UniProt: A0A0N1PC60

Database: UniProt
Entry: A0A0N1PC60_LEPSE

LinkDB:  A0A0N1PC60_LEPSE 
Original site:  A0A0N1PC60_LEPSE

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (26)   

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ID   A0A0N1PC60_LEPSE        Unreviewed;      2311 AA.
AC   A0A0N1PC60;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN   ORFNames=ABL78_4444 {ECO:0000313|EMBL:KPI86504.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI86504.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI86504.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI86504.1,
RC   ECO:0000313|Proteomes:UP000038009};
RX   PubMed=26317207;
RA   Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA   Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA   Yurchenko V.;
RT   "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT   Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT   donovani.";
RL   PLoS Pathog. 11:E1005127-E1005127(2015).
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:KPI86504.1}.
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DR   EMBL; LJSK01000128; KPI86504.1; -; Genomic_DNA.
DR   EnsemblProtists; KPI86504; KPI86504; ABL78_4444.
DR   VEuPathDB; TriTrypDB:Lsey_0128_0180; -.
DR   OMA; KGLACHF; -.
DR   OrthoDB; 5475218at2759; -.
DR   Proteomes; UP000038009; 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   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          1650..2006
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
FT   REGION          693..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1237..1265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1285..1327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..732
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1247..1263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2311 AA;  261196 MW;  8E8936EAB93E5916 CRC64;
     MTTRLESGTK EGWLFNYHPT SETVQEEDGV RGEGAQRAAL VLLFQDLAGD TFYVHLHYNP
     YILVHAVEGH EREVELGLMS VFGPQLIHEI TPIEKEDLDL INHLSGKKRI YLKVIFRNVQ
     DLTTVRGRLE KEVKRNSSRA TDYSIQNLFS GSLSDAMAKT FEEDAADSAA NGGGRWMDWV
     QDIREYDVKY HMRVAIDMKV YVGLWYDVTV SEGEVTVQRC DDSRYAPAMP RVVAFDIETT
     KAPLRFPQPE VDQIYMISYM LDGRGYLIIN REIVTEDIAP FEYTPKPEYE GFFDTFNEED
     EAATLRRFFD EMKKYQPNVY VTYNGDYFDF PFIHARSLYH GMNMRKEIGF TQMADGAFLN
     QQIPHLDCFY WVKRDSYLPQ GSQGLKAVTK YKLGYEPIEV DPENMLPLAQ SHPQRMASYS
     VSDAVSTWYL YQKYVHPFIF SLATIIPMSP DDVLRKGSGG LCESLLMVQA EANNIVFPNK
     KELVRERFYE GHLIDMETYI GGRVEALRSG VYRSDIPLTF NMNPDTYQSL MDDVDSALRF
     CVEVENGVKV EEVTNFEEVK MGILEKLTAL RDRPHQQEKP FIYHLDVGAM YPNIILTNRL
     QPYAIARPDV CAGCCYNSPN NELQCKRVMS WKWRAELFTA GRHEFQRVKA QLENESFAAG
     VIEQANLAAV QKKAYGNRKG NVLEGTAYER KDDWKKNDRN NMDGGGRNNG GGGGYRQESR
     RQQREAADAL LRREFGADNN NNSNDSDEDD EDGPKAYHKL NDSTQFNMLK RRLSEYSRKA
     YGKIHETREV MRSNVVCQRE NSFYVDTVRL FRDRRYEYKA ALKTWKKKLD AAKDADERKV
     CQSRCVQMES LQLAHKCILN SFYGYVMRKG SRWSSMEMAG IVTYLGATLI QMARSLVQQI
     GVPLELDTDG IWCCLPNTFP ENYTIKTSNT SKPKIALSYP CVVLNKMVHD RYSNHQYQNL
     VSPGVYKTHS ECSIYFEVDG PYLAMLLPAS REEGKSIKKR YAVFNPDGSM AELKGFELKR
     RGELMLVKDF QAQVFRRFLD GSTLAEAYAS AAYVANTALD LLESKGEGYD PEEILEKITE
     SSNMTRRLSE YPETQKSLAI TTARRIAEFL GPQMVKDKGL ACHFIISRMP AGRPVTERAI
     PVTIFRADPA IRTHFLRKWT GDTTLPSELN LKALLDWDYY TTRFSACVQK IVSIPAALQS
     LPNPVPRVAH PDWLEKRIRH LNSRYRQVSL VGMLSKTKAR NEEQQEAAAS AEATATSENG
     LNDDAAMVAN GSSKCAANRG GLQDLEDLMN SGAGDSVKPR RPMQPKSNSS RGQKGENADS
     DWEDDDDGAI EVESEDDVER QQREEDAELD SLAHDVKQKY FMPKSTTVLD ADFFTDPGTK
     RWLSQRKSTW LQRARLRKEL ALENGLNDAP WDSDASGAAR VAAADAKTAD MTSGINSHFI
     DLKSRALAAM WSVMEVRETG EDPGVVQVIA ALEQNLYSFR VQVPRRVILD VDPALQLHGF
     EATELNGRVL PRHVTPGRVY QVTILPGEAG ERQLNELRMM EGVRQIYEQH RSLKDVFIEQ
     LGCCSSVDSD RHLRNARRRP PSQREIFGLE ELEMNSFSNY LSRGVSDRTV FVFHAVTEQQ
     RGLVAVVHPQ TSSALVIFIQ PAEAAKPAIN WTTICEESAQ RLRTSPPASM HVTTETAVDQ
     RAAWRLIYQH LSTALESARA PLVAVLQSSQ PTAVLLQQHA LPPNLPYLRV LGAAEDERLL
     SDPFRWARLL SRRLFERFFA SLLWVEERLA LSRISGIPLC NIAQDSCVHV LDVLYTRALH
     RRSHVLWCSS NPAIAFDTVE ERPREVCMAG GYLSWCVEFS LSRLDVVALL FSQVIEEGDD
     PNARALCDRG VSTQFNILRD LVADLLGQAV ENTLADTLMN NVARWLRDPV SACYEPRLVE
     LLSSLAHRAL TGVLLRLAKL GGRTVKVDGE SVTVLTAKQS IQEAVSFANF VTTSLQDQPM
     MMILALQPVR YWCPYMILDP RNCAGLYLTA ADALSLKVGE SPSRADLHLI QQFTMTSRLP
     SRVRAIFVDR VVDTLFQLLK TIQAVHEDTV KDHNVTLATR HDHFARRLLQ RSQALCEGNI
     QTTIMGEVQH VADTRDLYTE EEHAAKQKGA LTLWSSSAVA LEYAKCICRV LELIPSNGAV
     CKVRNNCMRL CGISPFSPQA QFQPDPFLAY RLHSLTCSFC NSHISIDLLT ERKTPITPFV
     CSECEAPIAA NAVEGSLVRH VSQLLRTYSQ QDFVCSKCHE MATTYVAEGC CGPLVGKSKP
     IDGELRALQY LGKIQGFTWL VESVEAALLC A
//

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