XPF-like nuclease domain of DNA excision repair protein ERCC1; ERCC1 is a non-catalytic ...
140-254
1.05e-86
XPF-like nuclease domain of DNA excision repair protein ERCC1; ERCC1 is a non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. In conjunction with SLX4, ERCC1 is responsible for the first step in the repair of interstrand cross-links (ICL), as well as for homology-directed repair (HDR) of DNA double-strand breaks. ERCC1 participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. ERCC1 also plays a critical role in targeting the XPF-ERCC1 complex to DNA. XPF-ERRC1 and its yeast homolog Rad1-Rad10 play key roles in the excision of DNA lesions and are required for certain types of homologous recombination events and for the repair of DNA cross-links. The critical motif, DX(n)ERKX(3)D, for endonuclease activity is absent in the nuclease domain of ERCC1.
:
Pssm-ID: 410855 Cd Length: 115 Bit Score: 270.01 E-value: 1.05e-86
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
657-807
1.45e-39
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
:
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 146.27 E-value: 1.45e-39
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
372-524
9.02e-39
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
:
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 143.96 E-value: 9.02e-39
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
545-645
2.69e-12
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
The actual alignment was detected with superfamily member cd00190:
Pssm-ID: 473915 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 2.69e-12
XPF-like nuclease domain of DNA excision repair protein ERCC1; ERCC1 is a non-catalytic ...
140-254
1.05e-86
XPF-like nuclease domain of DNA excision repair protein ERCC1; ERCC1 is a non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. In conjunction with SLX4, ERCC1 is responsible for the first step in the repair of interstrand cross-links (ICL), as well as for homology-directed repair (HDR) of DNA double-strand breaks. ERCC1 participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. ERCC1 also plays a critical role in targeting the XPF-ERCC1 complex to DNA. XPF-ERRC1 and its yeast homolog Rad1-Rad10 play key roles in the excision of DNA lesions and are required for certain types of homologous recombination events and for the repair of DNA cross-links. The critical motif, DX(n)ERKX(3)D, for endonuclease activity is absent in the nuclease domain of ERCC1.
Pssm-ID: 410855 Cd Length: 115 Bit Score: 270.01 E-value: 1.05e-86
Binding domain of DNA repair protein Ercc1 (rad10/Swi10); Ercc1 and XPF (xeroderma pigmentosum ...
140-253
3.65e-73
Binding domain of DNA repair protein Ercc1 (rad10/Swi10); Ercc1 and XPF (xeroderma pigmentosum group F-complementing protein) are two structure-specific endonucleases of a class of seven containing an ERCC4 domain. Together they form an obligate complex that functions primarily in nucleotide excision repair (NER), a versatile pathway able to detect and remove a variety of DNA lesions induced by UV light and environmental carcinogens, and secondarily in DNA interstrand cross-link repair and telomere maintenance. This domain in fact binds simultaneously to both XPF and single-stranded DNA; this ternary complex explains the important role of Ercc1 in targeting its catalytic XPF partner to the NER pre-incision complex.
Pssm-ID: 461070 Cd Length: 114 Bit Score: 233.91 E-value: 3.65e-73
DNA repair protein rad10; All proteins in this family for which functions are known are ...
139-250
1.35e-56
DNA repair protein rad10; All proteins in this family for which functions are known are components in a multiprotein endonuclease complex (usually made up of Rad1 and Rad10 homologs). This complex is used primarily for nucleotide excision repair but also for some aspects of recombination repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129685 Cd Length: 112 Bit Score: 189.28 E-value: 1.35e-56
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
657-807
1.45e-39
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 146.27 E-value: 1.45e-39
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
372-524
9.02e-39
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 143.96 E-value: 9.02e-39
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
657-807
1.68e-38
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 142.82 E-value: 1.68e-38
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
372-518
1.91e-35
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 134.34 E-value: 1.91e-35
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
545-645
2.69e-12
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 2.69e-12
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
545-645
1.15e-09
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 59.23 E-value: 1.15e-09
XPF-like nuclease domain of DNA excision repair protein ERCC1; ERCC1 is a non-catalytic ...
140-254
1.05e-86
XPF-like nuclease domain of DNA excision repair protein ERCC1; ERCC1 is a non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. In conjunction with SLX4, ERCC1 is responsible for the first step in the repair of interstrand cross-links (ICL), as well as for homology-directed repair (HDR) of DNA double-strand breaks. ERCC1 participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. ERCC1 also plays a critical role in targeting the XPF-ERCC1 complex to DNA. XPF-ERRC1 and its yeast homolog Rad1-Rad10 play key roles in the excision of DNA lesions and are required for certain types of homologous recombination events and for the repair of DNA cross-links. The critical motif, DX(n)ERKX(3)D, for endonuclease activity is absent in the nuclease domain of ERCC1.
