ID H2YP33_CIOSA Unreviewed; 2187 AA.
AC H2YP33;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=DNA polymerase epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
OS Ciona savignyi (Pacific transparent sea squirt).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000007091.1, ECO:0000313|Proteomes:UP000007875};
RN [1] {ECO:0000313|Proteomes:UP000007875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAVP00000007091.1}
RP IDENTIFICATION.
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; ENSCSAVT00000007183.1; ENSCSAVP00000007091.1; ENSCSAVG00000004243.1.
DR GeneTree; ENSGT00390000010194; -.
DR Proteomes; UP000007875; 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:UP000007875};
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 1481..1878
FT /note="DNA polymerase epsilon catalytic subunit A C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01159"
SQ SEQUENCE 2187 AA; 250733 MW; 90D5F48636323950 CRC64;
SSESISESSA KRLEQAQLND VLDAKFGYEK LKHPCERLGW LINLSSADCL DEDKRLISAV
DYYFVQDDGK RFKVSLPYHP YFYLAVKKGS EQEVTSHLKK KFSRIYSIEV VKKEDLDLHN
HLVGLKRTYL KLSFHHVDDM TSVRQAVHRV VRKNNERKNE TSIKIQEQLD NLVDIREYDV
PYHVRVGINL KIHVGLWYTV QFRGHSLPPV ITHREDLLER PDPVVLAFDI ETTKLPLKFP
DAETDNIIMI SYMIDGQGYL ICNRDIVSMD VDDFEFTPKP EFEGKFTIFN EKDELSTIHR
FFDHILEVKP QIFVTYNGDF FDWPFVEARA SKCGLDMLRE IGFSKDSQGE YKSRQASHMD
AYKWVKRDSY LPVGSQNLKA AAKAKLRYDP VELDPEEICR LASEEPQSLA NYSVSDAVAT
YYLYMKYVHP FIFALCTIIP MEPDSVLRKG SGTLCEALLM VQAYHANIVF PNKQESVYNK
LTNDGHVLDS ETYVGGHVEA LECGVFRANL PSSFRGDPEA YQGLHDQVER TVKFCIETEE
GIPLTEVLNF DEVCKDIKEK LVGLRDNPTR SENPVIYHLD VGAMYPNIIL TNRLQPSAMV
DEATCAACDF NKPGATCQRS MNWMWRGEYL PASRSEFHRI QQQLENEQFP DPNIPGKQVA
FHELSKEEQA NNEKKRLQEY CRRAYKKIKV KRLEEKFTTV CQRENSFYVD TVRMFRDRRY
EFKAALKRAK KQVSAALESG DASEVKKAKG LEVLYDSLQL AHKCILNSFY GYVMRRGARW
YSMEMAGIVC YTGAKIIQDA RMMIDKIGRP LELDTDGIWC ILPSSFPENY VINTTNAKKT
RVTISYPGAI LNVMVKDNFT NHQYEELVDP ATLKYERRNE NSIFFEVDGP YLGMVLPAAK
EEGKSLKKRY AVFNFDGSIA ELKGFEVKRR GELQLIKIFQ SSVFGEFLKG NTLEEVYQSI
AKVADYWLDV LYSKASNMPD DELFELITEN RSMSRKLEDY GSQKSTSIST AKRLAEFLGD
QMVKDAGLSC RFIISQKPEG APVTERAIPM AIFQSEASTK RHYLRKWTRQ SNMSDFDIRA
ILDWSYYIER LGSAIQKIIT IPAALQGISN PVPRIRHPDW LHKRLMEKND VYKQKRITDM
FSVKKRPPLY AADIGDIESL GEKGSENKHN PTVTMAKRRK TDVFEKSCQI RKHSNDTNSS
LELGWREVLG PPPPINDLFT GSLGKRKNWM DFHQQKWEIQ RKQRKMKKSD EANSSNIQAP
RSLNSSFMRQ QAHSVINSTW QVVQVTNTGK PGLFKVFALI GSELHTLKVN VPRIFYVNQK
SVKEATADAP WRKVHRILPR SAAVLNLYEY RMEEDEYQRH ICEIRKELMK PDVVGVYELQ
VPLFLRLLVD YGYFNRQLCY FLSSSQASRS LMGSDTDTFD FEQFELQSLI GNSYLEGGSL
KQVYIYHHAI GNKHIVGIFL STTSKSMVYI VDRVRSNRMP NLQNLFNENV DEEVLPNAGY
LFEVRVEVEV KQMYRNMQVG CCDHILFQRY LTTYKNERRG PTVVIYQSSM LLDGMKSKLP
ILNDFPVITA PCKASMEYND ELTWQKEAAS EMIEHFLESE MVFPRLLSYS KYFHIPVGNL
PNQPATFVTD LLCARHLRKH NHLLWCSPSD QPDLGGVEVG DKRLGLNDHA NTCIEINNSA
FHQTVCVQVD ISSLAINTIL QSHHVNDVEG ASSGVCFEGD LMSNSNSAMV CLVNYDDSAP
CSSTFRILKS MVLSWLRDVS VHRNQLADHQ LQSFHQWVAD RGSLFYDPAL QKTLQIMMKK
LFLQLISELK RLGSLIVFAN FSSIILSTKK NNVDDALAYM EYISNTIISK DIFHSMVLTV
RQCWKRLLWL DNANYGGIKA VLNRRTSSDE MVEMNFTLGS YLPPHADIQQ NFEAVIAGYI
SLVYQESVQE KLNRTSGSTP VLPRGNTQTQ LSESINEGTK PHMVTFSQAL ISGDVMEQMF
RLLVFHNLKQ SFYVMFPRLP GTQLHLDNPT LEFVKSVCKV LAVDDNVASQ VENLRRNLLR
LIGVGEFAPS ADWSDPCASY VIGQMTCGMC GLNRDIDLCR HALLIDGTCK WLCCGCGQPY
NEKWIEQQLV DDIQRKLLSY NLQDLVCRKC SAVNQLNMNK RCECAGDFEL TAKSGSIQQT
LKVFRNIADL ANLEYLAYTI DWISTST
//
