UniProt: G3U301

Database: UniProt
Entry: G3U301_LOXAF

LinkDB:  G3U301_LOXAF 
Original site:  G3U301_LOXAF

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (15)   
   InterPro (10)   
   Pfam (3)   
   SMART (2)   
All databases (27)   

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ID   G3U301_LOXAF            Unreviewed;      2270 AA.
AC   G3U301;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
GN   Name=POLE {ECO:0000313|Ensembl:ENSLAFP00000022209.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000022209.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000022209.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022209.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000022209.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022209.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|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   Ensembl; ENSLAFT00000033742.1; ENSLAFP00000022209.1; ENSLAFG00000010802.4.
DR   GeneTree; ENSGT00390000010194; -.
DR   HOGENOM; CLU_000556_0_0_1; -.
DR   Proteomes; UP000007646; 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; 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; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR   PANTHER; PTHR10670:SF1; 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:UP000007646};
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          1526..1926
FT                   /note="DNA polymerase epsilon catalytic subunit A C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01159"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1291..1311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2001..2023
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2270 AA;  260030 MW;  A457F3141F2BF8FF CRC64;
     MVLHNSGRRR AEPSADGEAS RDDGPSSSVS ALKRLERSQW TDKMDLRFGF QRLKEPGEKT
     GWLINMHPTE VLDEDKRLVS AVDYYFIQDD GSRFKVALPY KPYFYIATRK GCEREVSSFL
     SRKFQGKIAK VETVPKEDLD LPNHLVGLKR NYIKLSFNTV EDLVKARKEI SPAVRKNREQ
     DHASDTYTAM LSSVLQGGGV ITDEEETSKK IADQMDNIVD MREYDVPYHI RLSIDLKIQV
     AHWYNVRYRG SAFPVEITRR DDLVERPDPV VLAFDIETTK LPLKFPDAET DQIMMISYMI
     DGQGYLITNR EIVSEDIEDF EFTPKPEYEG PFCVFNEPDE VHLIQRWFEH VQETKPTIMV
     TYNGDFFDWP FVEARAAVHG LSMYQEIGFQ KDSQGEYKAP QCIHMDCLRW VKRDSYLPVG
     SHNLKAAAKA KLGYDPVELD PEDMCRMAAE QPQTLATYSV SDAVATYYMY MKYVHPFIFA
     LCTIIPMEPD EVLRKGSGTL CEALLMVQAF HANIIFPNKQ EQEFNKLTDD GHVLDAETYV
     GGHVEALESG VFRSDIPCRF RMNPAAFDFL LQRVEKTMHH AIEEEEKVPM EQVTNFQEVC
     DQIKTRLTSL KDVPNRIECP LIYHLDVGAM YPNIILTNRL QPSAMVDEAT CAACDFNKPG
     ANCQRKMAWQ WRGEFMPASR SEYHRIQHQL ESEKFPPLIP EGPTRAFHEL SREEQAKYEK
     RRLADYCRKA YKKLHVTRVE QRLTTICQRE NSFYVDTVRA FRDRRYEFKG LHKVWKKKLS
     AAMEMGDAAE VKRCKNMEIL YDSLQLAHKC ILNSFYGYVM RKGARWYSME MAGIVCFTGA
     NIITQARELI EQIGRPLELD TDGIWCVLPN SFPENFVVKT TNVKKPKVTI SYPGAMLNIM
     VKEGFTNHQY QELAEPSSLT YVTHSENSIF FEVDGPYLAM ILPASKEEGK KLKKRYAVFN
     EDGSLAELKG FEVKRRGELQ LIKIFQSSVF EAFLKGSTLE EVYGSVAKVA DYWLDVLYSK
     AANMPDSELF ELISENRSMS RKLEDYGEQK STSISTAKRL AEFLGDQMVK DAGLSCRYII
     SRKPEGSPVT ESRAIPLAIF QAEPTVRKHF LRKWLKSSSL QEFDIRTILD WDYYIERLGS
     AIQKIITIPA ALQQVKNPVP RVRHPDWLHK KLLEKNDVYK QKKISELFVL EGKRQVVMNQ
     APEGSRSPGP PDVEDFGLMK PPHAAVPVVT RRKRVLWESQ EESQELELTV PWQDILGQPP
     ALGTTQEEWL VWLRFHKKKW QLQARQRLAR RKRQRLEGTE SAPKAGALRE GPTTALGSFL
     RRTARSILDL PWQIVQISET SQPGLFRLWA VIGSDLYCIR LSIPRVFYVN QRVAKAEEGP
     SYRKVNRVLP RANVVHHLYE YSVPEDMYQE HINEINTELS APDIEGVYET QVPLLFRALV
     QLGCVCVVNK QLVRHLSGWE AETFALEHLE MRSLAQFSYL EPGSIRHLYL YHHAQGHKAL
     FGVFIPTQRR ASVFVLDRVR SNQMPNLSAM YASEHSLLLE QVGSEFLPPP KHTFEVRAET
     DLKTICRAIQ RVLLAYKEER RGPTVVAVQS SWELRRLAGE VPVLEEFPLV PVRVTDKVSY
     AVLDWQRHGA RHMIRHYLHL DTCLSQAFEM SRYFHIPVGN LPEDISTFGS DLFFARHLQR
     HSHLLWLSPT SRPDLGGKEA DDSRLVMELD DHATVEINSS GCYSTVCVEL DIQNLAVNTV
     LQSHRVNDME GAASAGISFD AIPQASLEDM ITGNQATSMP ASYDETALCS STFRILKNMV
     VGWVKEITQY HNVYADNQVM HFYRWLRSPS SLLHDPALHR TLHSMMKKLF LQLIAEFKRL
     GSSVVYANFN RIILCTKKRR IEDALAYVEY ITNSIHSKEI FHSLTISFSR CWEFLLWMDP
     SNYGGIKGKV SPSIHCGQVR GTSLGELKPH SEHSRLEDLL ENNWNILQFL PQAASCQSYF
     LMIVSAYIVA VYHSMKEELR RNAPGSTPVK RRGASQFSQE TEGAAGALPG TITFSQDYVA
     NELTQNFFTI TQKIQKKVTG FRNSTEPSEM FPQLPGSHLL LNNPALEFIK YVCKVLSLDT
     NITNQVNKLR RDLLRLVGVG EFSPEAQFRD PCRSHVLSEV ICHSCNFCRD LDLCKDSAFS
     QDGAVLPQWL CSNCEVPYDS TVIEAALVDA LQKKLMAFTL QDLVCLKCAG VKETHMPVHC
     SCAGDFALTV HTKVFMEQIR IFRNIAQHFS MSYLLEILEW LLQETPPPGH
//

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