ID G3T6B0_LOXAF Unreviewed; 2286 AA.
AC G3T6B0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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:ENSLAFP00000009043.4};
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:ENSLAFP00000009043.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000009043.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000009043.4,
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:ENSLAFP00000009043.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000009043.4};
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 STRING; 9785.ENSLAFP00000009043; -.
DR Ensembl; ENSLAFT00000010808.4; ENSLAFP00000009043.4; ENSLAFG00000010802.4.
DR eggNOG; KOG1798; Eukaryota.
DR GeneTree; ENSGT00390000010194; -.
DR InParanoid; G3T6B0; -.
DR OMA; MLDQCRY; -.
DR TreeFam; TF105017; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
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:0006287; P:base-excision repair, gap-filling; IEA:Ensembl.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IEA:Ensembl.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:Ensembl.
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; 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 1528..1928
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 1293..1313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..1970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2017..2039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1948..1970
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2286 AA; 262092 MW; F0F3F6344AA12A08 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 QPQASQTLAT YSVSDAVATY YMYMKYVHPF
IFALCTIIPM EPDEVLRKGS GTLCEALLMV QAFHANIIFP NKQEQEFNKL TDDGHVLDAE
TYVGGHVEAL ESGVFRSDIP CRFRMNPAAF DFLLQRVEKT MHHAIEEEEK VPMEQVTNFQ
EVCDQIKTRL TSLKDVPNRI ECPLIYHLDV GAMYPNIILT NRLQPSAMVD EATCAACDFN
KPGANCQRKM AWQWRGEFMP ASRSEYHRIQ HQLESEKFPP LIPEGPTRAF HELSREEQAK
YEKRRLADYC RKAYKKLHVT RVEQRLTTIC QRENSFYVDT VRAFRDRRYE FKGLHKVWKK
KLSAAMEMGD AAEVKRCKNM EILYDSLQLA HKCILNSFYG YVMRKGARWY SMEMAGIVCF
TGANIITQAR ELIEQIGRPL ELDTDGIWCV LPNSFPENFV VKTTNVKKPK VTISYPGAML
NIMVKEGFTN HQYQELAEPS SLTYVTHSEN SIFFEVDGPY LAMILPASKE EGKKLKKRYA
VFNEDGSLAE LKGFEVKRRG ELQLIKIFQS SVFEAFLKGS TLEEVYGSVA KVADYWLDVL
YSKAANMPDS ELFELISENR SMSRKLEDYG EQKSTSISTA KRLAEFLGDQ MVKDAGLSCR
YIISRKPEGS PVTERAIPLA IFQAEPTVRK HFLRKWLKSS SLQEFDIRTI LDWDYYIERL
GSAIQKIITI PAALQQVKNP VPRVRHPDWL HKKLLEKNDV YKQKKISELF VLEGKRQVVM
NQAPEGSRSP GPPDVEDFGL MKPPHAAVPV VTRRKRVLWE SQEESQELEL TVPWQDILGQ
PPALGTTQEE WLVWLRFHKK KWQLQARQRL ARRKRQRLEG TESAPKAGAL REGPTTALGS
FLRRTARSIL DLPWQIVQIS ETSQPGLFRL WAVIGSDLYC IRLSIPRVFY VNQRVAKAEE
GPSYRKVNRV LPRANVVHHL YEYSVPEDMY QEHINEINTE LSAPDIEGVY ETQVPLLFRA
LVQLGCVCVV NKQLVRHLSG WEAETFALEH LEMRSLAQFS YLEPGSIRHL YLYHHAQGHK
ALFGVFIPTQ RRASVFVLDR VRSNQMPNLS AMYASEHSLL LEQVGSEFLP PPKHTFEVRA
ETDLKTICRA IQRVLLAYKE ERRGPTVVAV QSSWELRRLA GEVPVLEEFP LVPVRVTDKV
SYAVLDWQRH GARHMIRHYL HLDTCLSQAF EMSRYFHIPV GNLPEDISTF GSDLFFARHL
QRHSHLLWLS PTSRPDLGGK EADDSRLVME LDDHATVEIN SSGCYSTVCV ELDIQNLAVN
TVLQSHRVND MEGAASAGIS FDAIPQASLE DMITGNQATS MPASYDETAL CSSTFRILKN
MVVGWVKEIT QYHNVYADNQ VMHFYRWLRS PSSLLHDPAL HRTLHSMMKK LFLQLIAEFK
RLGSSVVYAN FNRIILCTKK RRIEDALAYV EYITNSIHSK EIFHSLTISF SRCWEFLLWM
DPSNYGGIKG KVSPSIHCGQ RESLEGEEAE REQEEEEEEE EEEEEGLEEA RVEDLLENNW
NILQFLPQAA SCQSYFLMIV SAYIVAVYHS MKEELRRNAP GSTPVKRRGA SQFSQETEGA
AGALPGTITF SQDYVANELT QNFFTITQKI QKKVTGFRNS TEPSEMFPQL PGSHLLLNNP
ALEFIKYVCK VLSLDTNITN QVNKLRRDLL RLVGVGEFSP EAQFRDPCRS HVLSEVICHS
CNFCRDLDLC KDSAFSQDGA VLPQWLCSNC EVPYDSTVIE AALVDALQKK LMAFTLQDLV
CLKCAGVKET HMPVHCSCAG DFALTVHTKV FMEQIRIFRN IAQHFSMSYL LEILEWLLQE
TPPPGH
//
