P87154

PR
Gene name
cct7 (SPBC25H2.12c)
Protein name
DNA polymerase epsilon catalytic subunit A
Names
DNA polymerase II subunit A
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPBC25H2.13c
EC number
2.7.7.7: Nucleotidyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1183-1256 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P87154

Entry ID Method Resolution Chain Position Source
AF-P87154-F1 Predicted AlphaFoldDB

No variants for P87154

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P87154

No associated diseases with P87154

3 regional properties for P87154

Type Name Position InterPro Accession
domain DNA-directed DNA polymerase, family B, exonuclease domain 98 - 428 IPR006133
domain DNA-directed DNA polymerase, family B, multifunctional domain 773 - 1143 IPR006134
domain DNA polymerase epsilon, catalytic subunit A, C-terminal 1497 - 1886 IPR013697

Functions

Description
EC Number 2.7.7.7 Nucleotidyltransferases
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
chromosome, telomeric repeat region A complex of DNA and protein that seals the end of a chromosome. The telomeric repeat DNA consists of simple tandemly repeated sequences specific for each species. Typically one strand is G-rich and the other C-rich. The G-rich strand forms a 3'-terminal overhang, the length of which varies with species. The single strand overhang is bound by a variety of proteins, including telomere capping proteins that bind to the single-stranded DNA and seal the telomeric loop.
epsilon DNA polymerase complex A heterotetrameric DNA polymerase complex that catalyzes processive DNA synthesis in the absence of PCNA, but is further stimulated in the presence of PCNA. The complex contains a large catalytic subunit and three small subunits, and is best characterized in Saccharomyces, in which the subunits are named Pol2p, Dpb2p, Dpb3p, and Dpb4p. Some evidence suggests that DNA polymerase epsilon is the leading strand polymerase; it is also involved in nucleotide-excision repair and mismatch repair.
nuclear replication fork The Y-shaped region of a nuclear replicating DNA molecule, resulting from the separation of the DNA strands and in which the synthesis of new strands takes place. Also includes associated protein complexes.

6 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA-directed DNA polymerase activity Catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1); the synthesis of DNA from deoxyribonucleotide triphosphates in the presence of a DNA template and a 3'hydroxyl group.
nucleotide binding Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.
single-stranded DNA 3'-5' exodeoxyribonuclease activity Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a single-stranded DNA molecule.
zinc ion binding Binding to a zinc ion (Zn).

