P30316

PR
Gene name
pol3 (pold, SPBC336.04)
Protein name
DNA polymerase delta catalytic subunit
Names
3'-5' exodeoxyribonuclease, DNA polymerase III
Species
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
KEGG Pathway
spo:SPBC336.04
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)

1-132 (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 P30316

Entry ID Method Resolution Chain Position Source
AF-P30316-F1 Predicted AlphaFoldDB

No variants for P30316

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P30316

No associated diseases with P30316

9 regional properties for P30316

Type Name Position InterPro Accession
domain Polymerase/histidinol phosphatase, N-terminal 341 - 408 IPR003141
domain PHP domain 342 - 700 IPR004013
domain DNA polymerase III epsilon subunit, exonuclease domain 422 - 642 IPR006054
domain Bacterial DNA polymerase III, alpha subunit, NTPase domain 842 - 1023 IPR011708-1
domain Bacterial DNA polymerase III, alpha subunit, NTPase domain 1039 - 1110 IPR011708-2
domain Exonuclease, RNase T/DNA polymerase III 426 - 592 IPR013520
domain DNA polymerase III PolC-like, N-terminal domain II 92 - 205 IPR024754
domain DNA polymerase III PolC-type, N-terminal domain I 5 - 78 IPR028112
domain DNA polymerase III alpha subunit finger domain 1114 - 1270 IPR040982

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.
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.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

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.

7 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.
DNA strand elongation involved in DNA replication The process in which an existing DNA strand is extended by activities including the addition of nucleotides to the 3' end of the strand, complementary to an existing template, as part of DNA replication.
DNA synthesis involved in UV-damage excision repair Any DNA synthesis that is involved in UV-damage excision repair.
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.
mitotic DNA replication lagging strand elongation Any lagging 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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTDRSSNEGV VLNKENYPFP RRNGSIHGEI TDVKRRRLSE RNGYGDKKGS SSKEKTSSFE
70 80 90 100 110 120
DELAEYASQL DQDEIKSSKD QQWQRPALPA INPEKDDIYF QQIDSEEFTE GSVPSIRLFG
130 140 150 160 170 180
VTDNGNSILV HVVGFLPYFY VKAPVGFRPE MLERFTQDLD ATCNGGVIDH CIIEMKENLY
190 200 210 220 230 240
GFQGNEKSPF IKIFTTNPRI LSRARNVFER GEFNFEELFP VGVGVTTFES NTQYLLRFMI
250 260 270 280 290 300
DCDVVGMNWI HLPASKYQFR YQNRVSNCQI EAWINYKDLI SLPAEGQWSK MAPLRIMSFD
310 320 330 340 350 360
IECAGRKGVF PDPSIDPVIQ IASIVTQYGD STPFVRNVFC VDTCSQIVGT QVYEFQNQAE
370 380 390 400 410 420
MLSSWSKFVR DVDPDVLIGY NICNFDIPYL LDRAKSLRIH NFPLLGRIHN FFSVAKETTF
430 440 450 460 470 480
SSKAYGTRES KTTSIPGRLQ LDMLQVMQRD FKLRSYSLNA VCSQFLGEQK EDVHYSIITD
490 500 510 520 530 540
LQNGTADSRR RLAIYCLKDA YLPQRLMDKL MCFVNYTEMA RVTGVPFNFL LARGQQIKVI
550 560 570 580 590 600
SQLFRKALQH DLVVPNIRVN GTDEQYEGAT VIEPIKGYYD TPIATLDFSS LYPSIMQAHN
610 620 630 640 650 660
LCYTTLLDSN TAELLKLKQD VDYSVTPNGD YFVKPHVRKG LLPIILADLL NARKKAKADL
670 680 690 700 710 720
KKETDPFKKA VLDGRQLALK VSANSVYGFT GATNGRLPCL AISSSVTSYG RQMIEKTKDV
730 740 750 760 770 780
VEKRYRIENG YSHDAVVIYG DTDSVMVKFG VKTLPEAMKL GEEAANYVSD QFPNPIKLEF
790 800 810 820 830 840
EKVYFPYLLI SKKRYAGLFW TRTDTYDKMD SKGIETVRRD NCPLVSYVID TALRKMLIDQ
850 860 870 880 890 900
DVEGAQLFTK KVISDLLQNK IDMSQLVITK ALSKTDYAAK MAHVELAERM RKRDAGSAPA
910 920 930 940 950 960
IGDRVAYVII KGAQGDQFYM RSEDPIYVLE NNIPIDAKYY LENQLSKPLL RIFEPILGEK
970 980 990 1000 1010 1020
ASSLLHGDHT RTISMAAPSV GGIMKFAVKV ETCLGCKAPI KKGKTALCEN CLNRSAELYQ
1030 1040 1050 1060 1070 1080
RQVAQVNDLE VRFARLWTQC QRCQGSMHQD VICTSRDCPI FYMRIAEHKK LQQSVDLLKR
FDEMSW