BRCA1-associated RING domain protein 1 isoform 2 [Homo sapiens]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
BRCT_Bard1_rpt2 | cd17720 | second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ... |
652-752 | 3.23e-45 | |||
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain. : Pssm-ID: 349352 Cd Length: 101 Bit Score: 156.75 E-value: 3.23e-45
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ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
405-514 | 1.09e-36 | |||
Ankyrin repeat [Signal transduction mechanisms]; : Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 139.70 E-value: 1.09e-36
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BRCT_Bard1_rpt1 | cd17734 | first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ... |
551-627 | 8.33e-30 | |||
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain. : Pssm-ID: 349366 Cd Length: 80 Bit Score: 112.69 E-value: 8.33e-30
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RING_Ubox super family | cl17238 | RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger ... |
33-99 | 1.08e-29 | |||
RING finger (Really Interesting New Gene) domain and U-box domain superfamily; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type RING fingers are closely related to RING-HC fingers. In contrast, C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type RING fingers are more closely related to RING-H2 fingers. However, not all RING finger-containing proteins display regular RING finger features, and the RING finger family has turned out to be multifarious. The degenerate RING fingers of the Siz/PIAS RING (SP-RING) family proteins and sporulation protein RMD5, are characterized by lacking the second, fifth, and sixth Zn2+ ion-coordinating residues. They bind only one Zn2+ ion. On the other hand, the RING fingers of the human APC11 and RBX1 proteins can bind a third Zn atom since they harbor four additional Zn ligands. U-box is a modified form of the RING finger domain that lacks metal chelating Cys and His residues. It resembles the cross-brace RING structure consisting of three beta-sheets and a single alpha-helix, which would be stabilized by salt bridges instead of chelated metal ions. U-box proteins are widely distributed among eukaryotic organisms and show a higher prevalence in plants than in other organisms. RING finger/U-box-containing proteins are a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enable efficient transfer of ubiquitin from E2 to the substrates. The actual alignment was detected with superfamily member cd16496: Pssm-ID: 473075 [Multi-domain] Cd Length: 86 Bit Score: 112.43 E-value: 1.08e-29
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Name | Accession | Description | Interval | E-value | |||
BRCT_Bard1_rpt2 | cd17720 | second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ... |
652-752 | 3.23e-45 | |||
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain. Pssm-ID: 349352 Cd Length: 101 Bit Score: 156.75 E-value: 3.23e-45
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ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
405-514 | 1.09e-36 | |||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 139.70 E-value: 1.09e-36
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BRCT_Bard1_rpt1 | cd17734 | first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ... |
551-627 | 8.33e-30 | |||
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain. Pssm-ID: 349366 Cd Length: 80 Bit Score: 112.69 E-value: 8.33e-30
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RING-HC_BARD1 | cd16496 | RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ... |
33-99 | 1.08e-29 | |||
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar proteins; BARD-1 is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an C3HC4-type RING-HC finger that binds BRCA1 at its N-terminus and three tandem ankyrin repeats and tandem BRCT repeat domains at its C-terminus. The BRCT repeats bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. Pssm-ID: 438159 [Multi-domain] Cd Length: 86 Bit Score: 112.43 E-value: 1.08e-29
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Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
413-505 | 2.49e-27 | |||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 105.97 E-value: 2.49e-27
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zf-RING_6 | pfam14835 | zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer ... |
41-86 | 6.14e-19 | |||
zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer tumour-suppressor BRCA1 interacts with multiple cognate proteins, including the RING protein BARD1. Proper function of the BRCA1 RING domain is critical, as evidenced by the many cancer-predisposing mutations found within this domain. A dimer is formed between the RING domains of BRCA1 and BARD1. The BRCA1-BARD1 structure provides a model for its ubiquitin ligase activity, illustrates how the BRCA1 RING domain can be involved in associations with multiple protein partners and provides a framework for understanding cancer-causing mutations at the molecular level. The corresponding BRCA1-RING domain is on family zf-C3HC4_2, pfam13923. Pssm-ID: 434253 [Multi-domain] Cd Length: 65 Bit Score: 81.25 E-value: 6.14e-19
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PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
389-505 | 2.45e-15 | |||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 78.94 E-value: 2.45e-15
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BRCT | smart00292 | breast cancer carboxy-terminal domain; |
552-621 | 4.27e-10 | |||
breast cancer carboxy-terminal domain; Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 56.61 E-value: 4.27e-10
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ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
442-469 | 1.31e-06 | |||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 45.27 E-value: 1.31e-06
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TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
410-500 | 3.71e-06 | |||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 50.40 E-value: 3.71e-06
