UniProt: B2ALD8

Database: UniProt
Entry: B2ALD8_PODAN

LinkDB:  B2ALD8_PODAN 
Original site:  B2ALD8_PODAN

All links

Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   SMART (2)   
Literature (2)   
   PubMed (2)   
All databases (32)   

Download RDF

ID   B2ALD8_PODAN            Unreviewed;      2253 AA.
AC   B2ALD8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN   ORFNames=PODANS_5_3400 {ECO:0000313|EMBL:CAP64785.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP64785.1};
RN   [1] {ECO:0000313|EMBL:CAP64785.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC   {ECO:0000313|EMBL:CAP64785.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP64785.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP64785.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP29294.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Submitted (APR-2015) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU633866; CAP64785.1; -; Genomic_DNA.
DR   EMBL; FO904940; CDP29294.1; -; Genomic_DNA.
DR   RefSeq; XP_001904878.1; XM_001904843.1.
DR   STRING; 515849.B2ALD8; -.
DR   GeneID; 6189093; -.
DR   KEGG; pan:PODANSg1900; -.
DR   VEuPathDB; FungiDB:PODANS_5_3400; -.
DR   eggNOG; KOG1798; Eukaryota.
DR   HOGENOM; CLU_000556_0_1_1; -.
DR   OrthoDB; 5475218at2759; -.
DR   Proteomes; UP000001197; Chromosome 5.
DR   GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
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:UP000001197};
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..1913
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1242..1265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1244..1260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2253 AA;  256997 MW;  EA6755A97D57C389 CRC64;
     MPNTSLRQPR GGYRRGGKQA YHGPKTKTFA ASSSTRGEAT SMDEKWERTA LAHQIDENMG
     FARYDAGRKR EGWLVNVQAT SIDDPRIPGG GGRAALDCYF IEEDGQTFKA TVDFEPYFLI
     ACRKGHEGEV EEWCKRVPGG GVVKSIKKIE KEDLSMPNHL LGYRRTFLEI KFHNVQDLMA
     ARRDIMPIAE KNKKGMDAMD TYAEVATTNG NFDLFDDDLR RDDQRHKTSF SEASDFIVDI
     REYDVPYHVR VMIDLDIRVG NWYFVEAKNG VTTVIRNEDR LAPADPVVMA YDIETCKAPL
     KFPDAAVDQI MMISYMIDGQ GFLITNREVV SEDIADFDYT PRPEYPGPFM IFNEPDEKSV
     LERFFLHIKE ARPTVIATYN GDFFDWPFVE ARASINGIDL YHEIGWKRDS DDQFKCNYSV
     HMDCFHWVNR DSYLPQGSRG LKAVTVAKLG YDPDELDPEL MTPYAQERPQ TLAEYSVSDA
     VATYYLYMKY VHPFIFSLCT ILPLGPDDTL RKGTGTLCEM LLMVQAYQKG IVLPNKHVQA
     KESFWEGHLL ESETYVGGHV ESIEAGVFRA DIPVTFSVDT GAVDELLRDL DAALKFSITV
     EEKKSMDDIT NYDEVKEQIV AKLMNLKETP NRLENPLIYH LDVASMYPNI MTTNRLQPDS
     MISESDCAAC DFNRPGKTCD RRLPWAWRGE YLPAKRDEYN MIRHALESER FPGKRPNMPT
     RSFGELPADE QASLIRKRLQ LYSQKVYHKI HDSTTIVREA IICQRENPFY IDTVRDFRDR
     RYDYKGKAKV WKGKTDALRS SGASASEVDH AKKMIVLFDS LQLAHKVILN SFYGYVMRKG
     SRWYSMEMAG VTCLTGATII QLARSLVERL GRPLELDTDG IWCMLPATFP ENFTFKLKNG
     KKMTISYPCV MLNHLVHDKF TNHQYQTLVD PKTFKYETHS DNSIFFEVDG PYKAMVLPTS
     KEEDKNLKKR YAVFNDDGSL AELKGFEVKR RGELKLIKIF QQQIFKFFLD GTTLAECYTA
     VAKVANRWLD VLDSKGTTLA DEELMELISE NRSMTKTLEE YGSQKSTSIT TAKRLADFLG
     EAMVKDKGLN CKFIICARPK GAPVTERAVP VAIFSAEEET KRMYLKKWLK EEPADTDPRA
     LLDWEYYRER LGSVIQKLIT IPAALQKVRN PVPRIPHPDW LQRRINIKDD KMKQKKLTDL
     FGPTTKRPLN DITNQLGDLE DIGDLLKPKT VTSAIAASQK VLASHKRKSP EPEEDPFAAL
     PKKMPDPSED YPAFLEYQKQ KWKLQKQARA RRRHLFGERR GNAQNSLQQT FRNQAEVTFR
     NTWQVLQLKA TDMPGIVIAY VLIDNKIHTV KINVQRQVFL NLKSKELPDI EIDGCQVEQV
     NHTLPNGHSS VHLFKLTVPE EIYFAEAEKF SLLFNHPSVE GVYEKQIPLN LRALLQLGNL
     CTIDTSQAGV LGKGLEQGFD LDGLKKPTKP KPYLEGARMS YVYLSHISAG DRQIFGLFST
     TGDQAHVIIQ QKSKDGGQDL PNISKLYSDL LARRISEEGE DSTWQERFQY QEKLSVKITQ
     VTTRRKAFLE IGDIVKKMKK EESCPMMMVI QSSQRNLLVH DIPILGEFPV MPLKYDTADS
     SLPPLGWQTV VARRLVNHYL SLGSWITHLT ALAKYGDVPL CNLERDDPRF LIDVAYARRL
     QANSVVLWWS PSPRPDHAGY EKDDVVGPLD QVQMPSVNTP GTYASVCIDI EVRNLGINTI
     LTSSLINELE GADSISFNPA GDGGGGEESF QSENAFANAG VQVLREMVKS WWAEACKGST
     MADIMVQHLI RWVESPASCL YDRALHYYVQ MMSRKALLQL MADFRRVGSH VVYASANRLL
     LQTTKSEVGN AYAYSQYILK SIKAKPLFHF IDLEIKEYWD YLVWYDEFNY GGKACQEVLE
     KDEQDLQMIM HWQIATFLPV RLQPVFRDWV VEFIELMHGI KRPANGSDPT ATPRMTQLPF
     RGDSTQQADD KVPTGANQII LGKNFEKPLK KEILGLIQAQ KREMLHPELA NDYSFPVLPG
     SYLPQLLPSS ASTGPAHKKS ASAKPTANPI LELVKALMQV LSLDKNITLE ARLLRKELLA
     LFDVREFSKE GQFLNPSESL KITQLSCENC TMTRDLDLCR DEDLMPLPDE EPQAKRWACQ
     YCEAEYDRNA IEERLVGEVE GIVVEWTCQD LKCGKCGAAR VNEFMEHCTC SGEWRESVKR
     EEVMRRLRVY KRVAGFYGLR MLQDVVGEIW EGL
//

DBGET integrated database retrieval system