ID A0A427XQ36_9TREE Unreviewed; 2193 AA.
AC A0A427XQ36;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN Name=POL2 {ECO:0000313|EMBL:RSH80933.1};
GN ORFNames=EHS24_008362 {ECO:0000313|EMBL:RSH80933.1};
OS Apiotrichum porosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Apiotrichum.
OX NCBI_TaxID=105984 {ECO:0000313|EMBL:RSH80933.1, ECO:0000313|Proteomes:UP000279236};
RN [1] {ECO:0000313|EMBL:RSH80933.1, ECO:0000313|Proteomes:UP000279236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27194 {ECO:0000313|EMBL:RSH80933.1,
RC ECO:0000313|Proteomes:UP000279236};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Apiotrichum porosum DSM 27194.";
RL Submitted (NOV-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:RSH80933.1}.
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DR EMBL; RSCE01000007; RSH80933.1; -; Genomic_DNA.
DR STRING; 105984.A0A427XQ36; -.
DR OrthoDB; 5475218at2759; -.
DR Proteomes; UP000279236; 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; 3.30.420.10; 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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR013697; DNA_pol_e_suA_C.
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; 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|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|RuleBase:RU365029};
KW Nucleus {ECO:0000256|RuleBase:RU365029};
KW Reference proteome {ECO:0000313|Proteomes:UP000279236};
KW Transferase {ECO:0000256|RuleBase:RU365029};
KW Zinc {ECO:0000256|RuleBase:RU365029};
KW Zinc-finger {ECO:0000256|RuleBase:RU365029}.
FT DOMAIN 1468..1859
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2193 AA; 248344 MW; 26ACF0ECCDCF96E6 CRC64;
MSFRGRGRGR GGGSKGNTRF TGKRAAFRPG GGGNRPAPNR DDDGTALQER FEETKVADEI
DDKLGFWRFE SNLANGDSRD GWLVNMHQAL VQSDIHASGL AAVDYYFIQD DGGMFKATIP
YQPYFYVTCR GGTETIVEEW LIKRFEGVVV RVQREKKWDL SVPNHLLSAP PVFLKIFFHN
TQDFQNVKRE LLPLAVANSA KFTAVDAYAD VVGAENATNA ANGDGQERAW GEDEDTQKRK
SEREPADCII DIREHDIAYY LRVAIDLDLR VGLWYNVSST MGTIKMERLT DRVKRAEPVV
MAYDIETTKQ PLKFPDQQTD QIMMISYMID GQGYLITNRE IVGEDIEDFE YTPKPEYEGE
FTIFNEPDEA ALIRRWFEHI QDSKPTVMAT YNGDSFDFPF VDARAKIHGI SMYNEIGFRP
DNEGEYKCRA CMHMDCFRWV KRDSYLPQGS QGLKAVTKYK LGYNPIDLDP ELMTPYAIEQ
PQKLASYSVS DAVATYYLYM KYVNPFIFSL CNIIPLNPDE VLRKGSGTLC ETLLMVEAYQ
AHIIMPNRHE DPHGVTYEGH LLASETYVGG HVEALEAGVF RSDIPTHFKV APSAMQELLD
DLHNALKFSL VEEGNVKLED VENYDEVYDE IAKALILMRD EPNRVDPPLI YHLDVAAMYP
NIMLSNRLQP DSVKDEAACA VCDYNRPDKV CDRRLEWAWR GEYFPAKRDE VNMVRYALDQ
ELFPPKYPND PKRRFTDLPQ AEQSALIHKR LGDYSRKVYK KTHETKVVTK TAIICQRENS
FYIDTVRAFR DRRYEYKGLH KTWKKNLDKA FDEGGALPRG RRGQEDDCAM ARQLVEQIGR
PLELDTDGIW CMLPGVFPEN FTFKLKGGKK FGISYPCSML NHLVHEKFTN HQYHELVDPE
AGVYNVRKEN SIFFELDGPY KAMILPSSKE EDKLLKKRYA VFNFDGSLAE LKGFEVKRRG
ELQLIKIFQS QIFDKFLLGS TTEECYAAVA EVADQWLDIL QSKGSSLDDN ELVELIAENR
SMSKTLAEYG SQKSTSISTA RRLAEFLGEQ MVKDKGLSCR FIISERPHGA PVTERAIPVA
IFDADPTVKR HFLRKWVKDA SLIDFDIRTI LDWSYYTERL GSVIQKLITI PAALQKVANP
VPRIRHPDWL FRRVATREDK FQQHTLTDMF AKMRTKAADM EDFGTNKTAN KPRMAVVNRR
KKAKSPEIEE IAPDPEVDYP GYIRVMRKVW RKNRLEKQRL RKQGIRQDFS ISSMIRTQTA
NLAARQWDII QIAATTRPGE FLLWLAIDTT FQSVRLRVPR EFYLNFKSMP GDDTFSSRYD
VASVTRVLPR GQATRHLYRV QVEEGLFVDG ESHFSSLINN PNIDGAFELQ VPLMVRALLA
LGTACGLKST SLSGLNRGLD KGFDLAELER PGASVLRHRY LNDGKNLKYH FLFHATVNSR
HLIGLFSPTG PAKVYVVDGA RNRQQLPNPA RWYAERVAKA APGIFTYPEE LECATSYYPT
EAGAMRQLIK DLQAIRTGMN VIALCSPFEH AHYQARHAVF SEFPFVTIRT IKDEEPSLMW
LVTMARRMVV QYLRLSAWIA GQIEIAAHYD VPMGNLGPDP PTFLADLEFA RRLKDQDMVL
WWSQSPRPDL GGAEEDANGS DEPVAPQIST RGCYSSVVLE MELADMAINA VLQSALVNEM
EGSGTGAHAF GTASHNLDEY AQGTANASVM LGDAVLSIQT FTVLKSMVRS WFLDKSRAHV
RGIEGGPADL VIDQFWRWIS SNSSCMFEPA LYRFLHGLMR KTLLQLLAEF KRLGTQVVYA
DLNRVFLLTS KPDAGSAFAF AKYLVTAANS HDLFRHIVID VTLFWNYLAW MDVANFGGVR
IFPDEAGTGL PAPKQFEISM DWNIQAFLPA ELQPMFERRV ADYIYALYTA KRNATDGRGP
LKPVYNLNIE APGEAAPAQT NPAKVKEQAA AAKAVSTTLT RKLLDDTSKI KRRHATAQAN
GDDTALAFPR LPGAVAANQK TENAALAFVK DVCEVYSLST DLLIDVQVLR RNLLDLVGVR
EFAPEAAFRN PGESLTVPMV SCGRCNAIRD VDLGRDPDCL PSVNQAGEAQ APPRDMWACH
KCDAEYDRFA IEHPLIDMVS RIVTSWQTQD VICQKCSQSK SDNLAPTCHC GGAFRPSLNR
SELTNKLKMI QSVSQYHKLT MTGEYVADVL TRW
//