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BRCT | smart00292 | breast cancer carboxy-terminal domain; |
650-748 | 2.57e-05 | |||
breast cancer carboxy-terminal domain; Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 43.13 E-value: 2.57e-05
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BRCT_2 | pfam16589 | BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ... |
649-757 | 1.60e-04 | |||
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown. Pssm-ID: 465186 [Multi-domain] Cd Length: 84 Bit Score: 40.81 E-value: 1.60e-04
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BRCT | pfam00533 | BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
556-621 | 1.64e-04 | |||
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants. Pssm-ID: 425736 [Multi-domain] Cd Length: 75 Bit Score: 40.74 E-value: 1.64e-04
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Name | Accession | Description | Interval | E-value | ||||
BRCT_Bard1_rpt2 | cd17720 | second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar ... |
652-752 | 3.23e-45 | ||||
second (C-terminal) BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the second BRCT domain. Pssm-ID: 349352 Cd Length: 101 Bit Score: 156.75 E-value: 3.23e-45
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ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
405-514 | 1.09e-36 | ||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 139.70 E-value: 1.09e-36
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ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
405-524 | 2.89e-33 | ||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 129.69 E-value: 2.89e-33
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BRCT_Bard1_rpt1 | cd17734 | first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ... |
551-627 | 8.33e-30 | ||||
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; Bard1, also termed BARD-1, or RING-type E3 ubiquitin transferase BARD1, is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an N-terminal C3HC4-type RING-HC finger that binds BRCA1, and a C-terminal region with three ankyrin repeats and tandem BRCT domains that bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. The family corresponds to the first BRCT domain. Pssm-ID: 349366 Cd Length: 80 Bit Score: 112.69 E-value: 8.33e-30
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RING-HC_BARD1 | cd16496 | RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ... |
33-99 | 1.08e-29 | ||||
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar proteins; BARD-1 is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an C3HC4-type RING-HC finger that binds BRCA1 at its N-terminus and three tandem ankyrin repeats and tandem BRCT repeat domains at its C-terminus. The BRCT repeats bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage. Pssm-ID: 438159 [Multi-domain] Cd Length: 86 Bit Score: 112.43 E-value: 1.08e-29
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ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
405-514 | 1.81e-29 | ||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.90 E-value: 1.81e-29
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Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
413-505 | 2.49e-27 | ||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 105.97 E-value: 2.49e-27
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ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
394-511 | 1.30e-22 | ||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 98.87 E-value: 1.30e-22
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ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
405-510 | 7.50e-20 | ||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 90.78 E-value: 7.50e-20
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zf-RING_6 | pfam14835 | zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer ... |
41-86 | 6.14e-19 | ||||
zf-RING of BARD1-type protein; The RING domain of the breast and ovarian cancer tumour-suppressor BRCA1 interacts with multiple cognate proteins, including the RING protein BARD1. Proper function of the BRCA1 RING domain is critical, as evidenced by the many cancer-predisposing mutations found within this domain. A dimer is formed between the RING domains of BRCA1 and BARD1. The BRCA1-BARD1 structure provides a model for its ubiquitin ligase activity, illustrates how the BRCA1 RING domain can be involved in associations with multiple protein partners and provides a framework for understanding cancer-causing mutations at the molecular level. The corresponding BRCA1-RING domain is on family zf-C3HC4_2, pfam13923. Pssm-ID: 434253 [Multi-domain] Cd Length: 65 Bit Score: 81.25 E-value: 6.14e-19
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PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
389-505 | 2.45e-15 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 78.94 E-value: 2.45e-15
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PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
405-498 | 7.74e-14 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 74.23 E-value: 7.74e-14
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Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
405-471 | 1.02e-13 | ||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.06 E-value: 1.02e-13
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Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
411-462 | 1.36e-13 | ||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 65.76 E-value: 1.36e-13
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Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
442-495 | 3.50e-13 | ||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 64.60 E-value: 3.50e-13
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PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
412-497 | 2.20e-12 | ||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 70.31 E-value: 2.20e-12
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BRCT | cd00027 | C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
