UniProt: A4IBX6

Database: UniProt
Entry: A4IBX6_LEIIN

LinkDB:  A4IBX6_LEIIN 
Original site:  A4IBX6_LEIIN

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   SMART (2)   
Literature (2)   
   PubMed (2)   
All databases (30)   

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ID   A4IBX6_LEIIN            Unreviewed;      2224 AA.
AC   A4IBX6;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, 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=LINJ_35_4430 {ECO:0000313|EMBL:CAM72348.1};
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM72348.1, ECO:0000313|Proteomes:UP000008153};
RN   [1] {ECO:0000313|EMBL:CAM72348.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM72348.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM72348.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM72348.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
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; FR796467; CAM72348.1; -; Genomic_DNA.
DR   RefSeq; XP_001469245.1; XM_001469208.1.
DR   AlphaFoldDB; A4IBX6; -.
DR   SMR; A4IBX6; -.
DR   STRING; 5671.A4IBX6; -.
DR   GeneID; 5073340; -.
DR   KEGG; lif:LINJ_35_4430; -.
DR   VEuPathDB; TriTrypDB:LINF_350049400; -.
DR   eggNOG; KOG1798; Eukaryota.
DR   InParanoid; A4IBX6; -.
DR   OMA; KGLACHF; -.
DR   Proteomes; UP000008153; Chromosome 35.
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; 1.10.287.690; Helix hairpin bin; 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:UP000008153};
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          1564..1920
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
FT   REGION          607..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1233..1252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1238..1252
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2224 AA;  250085 MW;  9F7B544E1791F1BF CRC64;
     MSSFGPQIIS EIIAVEKEDL DLVNHLSGKK RVYLKVVFRN VQDLTTVRGR LEKTVKLNAS
     LGSENPLRSQ FSGSLGDAMA KPFAEDPLYS AAGSSRWMDW VQDIREYDVK YHMRVAIDMK
     VYCGLWYDVT VTEGGARVQR CDDSRYAPAM PRVIAFDIET TKAPLRFPQP EVDEVYMISY
     MLDGRGYLII NREIVTEDIA PFEYTPKPEY EGFFDTFNEE NEAATLRRFF DEMRKYKPNV
     YVTYNGDYFD FPFIHARALY HGMNMRNEIG FTQMADGAFL NKQIPHLDCF YWVKRDSYLP
     QGSQGLKAVT KYKLGYEPIE VDPEDMLPLA QSQPQRMASY SVSDAVSTWY LYQKYVHPFI
     FSLATIIPMP PDDVLRKGSG GLCESLLMVQ AEANNVVFPN KKETERERFY EGHLIDTETY
     IGGRVEALRS GVYRSDIPMT FDMNPDTYQS LIDDVDEALR FTLEVENGVK VEEVTNLEEV
     RAAILAKLTN LRDRPHQQEK PFIYHLDVGA MYPNIILTNR LQPYAIARPD VCAGCCFNSP
     NNEAQCKRVM SWKWRAELFT AGRYEFQRVK AQLENESFAA GVIEQANLAA VQKKAYGNRK
     GNVLEGTSYE RKDDWKKSQS SRKGGGGAGY RQESRQQQRE AADALLQREF GADRNGEGGS
     SDSDGDADGP KAYHKLNENT QFNMLKRRLS EYSRKAYGKI HETREVMRSN VVCQRENSFY
     VDTVRLFRDR RYEYKAALKT WKKRLDAAKD SDERKVCQSR CVQMESLQLA HKCILNSFYG
     YVMRKGSRWS SMEMAGIVTY LGATLIQMAR SLVQQIGVTL ELDTDGIWCC LPNTFPENFT
     LATTNPSKPK ISISYPCVVL NKMVHDRYSN HQYQDLVSTG VYKTRSECSI YFEVDGPYLA
     MLLPASREEG KSIKKRYAVF SPDGSLAELK GFELKRRGEL MLVKDFQSQV FRRFLDGRTL
     ADAYASAAVV ADAALDMLES KGEGYDTEEI LEKITESSNM TRRLSEYPES QKSLAITTAR
     RIAEFLGPQM VKDKGLACHF IISRMPAGRP VTERAIPVTI FRADPAVRTH FLRKWTADTT
     VPSELNLKTL LDWDYYTARF SACVQKIVSI PAALQSLPNP VPRVVHPDWL EKRIRHRNSR
     YRQVSLVGML SKVQGKNEAL AGVSAAAAAA AAVRVDEDED GVVLEQGGGA GAVEGELQDL
     EDMAGGAGSS TVRHVPKTQK ARAACAGERR CAAGTDAETD WDEDDTDCEG ESEDDMERLQ
     READAELDAL AHDVKQRYFA PRSANALDAD FFADRGAKRW LAQRKDTWLQ RARLRRELAL
     ENGLSEVALG GENSDAVALG QATAPDVAGM NSHFIDLKSR ALATVWNVLE VRENEESPGT
     VQVLAALEHS LYSFRVQVRR TVLVDADPAL RLQAFDATEV SGRVLPRRAA AGRLYQVNVP
     PGEEGERCLN ALHVMEGVRR IYEEHRTRVD TFVEQLGCCV SVDSARHLRN ARRRPPSQRE
     LFGIDEMNMH TCTNYLSCGA ADRAVFVFHA VTEQRGLIAA VYPQTNTAFV VFIQPAEAAK
     PVISWSSICA ESAKRLHTST PEPIRVTSAV AEDQRAAWRQ VHQHLSAALE NAKAPLLAVL
     QSCQPTSTLL QQRALPVGLP YLRVLGAAED ERLLSDPFRW TRLLARRLFE RFFASLLWVE
     ERLALSRVSG IPLCNIAQDS CVHVLDVLYS RALHRRHHVL WCSSDPLITF DTVEERPREV
     CMAGGYTSWC VEFGLSRLDV VALLFSQAIE EGDDPNARVL CDRGVSTHFN ILRDLVADLL
     GQAMENILAD TLLNNVARWL RDPASSCYEP RLVELLSSLA HRALTGILLR LAKLGGRAVK
     VDGSSVTVLT SKYSLQEAVS FARFLTASLQ DQPMLLLLSL QPLRYWCPYV VLDPCDYAGL
     FITEDAIKLK QGEEPTRADL HVAHQLTMAS RLPSRARNTF VERVVETLYQ LNASTHHVYC
     DTVGDHTVTL ATRHDHLTRR LLQDSQKLFE GVLQTDIMDE VQRVMDTRDL YTEEEHAAHE
     RGELTLWSSG AVALEYAKCV CRVLELIPCN GAVGKVRNNC MRLCGISPFS AQSQFQADPF
     LAHRLQSVTC SFCNSHISID LLVRRKSVTS PFTCTACAAP IAAASMEGTL VRHVSQLLRV
     YNQQDFVCTK CREMTTTYVA ERCCGALVGK AAPVEGELRA LHRLAKIQGF AWLAESVEAA
     LLCT
//

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