Pssm-ID: 410855 Cd Length: 115 Bit Score: 270.01 E-value: 1.05e-86
Central domain of ERCC1; ERCC1 is a subunit of the DNA structure-specific endonuclease ...
139-266
4.97e-86
Central domain of ERCC1; ERCC1 is a subunit of the DNA structure-specific endonuclease XPF-ERCC1, which incises a damaged DNA strand on the 5' side of a lesion during nucleotide excision repair. It also plays roles in DNA interstrand crosslink repair and homologous recombination. The ERCC1 central domain modeled here interacts tightly with XPF and may be involved in binding to single-stranded DNA. It belongs to a superfamily of nucleases including very short patch repair (Vsr) endonucleases, archaeal Holliday junction resolvases, MutH methyl-directed DNA mismatch-repair endonucleases, and catalytic domains of many restriction endonucleases, such as EcoRI, BamHI, and FokI.
Pssm-ID: 411729 Cd Length: 128 Bit Score: 268.61 E-value: 4.97e-86
Binding domain of DNA repair protein Ercc1 (rad10/Swi10); Ercc1 and XPF (xeroderma pigmentosum ...
140-253
3.65e-73
Binding domain of DNA repair protein Ercc1 (rad10/Swi10); Ercc1 and XPF (xeroderma pigmentosum group F-complementing protein) are two structure-specific endonucleases of a class of seven containing an ERCC4 domain. Together they form an obligate complex that functions primarily in nucleotide excision repair (NER), a versatile pathway able to detect and remove a variety of DNA lesions induced by UV light and environmental carcinogens, and secondarily in DNA interstrand cross-link repair and telomere maintenance. This domain in fact binds simultaneously to both XPF and single-stranded DNA; this ternary complex explains the important role of Ercc1 in targeting its catalytic XPF partner to the NER pre-incision complex.
Pssm-ID: 461070 Cd Length: 114 Bit Score: 233.91 E-value: 3.65e-73
DNA repair protein rad10; All proteins in this family for which functions are known are ...
139-250
1.35e-56
DNA repair protein rad10; All proteins in this family for which functions are known are components in a multiprotein endonuclease complex (usually made up of Rad1 and Rad10 homologs). This complex is used primarily for nucleotide excision repair but also for some aspects of recombination repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129685 Cd Length: 112 Bit Score: 189.28 E-value: 1.35e-56
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
657-807
1.45e-39
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 146.27 E-value: 1.45e-39
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
372-524
9.02e-39
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 143.96 E-value: 9.02e-39
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
657-807
1.68e-38
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 142.82 E-value: 1.68e-38
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
372-518
1.91e-35
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 134.34 E-value: 1.91e-35
nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap ...
140-253
8.20e-28
nuclease domain of XPF/MUS81 family proteins; The XPF/MUS81 family belongs to 3'-flap endonuclease that act upon 3'-flap structures and involved in DNA repair pathways that are necessary for the removal of UV-light-induced DNA lesions and cross-links between DNA strands. Family members exist either as heterodimers or as homodimers in their functionally competent states which consist of a catalytic and a noncatalytic subunit. The catalytic subunits have a DX(n)RKX(3)D motif. This motif is required for metal-dependent endonuclease activity but not for DNA junction binding. The equivalent regions of the noncatalytic subunits (ERCC1, EME1, and FAAP24) have diverged. The noncatalytic subunits have roles such as binding ssDNA or an ability to target the endonuclease to defined DNA structures or sites of DNA damage.
Pssm-ID: 410849 [Multi-domain] Cd Length: 126 Bit Score: 108.62 E-value: 8.20e-28
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
545-645
2.69e-12
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.
Pssm-ID: 238113 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 2.69e-12
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
545-645
1.15e-09
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.
Pssm-ID: 214473 Cd Length: 229 Bit Score: 59.23 E-value: 1.15e-09
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated ...
299-323
3.69e-03
Helix-hairpin-helix motif; The helix-hairpin-helix DNA-binding motif is found to be duplicated in the central domain of RuvA. The HhH domain of DisA, a bacterial checkpoint control protein, is a DNA-binding domain.
Pssm-ID: 425789 [Multi-domain] Cd Length: 30 Bit Score: 35.47 E-value: 3.69e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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