAAIQR DFRNVVRFFL VELFRTCEKT RGTNRAPLRV LPNGAPDATQ
RDVTKTQEVE ASREFISRKL TRKLLKAVGS IQDRHREAMM DEEALPHWEF PVLPGSHLQM
TNPILEFVKF ACAVFALAKE YQIELDLLKR NLLELVNVRE FSGEATFHNP CEPLILSNVP
CRHCDALRDF DFCRDPELLP NNREVNARWL CSNCGGEYDR TMIEFAMMDM VWDLERRFAQ
QDLRCTKCKR IRSDNLSRHC ACSGSYQLTM NMTDVRRKLR TIFNVSIAHN FNRLKECSQT
ILSYW
//