15 GO annotations of biological process

Name Definition
base-excision repair, gap-filling Repair of the damaged strand by the combined action of an apurinic endouclease that degrades a few bases on the damaged strand and a polymerase that synthesizes a 'patch' in the 5' to 3' direction, using the undamaged strand as a template.
CENP-A containing chromatin assembly The formation of chromatin containing the histone H3 variant CENP-A to form centromeric chromatin. This specialised chromatin occurs at centromeric region in point centromeres, and the central core in modular centromeres.
chromatin organization The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA.
CMG complex assembly The aggregation, arrangement and bonding together of a set of components to form the CMG complex, a protein complex that contains the GINS complex, Cdc45p, and the heterohexameric MCM complex, and that is involved in unwinding DNA during replication. The process begins when additional proteins (e.g. Cdc45 and Sld3) join the loaded, inactive double MCM hexamer at replication origins, and ends when Mcm10 triggers the separation of the Mcm2-7 double hexamers, forming two active CMG complexes.
DNA replication proofreading Correction of replication errors by DNA polymerase using a 3'-5' exonuclease activity.
DNA strand elongation involved in mitotic DNA replication Any DNA strand elongation involved in mitotic cell cycle DNA replication.
DNA-templated DNA replication A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands.
heterochromatin assembly by small RNA A heterochromatin formation-based gene silencing process mediated by a small RNA molecule that occur before the beginnning of trancription.
leading strand elongation The process in which an existing DNA strand is extended continuously in a 5' to 3' direction by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication. Leading strand elongation proceeds in the same direction as the replication fork.
mitotic cell cycle Progression through the phases of the mitotic cell cycle, the most common eukaryotic cell cycle, which canonically comprises four successive phases called G1, S, G2, and M and includes replication of the genome and the subsequent segregation of chromosomes into daughter cells. In some variant cell cycles nuclear replication or nuclear division may not be followed by cell division, or G1 and G2 phases may be absent.
mitotic DNA replication initiation Any DNA replication initiation involved in mitotic cell cycle DNA replication.
mitotic DNA replication leading strand elongation Any leading strand elongation that is involved in mitotic cell cycle DNA replication.
nucleotide-excision repair, DNA gap filling Repair of the gap in the DNA helix by DNA polymerase and DNA ligase after the portion of the strand containing the lesion has been removed by pyrimidine-dimer repair enzymes.
premeiotic DNA replication The replication of DNA that precedes meiotic cell division.
regulation of DNA recombination at centromere Any process that modulates the frequency, rate or extent of DNA recombination within centromeric DNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPLKTARGAS KYQFRKFNGN YNGKSKSNGR TFAKSTEEVG FNDPMKIVYK KNEIDRMMGF
70 80 90 100 110 120
