ID Q4U8N2_THEAN Unreviewed; 2210 AA.
AC Q4U8N2;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, 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=TA09840 {ECO:0000313|EMBL:CAI76821.1};
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI76821.1, ECO:0000313|Proteomes:UP000001950};
RN [1] {ECO:0000313|EMBL:CAI76821.1, ECO:0000313|Proteomes:UP000001950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(2005).
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; CR940353; CAI76821.1; -; Genomic_DNA.
DR RefSeq; XP_953446.1; XM_948353.1.
DR STRING; 5874.Q4U8N2; -.
DR GeneID; 3863306; -.
DR KEGG; tan:TA09840; -.
DR VEuPathDB; PiroplasmaDB:TA09840; -.
DR eggNOG; KOG1798; Eukaryota.
DR InParanoid; Q4U8N2; -.
DR OrthoDB; 5475218at2759; -.
DR Proteomes; UP000001950; Chromosome 4.
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 Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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:UP000001950};
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 1640..2041
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
SQ SEQUENCE 2210 AA; 257910 MW; 8F1DA2DE932C9A73 CRC64;
MERVERAPNW NTNGKRCGFL YNVVVTNVKA SVDLKRSVEL KKTIKQSSSQ IRDEKDSDNF
YSNKTSLSAE NQYNSALTLH FVSEDGAEWS TSLIYSPYFY IAVLREELMD IALQFLYNNF
RSHSIGPVLL EPCRRIDLSL PNHLEKVDPV EGVSKHNLAK LIKISFKTID QLERGRDMIT
SLKRQFEKDN QINESKNEYD EFDEDVFSSN YQSKTQYDNF NTVSKDSEIT VEGMGLSKKY
ASNSVLRIIG ELYEHDVLYI NRVCIDLGIR CGTWYEVRRE DFNVSVTPLE KTSVPPLNVF
AWDIECYKPP LKFPDMETDE IMLISVMFNG QGYLIVNRTI VSKDIAEFLY QPREDIVGNA
CFKIYNERTE RDLLMRFFYL INYLKPHIFV TYNGDNFDFP YVNRRAEING IHMNKVSGLH
LSSELFQHAA ILNMDCYKWV ERDSYLPFGS RTLKQVCKLM LKYNPVEIDP EDMVHLARVT
PQKLAVYSVS DAVATYHLYM KFIHNFILAL SYIVPLAPNE VLRQGAGTLC ENLLMAQAYA
NNILFPNKHI QKAIRFYTNP ETERQHLVYE NTYIGGRVES LRCGIFRDDQ AENFELSSST
YDDLINNLEN SLIYWAKHSK IINNIDEIDI ISETPMKTNN PMEIDNSMET DNPVRTENSV
GIPSERLRRI FSRFDNFEQV YKELCVRLGR LRDEPNVRTY PRIYHLDVGA MYPNIIITQR
LQPTAIVDEK FCEKCSYYSE SERCQKRMRW KQRLEISPID KSQILVVMQN LKARTYQPSE
IPYQHREETF EDSEVDSDTQ ESELKPKVRT WEQLTEREKG AHLQRAVKAC SQKIFKKTRI
YKEADVESII CQRENHFYVQ TVQTFRDRRY AFKHLKKEGE NELKELIKNG CNDPVLIKSV
REKILINDSL QLAYKCILNS FYGYVKRTGS RWYSMEMGAI VTYTGASIID SARKLIEKIG
IPIELDTDGI WCMLPDIFPA VLDLTYTVNT PEGEKKKSVE LEYMTTVLNM LIAEEWTNEQ
YLDLEESGRY VTVQKNEIFF ELDGPWHAMF LPASEKSEEL LKKRYVVYNH NGQIVELKGF
EIKRRSEMRM IQLFQEDIFP QYLMGQTKEQ AYQNAAKVAI SYRKILDTRA SDLADDDLFD
LLLSKKTVRK PVIEQPHQKC FGITSARRLS ELFKNDSYLN DANLSMSFLL ASQPTDAPRT
ARAIPIQTFK VDKTVRSQFL AKWLKIQLST AMRMSSRDIL DWNYYKERID TQILKLVVLP
AIMQGLINPI PQVELPKWVK RKQSILDNKH HTISSYFNTI TQNIINTNHT VKNIENEIVD
DVIDWLEELK KKWIKSVINF KNIQKNTFNK INYNLHKELK SKLLNGKSHG LDFDDYYSLF
TETWHIIDFT LDPHECGYLN CKVSIYNKPV ILNVRIELWR KLYVNSNSKL QFTTNTNTNG
ATGTTNGTNT TNTNGINMKE VYMKEIKDNY FLPRGVNQMK LIELEMKESY FIKHLKNSIN
SILHKTIEGV YESKIPVTFD FISKIGTIIN IRNYTPNNVL SEGLEFKSNS ISSNISLQTV
DLNYLSDFNI TFVHIFHSID NDTKRRNRIY VGIYNRGEHY VNKIYIGGPI VLKKYNEEQF
SNISLPILEK YKQKWINSND IIGQYMNPYI FPDCFGYDYT IDIEGLDASS TACKNILKKV
DSYLNSLRPS ISKKKHFLYI YSSIDKSELG EWSKGEYYPV YFDPIGKSHP QILSNLFLKS
SFEESISLLS KQFSIFEEKL SLSRISAIPI FVLLSLNTLD TFKCLFDIMY SRALRISNTI
LWGTNESGVD LGIIHLNNTH CDYDIQENEN NFDFTLPGIY RSYGAKITFN QSIMYNAILL
ESKMNDYNNF EQNSNKNEHE IDLHSSIFHP NSFKILGTML ENLMNLTNLV YQKVDYVTFQ
NIVNMCSYLK SWLSDPTSIL YDPALYSMVS YTKPAMVGTR QYLVRLMKQL LIKHKLKTIH
VDPTYIIVQS DCISITKGRT RIEEALNDLA SNQSKFKNTP FYVEEEYVAM VQIDKNNYIR
YKNYVDASKE NCTENLKVLE FMPLAVEMFI RYFMKTITLD PLWRSLKSYY EDKNSETSSD
SIEPLNLVRT DFQRILKKIQ DMIIHDWHQP GSYFSRLYDL ISDTETFAKT FDKNNKLVKI
EFPRLPGTTL SDSDDWRLVT INLLLHIMKI DKSLDWTNFS LISSFDVCYT
//
