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 Q9LRE6

Entry ID Method Resolution Chain Position Source
AF-Q9LRE6-F1 Predicted AlphaFoldDB

No variants for Q9LRE6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9LRE6

No associated diseases with Q9LRE6

4 regional properties for Q9LRE6

Type Name Position InterPro Accession
domain DNA-directed DNA polymerase, family B, exonuclease domain 138 - 481 IPR006133
domain DNA-directed DNA polymerase, family B, multifunctional domain 545 - 978 IPR006134
conserved_site DNA-directed DNA polymerase, family B, conserved site 759 - 767 IPR017964
domain C4-type zinc-finger of DNA polymerase delta 1015 - 1086 IPR025687

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

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.

4 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-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.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P28339 POLD1 DNA polymerase delta catalytic subunit Bos taurus (Bovine) PR
P54358 PolD1 DNA polymerase delta catalytic subunit Drosophila melanogaster (Fruit fly) PR
P28340 POLD1 DNA polymerase delta catalytic subunit Homo sapiens (Human) PR
P52431 Pold1 DNA polymerase delta catalytic subunit Mus musculus (Mouse) PR
O54747 Pold1 DNA polymerase delta catalytic subunit Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MSSGGRGGKR RGAPPPGPSG AAAKRAHPGG TPQPPPPAAT AAAPVAEEED MMDEDVFLDE
70 80 90 100 110 120
TILAEDEEAL LLLDRDEALA SRLSRWRRPA LPADLASGCS RNVAFQQLEI DYVIGESHKV
130 140 150 160 170 180
LLPNSSGPAA ILRIFGVTRE GHSVCCQVHG FEPYFYISCP MGMGPDDISR FHQTLEGRMK
190 200 210 220 230 240
DSNRNSNVPR FVKRIELVQK QTIMHYQPQQ SQPFLKIVVA LPTMVASCRG ILERGITIEG
250 260 270 280 290 300
LGSKSFLTYE SNILFALRFM IDCNIVGGNW IEVPAGKYMK AARIMSYCQL ELDCLYSDLV
310 320 330 340 350 360
SHAAEGEHSK MAPFRILSFD IECAGRKGHF PEPTHDPVIQ IANLVTLQGE GQPFVRNVMT
370 380 390 400 410 420
LKSCSPIVGV DVMSFDTERD VLLAWRDFIR EVDPDIIIGY NICKFDLPYL IERAEVLKIV
430 440 450 460 470 480
EFPILGRIRN SRVRVRDTTF SSRQYGMRES KDVAVEGRVQ FDLLQAMQRD YKLSSYSLNS
490 500 510 520 530 540
VSAHFLGEQK EDVHHSIISD LQNGNSETRR RLAVYCLKDA YLPQRLLDKL MYIYNYVEMA
550 560 570 580 590 600
RVTGVPISFL LSRGQSIKVL SQLLRKAKQK NLVIPNIKGQ ASGQDTFEGA TVLEARAGFY
610 620 630 640 650 660
EKPIATLDFA SLYPSIMMAY NLCYCTLVPP EDARKLNLPP ESVNKTPSGE TFVKPDVQKG
670 680 690 700 710 720
ILPEILEELL AARKRAKADL KEAKDPFERA VLDGRQLALK ISANSVYGFT GATVGQLPCL
730 740 750 760 770 780
EISSSVTSYG RQMIEHTKKL VEDKFTTLGG YEHNAEVIYG DTDSVMVQFG VSTVEDAMKL
790 800 810 820 830 840
GREAADYISG TFIKPIKLEF EKIYFPYLLI SKKRYAGLYW TNPEKFDKMD TKGIETVRRD
850 860 870 880 890 900
NCLLVKNLVT ECLHKILVDR DVPGAVQYVK NTISDLLMNR VDLSLLVITK GLTKTGEDYA
910 920 930 940 950 960
VKAAHVELAE RMRKRDAATA PTVGDRVPYV IIKAAKGAKA YERSEDPIYV LDNNIPIDPQ
970 980 990 1000 1010 1020
YYLENQISKP LLRIFEPILK NASRELLHGS HTRAVSISTP SNSGIMKFAK KQLTCLGCKA
1030 1040 1050 1060 1070 1080
VISGSNQTLC FHCKGREAEL YCKTVGNVSE LEMLFGRLWT QCQECQGSLH QDVLCTSRDC
1090 1100
PIFYRRRKAQ KDMAEARVQL QRWDF