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Database: UniProt
Entry: A0A337SHP3_FELCA
LinkDB: A0A337SHP3_FELCA
Original site: A0A337SHP3_FELCA 
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
//
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