Q54N97
Gene name |
pold1 (DDB_G0285381) |
Protein name |
DNA polymerase delta catalytic subunit |
Names |
DNA polymerase III |
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0285381 |
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)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q54N97
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q54N97-F1 | Predicted | AlphaFoldDB |
No variants for Q54N97
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q54N97 | |||||
No associated diseases with Q54N97
4 regional properties for Q54N97
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.7.7 | Nucleotidyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| delta DNA polymerase complex | A multimeric DNA polymerase enzyme complex which differs in composition amongst species; in humans it is a heterotetramer of four subunits of approximately 125, 50, 68 and 12kDa, while in S. cerevisiae, it has three different subunits which form a heterotrimer, and the active enzyme is a dimer of this heterotrimer. Functions in DNA replication, mismatch repair and excision repair. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| 3'-5'-exodeoxyribonuclease activity | Catalysis of the sequential cleavage of mononucleotides from a free 3' terminus of a DNA molecule. |
| 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. |
| metal ion binding | Binding to a metal ion. |
| 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. |
5 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 repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
| DNA replication proofreading | Correction of replication errors by DNA polymerase using a 3'-5' exonuclease activity. |
| 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. |
| 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 |
| MKRSIVTGGG | NNDKKFKAQP | PPKNNYRGGG | DDEEDDEFEE | DDDEDEGDEF | GEEEDEDDID |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VENIIASDSM | DIDIQDDGSQ | QLFLWSRKPV | QDLVPHKKPL | IFQQLEVDYT | EIKEPVPGMP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GPKVGPLPAI | RLFGVTKEGN | SVLCKVHGFL | PYFFISCPPG | FTEADCKSLK | HDLNESMKMS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SNQSNEKDIE | NIVVSIDIEK | KKSIMGYNPN | PLSDFIRITL | ILPKFVTRCR | EIFESGRHHF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TIPGQPFRQY | QTYESNILFA | LRFLIDKGIT | GCSWIELPAN | TYKLSETPVS | TCQIEVDTSL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ETIISLSDDD | SPAPYRILSF | DIECAGRKGV | FPEPEKDPVI | QISNIVKNNG | DAEPFIKNIF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TLKGCSSIVG | AHVIPHKREE | DLLREWRKFV | IKVDPDVIIG | YNIVNFDIPY | LISRARQLKI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PEFALLGRIK | TTISKIKSTR | FSSSNLGTRE | SKEISMPGRT | QFDLMQAIQR | DHKLTSYSLN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NVSAHFLKEQ | KEDVHFSIIS | DLQNGTDDDR | RRLAVYCIKD | AVLPMRLLDK | LMILINYTEM |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ARVTGVPLSY | LLGRGEGIKV | LSQLYRKAMV | ENFLIPTYKV | TGKGEKFQGA | IVIEPTPGFY |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DTPIATLDFT | SLYPSIMMAH | NLCYSTLLSA | EEAKKLPPEI | YTTTPFGDHF | IKSDTKKGLL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PRILEELLSA | RKKAKDELKN | EKDPFKRAVL | DGRQLALKIS | ANSVYGFTGA | RVGKLPCLEI |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SRSVTSFGRE | MLDKTKKIVE | ERYTIANGYK | HDAVIIYGDT | DSVMVKFGVK | TVAEAMEMGR |
| 790 | 800 | 810 | 820 | 830 | 840 |
| DAAKFVTTTF | IRPINLDFEK | VYYPYLLMAK | KKYAGLYWTK | PDIHDRMDVK | GLEMVRRDTC |
| 850 | 860 | 870 | 880 | 890 | 900 |
| LLVRNVVSTI | LKKILIEKDL | KSAEEYTKSV | ISDLLQNRLD | LSMLVITKAL | SKTQYKGKVI |
| 910 | 920 | 930 | 940 | 950 | 960 |
| HNELARKMRA | RDPATAPNLG | DRVPYVVIQG | SKGAPIYEKA | EDPLYALEHN | ILLDCQYYLD |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| KQLKAPLIRI | FKPIMSNPDL | IFHGEHTRTI | AQSTLSDNNK | GFFGTLKKKK | VCMNCPKELT |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| DTESTTCINC | QHKEASLYQT | SLEKVTSLET | KFSEAWTQCQ | RCSGSLHQPV | LCSNRDCPIF |
| 1090 | 1100 | ||||
| YMRTKVQLDL | IEAKKTLNRF | NVEW |