ID A0A337SHP3_FELCA Unreviewed; 2284 AA.
AC A0A337SHP3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSFCAP00000050177.1,
GN ECO:0000313|VGNC:VGNC:68938};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000050177.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000050177.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000050177.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000050177.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000050177.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000050177.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000050177.1};
RG Ensembl;
RL Submitted (SEP-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 EMBL; AANG04003227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9685.ENSFCAP00000050177; -.
DR Ensembl; ENSFCAT00000051047.2; ENSFCAP00000050177.1; ENSFCAG00000002498.6.
DR VGNC; VGNC:68938; POLE.
DR GeneTree; ENSGT00390000010194; -.
DR InParanoid; A0A337SHP3; -.
DR OMA; MLDQCRY; -.
DR OrthoDB; 5475218at2759; -.
DR Proteomes; UP000011712; Chromosome D3.
DR Bgee; ENSFCAG00000002498; Expressed in embryonic head and 10 other cell types or tissues.
DR GO; GO:0008622; C:epsilon DNA polymerase complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008310; F:single-stranded DNA 3'-5' DNA exonuclease activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006287; P:base-excision repair, gap-filling; IBA:GO_Central.
DR GO; GO:0045004; P:DNA replication proofreading; IBA:GO_Central.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
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:UP000011712};
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 1525..1925
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 1928..1968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1945..1968
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2284 AA; 261339 MW; D4C02A1128DCA3EB CRC64;
MVLRNSGRRR AEPGADGEAS RDDGPSSSVS ALKRLERSQW TDKMDLRFGF ERLKEPGEKT
GWLINMHPTE ILDEDKRLVS AVDYYFIQDD GSRFKVALPY KPYFYIATRK GCEREVSSFL
SKKFQGKIAK VETVPKEDLD LPNHLVGLKR NYIKLSFNTV EDLVRVRKDI SPAVRKSREQ
GHASDAYTAM LSSVLQGGSV VVDEEEASKK VTDQLDNIVD MREYDVPYHI RLSIDLKIHA
AHWYNVRYRG NAFPVEITRR DDLVERPDPV VLAFDIETTK LPLKFPDAET DQIMMISYMI
DGQGYLITNR EIVSEDVGDF EFTPKPEYEG PFCVFNEPDE VHLIQRWFEH VQEAKPTIMV
TYNGDFFDWP FVEARAAVHG LSMYQEIGFQ KDSQGEYKAS QCIHMDCLRW VKRDSYLPVG
SHNLKAAAKA KLGYDPVELD PEDMCRMATE QPQTLATYSV SDAVATYYLY MKYVHPFIFA
LCTIIPMEPD EVLRKGSGTL CEALLMVQAF HANIVFPNKQ EQEFNKLTDD GHVLDAETYV
GGHVEALESG VFRSDIPCRF RMNPAAFDLL LQRVEKTMRH AIEEEEKVPM EQVTNFQEVC
DQIKTKLTSL KDVPNRIECP LIYHLDVGAM YPNIILTNRL QPSAVVDEAT CAACDFNKPG
ADCQRKMAWQ WRGEFMPASR SEYHRIQHQL ESEKFPPLTA EGPARAFHEL SREEQAKYEK
RRLSDYCRKA YKKIHVTRVE ERLTTICQRE NSFYVDTVRA FRDRRYEFKG LHKVWKKKLS
AAVEVGDAAE VKRCKNMEVL YDSLQLAHKC ILNSFYGYVM RKGARWYSME MAGIVCFTGA
NIITQARELI EQIGRPLELD TDGIWCVLPN SFPENFVIKT TSVKKPKVTI SYPGAMLNIM
VKEGFTNDQY QELTEPASLT YVTRSENSIF FEVDGPYLAM ILPASKEEGK KLKKRYAVFN
EDGSLAELKG FEIKRRGELQ LIKIFQSSVF EAFLKGSTLE EVYGSVAKVA DYWLDVLYSK
AANMPDSELF ELISENRSMS RKLEDYGEQK STSISTAKRL AEFLGDQMVK DAGLSCRYII
SRKPEGSPVT ERAIPLAIFQ AEPMVRKHFL RKWLKSSSLQ DFDIRTILDW DYYIERLGSA
IQKIITIPAA LQQVKNPVPR VKHPDWLHKK LLEKNDICKQ KKISELFVLE GRRQVGVAQA
PEGTQSLGAP DMEDLGLAKP PRSVVPVATR RKRVLWESQG ESQDLELTVP WQEILGPPPA
LGTTQEEWLV WLRFHKKKWQ LQARQRLGRK KRRRLEVAEG DPRPGAVRDR PATGLGGFLR
RAARSILDLP WQIVQISETS QAGLFRLWAV ISSDLYCIRL NIPRQFYVNQ RVAKAEEGPS
YRKVSRVLPR SNVVYNLYEY SVPEDMYQEH VNEINTELSA PDIEGVYETQ VPLLFRALVQ
LGCVCVVNKQ LVRHLSGREA ETFALEHLEM RSLAQFSYLE PGSIRHLYLY HHAQGHKALF
GLFVPSQRRA SVFVLDTVRS NQMPSLSALY TAEHSLLMEK VGPELLPPPK HTFEVRAETD
LKTICRAIQR FLLAYKEERR GPTLIAVQSN WELKRLAGEV PVLEDFPLVP VRVADRVSYG
VLDWQRLGAR RMIRHYLNLD TCLSQAFEMS RYFHIPIGNL PEDISTFGSD LFFARHLQRH
NHLLWLSPTA RPDLGGKEAD DNRLVMEFDD QASVEINCPG CYSTLCVELD IQNLAVNTIL
QSHHINDMEG ADSVGISFDV IQQASLEDMI TGNQAAGTPA SYDETALCSS TFRILKSMVV
GWVKEITQYR NIYADNQVMH FYRWLRSPSS LLHDPALHRT LHNMMKKLFL QLIAEFKRLG
SSVVYANFNR IILCTKKRRV ADAIAYVEYI TNSVHSKEIF HSLTISFSRC WEFLLWMDPS
NYGGIKGNVP SSIHCGQQDS RKEGREEEEE EEEEGGEEEE EEEGAQEPDV EDMLENNWNI
VQFLPQAASC QSYFLMIVSA YIVAVYHSMK EELRRSVPGS TPLRRRGPSQ LSQEAQAVAG
ALPGVITFSQ DYVANELTQN FFTITQKIQK KVTGSRNATE LSKMFPVLPG SHLLLNNPAL
EFIKYVCKVL SLDTNITNQV NKLNRDLLRL VDVGEFSEEA QFRDPCRSYV LPEVICRSCN
FCRDLDLCKE PSFSQDGAVL PQWLCSNCLV AYDSSVIEMA LVEAVQKKLM AFTLQDLICL
KCQGVKETNM PVYCSCAGDF ALTIRTKVFM DQIRIFQNIA QHYGMSYLME TLEWLLQKNL
QLGH
//