DSYEGGQPRE AWLLNVHPTV IESTKGNSTL SAVDFYFIQD DGDTFRCTIP YSPYFYIAAR
130 140 150 160 170 180
EGKEALVDDY LKKKFVGLIK STTRIFKEDL QLKNHIVGYQ KLYIKLVFDN LNDLQAVRKS
190 200 210 220 230 240
LMSAVKANSS QQDAVDAYTN LSSENLNGII ENAFEDPLNH VLDIREYDVP YHSRTLIDLN
250 260 270 280 290 300
IRVGQWYTVS YHEGHVQISL LASRIERAEP TIMAFDIETT KLPLKFPDSS FDKIMMISYM
310 320 330 340 350 360
IDGQGFLITN REIISQNIED FHYTPREEFE GPFIIFNEPD EVGLLHRFFK HIRSAKPSVI
370 380 390 400 410 420
VTYNGDFFDW PFVDARAAFH GLNLTEETGF FRDAEDEYKS SYCSHMDAFR WVKRDSYLPQ
430 440 450 460 470 480
GSQGLKAVTV SKLGYNPIEL DPELMTPYAS EKPQVLAQYS VSDAVATYFL YMKYVHPFIF
490 500 510 520 530 540
SLCNIIPLNP DEVLRKGTGT LCETLLTVEA CTKNIILPNK HVDASQKFFD GHLLASETYV
550 560 570 580 590 600
GGHVESLESG VFRSDLPTNF NMDPKVYEEL ILQLDKALDF SLTVENNVNV DEIENYEEVR
610 620 630 640 650 660
DSILKKLSDL RDRPKRSEKP RIYHLDVASM YPNIMITNRL QPDSVKDESF CATCDLNVPN
670 680 690 700 710 720
KTCDRRMVWA WRGEYYPAKK GEYHMIYSAL QSERFPGPTP FSPFRSFQEL SPSEQAAMVQ
730 740 750 760 770 780
KRIADYSRKV YHRLYDNTVI ERETIICQKE NSFYIDTVKS FRDRRYDFKG LQKKWVKQLA
790 800 810 820 830 840
AIKEKGGLAE IEEAKKMVVL YDSLQLAHKV ILNSFYGYVM RKGSRWYSIE MAGITCLTGA
850 860 870 880 890 900
TIIQMARQIV ERAGRPLELD TDGIWCILPE SFPENFEFKK KSGGKVFISY PCVMLNHLVH
910 920 930 940 950 960
EKFTNHQYSA LKDPEKLVYE TTSENSIFFE VDGPYRAMIL PASTEEGKNL KKRYAVFNFD
970 980 990 1000 1010 1020
GSLAELKGFE VKRRGELKLI KDFQSQIFKV FLKGDSLEEC YQEVAYVADT WLEILFTKGS
1030 1040 1050 1060 1070 1080
NLTDDELIEL ISENRSMSKA LSEYGSQKST SITTARRLAD FLGDQMTKDK GLACRFIISA
1090 1100 1110 1120 1130 1140
SPKGRPVAER AVPVAIFFAE ESVKRHFLRL WLKDNGLYDV DIRDIIDWDY YLKRLGSVVQ
1150 1160 1170 1180 1190 1200
KLISIPAALQ RISNPVTRFP LPDWLQKRVA VLNSKYQQKK IDSIFSLAPT NPSTINNTKV
1210 1220 1230 1240 1250 1260
TDIEDLGSVT HKDKRIVARV TKRKLLQQSG NSEAPVSFEV KPVSFMDGYS NWLKYAKKKW
1270 1280 1290 1300 1310 1320
KYQKQVKLRR RHLIGFQSRQ FTNVLQSSAE VMFENLWHIL QIRETDVPGI LHAWVIIRNR
1330 1340 1350 1360 1370 1380
LTSIRFIVNR KFFVCFKDET LPNVEIEGCL IEKSNAILPH GSTSDKLFLL EIPEKSYLTE
1390 1400 1410 1420 1430 1440
KVSISMIFAH PSVSGIYETR IEPIERLILE MGSRKRFNNS VPGALGKGFE FGFESKMFTD
1450 1460 1470 1480 1490 1500
PSDNDVSYLD GVEMNYLYAF HFSISNRFVF SLFMPHLKKV EAIIYDKLPG SDMSFPSISK
1510 1520 1530 1540 1550 1560
IYEELRSKFD NLIKESSIEY PDTLSCNVIF SGNERKAYKL IDEKLLQYFS TKTKNSLLII
1570 1580 1590 1600 1610 1620
ESSLPHILKA NVKQIEELPY IMIPRLESNI QSLSWKQHIA TKMIQHFLAI GSWLFHRIQL
1630 1640 1650 1660 1670 1680
SRFSDIPLCN FESDDIQYSI DVVYSRKLKE HNIILWWNKG PTPDLGGIEK DSILQIASPK
1690 1700 1710 1720 1730 1740
DPLEVNNPGA YSNACVDISL SNLALCSILN SALINDIEGI GDMAALNDNY MTAINDDLEE
1750 1760 1770 1780 1790 1800
KLGIHDNIGL THSLPVLKAL VKTWWNEAAS GNNLADLIIQ HLARWISSSK SYLYSPLLSS
1810 1820 1830 1840 1850 1860
HVEVIMRKTF LQLLSEIKRL GAHIIHASAN KILIKTSKLI VQNAVTYSNY LLKSIKTLPL
1870 1880 1890 1900 1910 1920
FHFLDLNVTE YWDYLLWMDS VNYGGKMVAA NFSATNEEPQ TVVSWHIKSH LPPIIQPEFQ
1930 1940 1950 1960 1970 1980
SWIVEFIEEV YKQKLEKSNT KVGFVRVKNN NADEDSEIVG SGILKSKLIH PLKRKVAQVR
1990 2000 2010 2020 2030 2040
RCFQELQLDE NTREDLKFPK LPGSFLNYTD GALELVKSIC AVFELSHDLN LEVRFLKKSL
2050 2060 2070 2080 2090 2100
LSLLQIQEFS TQAVFRYPSR RLSLDQIPCK QCGVHQDFDL CLHEHLWPTR DDMGTLVFSD
2110 2120 2130 2140 2150 2160
GWSCSSCNLV YDRWVFEETL VDNLYHQLTL YQLQDLICSK CKTVKQWSLK ERCSCSGEWV
2170 2180 2190
LQLSPTKFRE MLNVYQSVAD FYEFSILQNS VQSILSVLN