Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6C4J0

Entry ID Method Resolution Chain Position Source
AF-Q6C4J0-F1 Predicted AlphaFoldDB

No variants for Q6C4J0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6C4J0

No associated diseases with Q6C4J0

3 regional properties for Q6C4J0

Type Name Position InterPro Accession
domain DNA-directed DNA polymerase, family B, exonuclease domain 89 - 412 IPR006133
domain DNA-directed DNA polymerase, family B, multifunctional domain 749 - 1090 IPR006134
domain DNA polymerase epsilon, catalytic subunit A, C-terminal 1513 - 1873 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

2 GO annotations of cellular component

Name Definition
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.

9 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.
double-stranded DNA binding Binding to double-stranded DNA.
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.
single-stranded DNA binding Binding to single-stranded DNA.
SUMO binding Binding to the small ubiquitin-like protein SUMO.
zinc ion binding Binding to a zinc ion (Zn).

11 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.
DNA replication proofreading Correction of replication errors by DNA polymerase using a 3'-5' exonuclease activity.
double-strand break repair via nonhomologous end joining The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear.
error-prone translesion synthesis The conversion of DNA-damage induced single-stranded gaps into large molecular weight DNA after replication by using a specialized DNA polymerase or replication complex to insert a defined nucleotide across the lesion. This process does not remove the replication-blocking lesions and causes an increase in the endogenous mutation level. For example, in E. coli, a low fidelity DNA polymerase, pol V, copies lesions that block replication fork progress. This produces mutations specifically targeted to DNA template damage sites, but it can also produce mutations at undamaged sites.
gene conversion A DNA recombination process that results in the unidirectional transfer of genetic material from a donor sequence to a highly homologous acceptor. The resulting acceptor sequence is identical to that of the donor.
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 checkpoint signaling A signal transduction process that contributes to a mitotic DNA replication checkpoint.
mitotic intra-S DNA damage checkpoint signaling A mitotic cell cycle checkpoint that slows DNA synthesis in response to DNA damage by the prevention of new origin firing and the stabilization of slow replication fork progression.
mitotic sister chromatid cohesion The cell cycle process in which the sister chromatids of a replicated chromosome are joined along the entire length of the chromosome, from their formation in S phase through metaphase during a mitotic cell cycle. This cohesion cycle is critical for high fidelity chromosome transmission.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGRPFNGNNT HVVKQRSDEF ERRRLERIEQ LGQKFAAVER RDAIDDRMGF TRFSGDEKRV
70 80 90 100 110 120
GWLVNMHETL LQSETAERGL AAVDYYFYDE EGGNFKSTVV FRPYFFVICK PHTEHAVKDL
130 140 150 160 170 180
