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 Q6FVD8

Entry ID Method Resolution Chain Position Source
AF-Q6FVD8-F1 Predicted AlphaFoldDB

No variants for Q6FVD8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6FVD8

No associated diseases with Q6FVD8

6 regional properties for Q6FVD8

Type Name Position InterPro Accession
domain BRCT domain 688 - 787 IPR001357-1
domain BRCT domain 847 - 945 IPR001357-2
domain DNA ligase, ATP-dependent, N-terminal 34 - 229 IPR012308
domain DNA ligase, ATP-dependent, central 271 - 513 IPR012310
conserved_site DNA ligase, ATP-dependent, conserved site 295 - 303 IPR016059
domain DNA Ligase 4, adenylation domain 258 - 486 IPR044125

Functions

Description
EC Number 6.5.1.1 Forming phosphoric ester bonds
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
DNA ligase IV complex A eukaryotically conserved protein complex that contains DNA ligase IV and is involved in DNA repair by non-homologous end joining; in addition to the ligase, the complex also contains XRCC4 or a homolog, e.g. Saccharomyces Lif1p.

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.

5 GO annotations of biological process

Name Definition
DNA biosynthetic process The biosynthetic process resulting in the formation of DNA.
DNA ligation involved in DNA repair The re-formation of a broken phosphodiester bond in the DNA backbone, carried out by DNA ligase, that contributes to DNA repair.
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.
DNA replication The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MADEGGLETG AHDELKGTEE QAVNFAPSPD FLWLCEQLFA KIDHVQFERA NNLLTKPVTA
70 80 90 100 110 120
RYYEVISNFT TLWRTTVGNN IYPALRLILP YRDRRVFNIK DYTLIKAICA FLKLPKDSST
130 140 150 160 170 180
EKKLINWKQD AGRSVRLSKF CVEEIKKRRS EPQIDRNERI TIDDLNGYLD QLAIERTEQG
190 200 210 220 230 240
RSFKNLANSD IMNKCLTSMT FLEMQYFFDI LLKNRPLGGH EHKLLNCWHP DAQDYLSVVS
250 260 270 280 290 300
DLETVAKRLW DPSQRLGNQD LKINIGLAFA PQLATKLHVS YQKIGEKLGW DFFIEEKMDG
310 320 330 340 350 360
ERIQMHYTNF GSDIKFYSRR ATDYTYLYGN NLKTGTLANF INLNKNVKDC VLDCEVVTFD
370 380 390 400 410 420
SNNKIVLPFG MVKSSAKNML SQDGIDTQGF HPLLMVFDVL YLNGATLVDL PYYKRREYLK
430 440 450 460 470 480
QILTPTAHRI EIIKSIRAND EQMIKKSLEK ALSVGSEGII LKRYDSRYVI ASRSDDWIKI
490 500 510 520 530 540
KPEYLEQFGE NMDLVLMGRD PSKKDSLMLG LLDYEEVIQD SPIMVNSQSS EENSQRFRGF
550 560 570 580 590 600
VSLCIIANGI SNEEYKEIDR KTKGLWNDSE KIPPLEYMKF GSKVPRQWID PKKSLILEIK
610 620 630 640 650 660
ARSLDNTRSS ERKFAAGCTL FGGYCRQIRE DKNWKTCYTL QEFERAKSGN NWRKRGSSKP
670 680 690 700 710 720
QKVISKKRRY NIISSVNKAL EDFAELEHRS DIFDGMYFYV LSDYFDGVKR KRIKKSEIQK
730 740 750 760 770 780
VIVANGGQLV QNVITRNYNL NDLRIISSRN TVECNSLIVR GYDIISPKWV FDCLLSGKIM
790 800 810 820 830 840
KLEPSHCFNF SKQLMDYAYK RIDQYGDPYE RDINKYEWSS LTSEKICTTA KQQPDVQFDN
850 860 870 880 890 900
SLMDVPHFLF HGRIVFLLSD NNNIQKESFM VDAYGGKVTN ELSSANLVIV VGAVTQRRIN
910 920 930 940
DIRKQISSEV IKQDHPPRIP DMVSEGWLYD CIKQNTQVAE DNYRLP