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

2 structures for P04819

Entry ID Method Resolution Chain Position Source
2OD8 X-ray 280 A B 32-53 PDB
AF-P04819-F1 Predicted AlphaFoldDB

9 variants for P04819

Variant ID(s) Position Change Description Diseaes Association Provenance
s04-167227 10 L>H No SGRP
s04-167183 25 S>P No SGRP
s04-167140 39 A>V No SGRP
s04-167092 55 G>D No SGRP
s04-167049 69 D>E No SGRP
s04-167026 77 E>G No SGRP
s04-166775 161 I>L No SGRP
s04-165976 427 V>A No SGRP
s04-165033 741 D>E No SGRP

No associated diseases with P04819

5 regional properties for P04819

Type Name Position InterPro Accession
domain DNA ligase, ATP-dependent, N-terminal 147 - 323 IPR012308
domain DNA ligase, ATP-dependent, C-terminal 623 - 732 IPR012309
domain DNA ligase, ATP-dependent, central 393 - 636 IPR012310
conserved_site DNA ligase, ATP-dependent, conserved site 417 - 425 IPR016059-1
conserved_site DNA ligase, ATP-dependent, conserved site 571 - 598 IPR016059-2

Functions

Description
EC Number 6.5.1.1 Forming phosphoric ester bonds
Subcellular Localization
  • [Isoform Mitochondrial]: Mitochondrion
  • ;
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA ligase (ATP) activity Catalysis of the reaction: ATP + deoxyribonucleotide(n) + deoxyribonucleotide(m) = AMP + diphosphate + deoxyribonucleotide(n+m).
metal ion binding Binding to a metal ion.

10 GO annotations of biological process

Name Definition
base-excision repair In base excision repair, an altered base is removed by a DNA glycosylase enzyme, followed by excision of the resulting sugar phosphate. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase.
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
DNA biosynthetic process The biosynthetic process resulting in the formation of DNA.
DNA ligation The re-formation of a broken phosphodiester bond in the DNA backbone, carried out by DNA ligase.
DNA recombination Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction.
lagging strand elongation The process in which an existing DNA strand is extended in a net 3' to 5' 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. Lagging strand DNA elongation proceeds by discontinuous synthesis of short stretches of DNA, known as Okazaki fragments, from RNA primers; these fragments are then joined by DNA ligase. Although each segment of nascent DNA is synthesized in the 5' to 3' direction, the overall direction of lagging strand synthesis is 3' to 5', mirroring the progress of the replication fork.
maintenance of DNA trinucleotide repeats Any process involved in sustaining the fidelity and copy number of DNA trinucleotide repeats. DNA trinucleotide repeats are naturally occurring runs of three base-pairs.
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.
nucleotide-excision repair A DNA repair process in which a small region of the strand surrounding the damage is removed from the DNA helix as an oligonucleotide. The small gap left in the DNA helix is filled in by the sequential action of DNA polymerase and DNA ligase. Nucleotide excision repair recognizes a wide range of substrates, including damage caused by UV irradiation (pyrimidine dimers and 6-4 photoproducts) and chemicals (intrastrand cross-links and bulky adducts).
Okazaki fragment processing involved in mitotic DNA replication Any DNA replication, Okazaki fragment processing that is involved in mitotic cell cycle DNA replication.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9W1H4 DNAlig1 DNA ligase 1 Drosophila melanogaster (Fruit fly) PR
P18858 LIG1 DNA ligase 1 Homo sapiens (Human) PR
P37913 Lig1 DNA ligase 1 Mus musculus (Mouse) PR
Q9JHY8 Lig1 DNA ligase 1 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MRRLLTGCLL SSARPLKSRL PLLMSSSLPS SAGKKPKQAT LARFFTSMKN KPTEGTPSPK
70 80 90 100 110 120
KSSKHMLEDR MDNVSGEEEY ATKKLKQTAV THTVAAPSSM GSNFSSIPSS APSSGVADSP
130 140 150 160 170 180
QQSQRLVGEV EDALSSNNND HYSSNIPYSE VCEVFNKIEA ISSRLEIIRI CSDFFIKIMK
190 200 210 220 230 240
QSSKNLIPTT YLFINRLGPD YEAGLELGLG ENLLMKTISE TCGKSMSQIK LKYKDIGDLG
250 260 270 280 290 300
EIAMGARNVQ PTMFKPKPLT VGEVFKNLRA IAKTQGKDSQ LKKMKLIKRM LTACKGIEAK
310 320 330 340 350 360
FLIRSLESKL RIGLAEKTVL ISLSKALLLH DENREDSPDK DVPMDVLESA QQKIRDAFCQ
370 380 390 400 410 420
VPNYEIVINS CLEHGIMNLD KYCTLRPGIP LKPMLAKPTK AINEVLDRFQ GETFTSEYKY
430 440 450 460 470 480
DGERAQVHLL NDGTMRIYSR NGENMTERYP EINITDFIQD LDTTKNLILD CEAVAWDKDQ
490 500 510 520 530 540
GKILPFQVLS TRKRKDVELN DVKVKVCLFA FDILCYNDER LINKSLKERR EYLTKVTKVV
550 560 570 580 590 600
PGEFQYATQI TTNNLDELQK FLDESVNHSC EGLMVKMLEG PESHYEPSKR SRNWLKLKKD
610 620 630 640 650 660
YLEGVGDSLD LCVLGAYYGR GKRTGTYGGF LLGCYNQDTG EFETCCKIGT GFSDEMLQLL
670 680 690 700 710 720
HDRLTPTIID GPKATFVFDS SAEPDVWFEP TTLFEVLTAD LSLSPIYKAG SATFDKGVSL
730 740 750
RFPRFLRIRE DKGVEDATSS DQIVELYENQ SHMQN