MEKMFERVLA STEIVTKEDL NLTNHLTGKK RKAVKLEFHN SEDLSSTRFT LSKIVDRQTQ
190 200 210 220 230 240
QTEQHLNIYE LEGDVDTSTD VESSITGIKE FDVPFETRVA IDLDIRVGNW YEVTKENDTA
250 260 270 280 290 300
VLKHMVEREY RADPVVMAYD IETEKAPLRF PDSAVDRIMM ISYMIDGEGF LITNREMVSE
310 320 330 340 350 360
DIEDFEYTPK PEFPGNFTIF NEPNEKAVLE KWFEHIRDVC PTVMTSYNGD FFDFPFIDKR
370 380 390 400 410 420
TAFHGMNLYD EIGWKKVEEE RYECSYCVHM DCLNWVKRDS YLPQGSQGLK AVTKVKLSYD
430 440 450 460 470 480
PKELDPEKMT PYARDHPQIL AEYSVSDAVA TYYLYMKYVH PFIFSLCCII PLNPDAVLRK
490 500 510 520 530 540
GTGTLCEMLL MVKAYEGRII LPDKHKPALE RHYKGHLVDN ETYTGGHVES LAAGVFRSDI
550 560 570 580 590 600
MVDFDIDTNS IDELLVNLDE TLEFCVTVEA GKKSSDFENL DEVRDQIIEQ LQELKSNPKR
610 620 630 640 650 660
SDYPLIYHVD VASMYPNIMT TNRLQPDSMV DEKDCAVCDY NRPDKTCARE LEWARRVDYY
670 680 690 700 710 720
PVSKGDVNNL KQGLVEEYSG GRFGNGSSVE ISYDEGMTER EKFQKRKGWA GLSGQEQANK
730 740 750 760 770 780
LKERVAAFSL KTKARKTDSE TTVQKTIVCQ RENPFYVDVV QEFKQRRIDY KTKAKRWNKE
790 800 810 820 830 840
AASASDPASR EEAKKMAITN DSMQLAHKVI LNSFYGYVMR KGSRWYSMEM AGVTCYTGAK
850 860 870 880 890 900
IIKIARQTME GLGIPLELDT DGIWCMLPKT FPEKFKCKFK DGSSYELEYP CSIMNYLVHR
910 920 930 940 950 960
DFTNHQYQKL NPETGKYDTH SENSIFFELD GPYKCMMMPT STDKGKGLKK RYVVFDDRNK
970 980 990 1000 1010 1020
IVELKGFEVK RRGELSLIKK FQSQLWDTFL EGSNLVECYA AQARVAEAWL AVIDSRGKNL
1030 1040 1050 1060 1070 1080
SDEELIDLVC ENKSMSKPVH EYGSQKSTAL TTARRLAEIM GDSILTGGKL STKYIIAVRT
1090 1100 1110 1120 1130 1140
KNSMPVPEAK KGSDEDSSTA DRAIPTLVFE TESLDEKLRF LKRWMGPRWE STDPRDVIDW
1150 1160 1170 1180 1190 1200
MYYRERLATT INKLVVIPAI LLGLKNPVRG CDPPEWASDI IKQRDNPIKQ STLSSYFVKG
1210 1220 1230 1240 1250 1260
KLPTPEPILS EEDEVMEIQV GDIESIGTTP SPSRPPGVPA RVVVSKRVRK TVEETDKSTP
1270 1280 1290 1300 1310 1320
SLPHKAPDPF ADYAAYIKYA KVKWKHQKAQ RDRRAHLFGE SDNGIASSWV SKNAHLAQDA
1330 1340 1350 1360 1370 1380
WHLVSIHAAE KPGQVEASVI IGDKMQRVQI NVPRKVYVGS REPLKWDKFT DVTNAMAVAE
1390 1400 1410 1420 1430 1440
EEQPKYLYRA VMSEDMYQTE MTNPESPLKD PHVTKIYEAD VSPDSRALIE LGSTFHLDAS
1450 1460 1470 1480 1490 1500
TPGILSKGFT HGFEAKWFKS GDSRSYLQNS GLSYAHIVHV VSSAVEIFVI TPTWDAPALV
1510 1520 1530 1540 1550 1560
FVHQSSSSEK LPDISKEYAR LRRGERYKQN MDDCTVFSFP DTMQYEVEYC SNHRRMLQKV
1570 1580 1590 1600 1610 1620
SKACDSLSGS RNGQLVFALH SPDRNVDEKV AALARIPCIR LRPVPPSTAA VGWQRDLVRR
1630 1640 1650 1660 1670 1680
LIASFLSHGA NISYLVEMAR YAKMPLCHVQ DTRDVIDVSY ARRLIQNSVV LWWSAALSTG
1690 1700 1710 1720 1730 1740
GALTDQAEVP VANNPGLYTN ICFEIKIEHL VLNALLQSAV IQDTEGDIHN ELLSNAFNPH
1750 1760 1770 1780 1790 1800
ALKTLKMVVK EWWEHGDKKR PPQDLLDNFT VWVYAPESRL FSPQLLYHTQ NLTKKTFLYL
1810 1820 1830 1840 1850 1860
AQECRKHQAQ LVYADQHKLV LQTEKTELQL VYSYSNYIVR QIRTHPILKY VSVDITRYWD
1870 1880 1890 1900 1910 1920
TFLWMDKWNY GGYSSDVIVD PSKQSESLLM HWHIANFLPE TLQQEFSKWV QEYIHLLRLR
1930 1940 1950 1960 1970 1980
KYPENRTTDV DDMPSDTPML TDGDKDDAAL LSDKFFGKGV VSYLHPKLVR RVKLLAQKLS
1990 2000 2010 2020 2030 2040
DVLSSGDSID AFKFPVLPGS MIQPETNPVV EFAKYVCHIY GINAKANFEV QILLRDLLNI
2050 2060 2070 2080 2090 2100
FDINEFSEEG TFRDPSMSLK LTNMMCFKCK NPCDLDLCKD SCCTKSGFRC PLCNSLYDMV
2110 2120 2130 2140 2150 2160
IVEQRLVGQL QRMILEYETQ DFRCDKCRRV KEYELTEFCP CSGSWVTIMS AEDVHKELSI
2170 2180
YDRCARWFEL KMLGSFLRQL GYV