551-620 | 7.17e-12 | ||||
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage. Pssm-ID: 349339 [Multi-domain] Cd Length: 68 Bit Score: 61.22 E-value: 7.17e-12
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PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
403-526 | 1.15e-11 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 67.60 E-value: 1.15e-11
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ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
394-525 | 1.31e-11 | ||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 66.13 E-value: 1.31e-11
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PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
385-513 | 2.09e-11 | ||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 66.97 E-value: 2.09e-11
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PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
417-515 | 5.36e-11 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 65.67 E-value: 5.36e-11
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BRCT_BRCA1_rpt1 | cd17735 | first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; ... |
553-634 | 6.95e-11 | ||||
first BRCT domain of breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also termed RING finger protein 53 (RNF53), is a RING finger protein encoded by BRCA1, a tumor suppressor gene that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling, and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus. The family corresponds to the first BRCT domain. Pssm-ID: 349367 Cd Length: 97 Bit Score: 59.28 E-value: 6.95e-11
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BRCT_microcephalin_rpt2 | cd17736 | second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage ... |
552-622 | 7.86e-11 | ||||
second BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA damage response protein involved in regulation of CHK1 and BRCA1. It has been implicated in chromosome condensation and DNA damage induced cellular responses. It may play a role in neurogenesis and regulation of the size of the cerebral cortex. Microcephalin contains three BRCT repeats. This family corresponds to the second repeat. Pssm-ID: 349368 [Multi-domain] Cd Length: 76 Bit Score: 58.37 E-value: 7.86e-11
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PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
411-516 | 1.38e-10 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.92 E-value: 1.38e-10
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PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
404-514 | 1.56e-10 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.92 E-value: 1.56e-10
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BRCT | smart00292 | breast cancer carboxy-terminal domain; |
552-621 | 4.27e-10 | ||||
breast cancer carboxy-terminal domain; Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 56.61 E-value: 4.27e-10
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PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
413-512 | 4.30e-10 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 62.59 E-value: 4.30e-10
|
||||||||
PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
408-511 | 1.19e-09 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 61.16 E-value: 1.19e-09
|
||||||||
PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
393-524 | 5.17e-09 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 59.21 E-value: 5.17e-09
|
||||||||
PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
391-505 | 6.26e-09 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 59.31 E-value: 6.26e-09
|
||||||||
Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
461-514 | 2.27e-08 | ||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 50.81 E-value: 2.27e-08
|
||||||||
PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
405-513 | 4.42e-08 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 56.13 E-value: 4.42e-08
|
||||||||
PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
411-504 | 4.49e-08 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.15 E-value: 4.49e-08
|
||||||||
PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
421-499 | 5.07e-08 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.77 E-value: 5.07e-08
|
||||||||
PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
410-524 | 5.16e-08 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 55.77 E-value: 5.16e-08
|
||||||||
Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
397-439 | 3.19e-07 | ||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 48.96 E-value: 3.19e-07
|
||||||||
Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
405-449 | 4.51e-07 | ||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.34 E-value: 4.51e-07
|
||||||||
PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
405-464 | 7.97e-07 | ||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.59 E-value: 7.97e-07
|
||||||||
PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
422-514 | 8.14e-07 | ||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 52.33 E-value: 8.14e-07
|
||||||||
PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
412-502 | 1.02e-06 | ||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.18 E-value: 1.02e-06
|
||||||||
PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
424-523 | 1.03e-06 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 51.97 E-value: 1.03e-06
|
||||||||
ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
442-469 | 1.31e-06 | ||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 45.27 E-value: 1.31e-06
|
||||||||
Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
442-469 | 1.43e-06 | ||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 45.36 E-value: 1.43e-06
|
||||||||
PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
410-525 | 1.80e-06 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 51.60 E-value: 1.80e-06
|
||||||||
PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
413-514 | 2.53e-06 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 50.73 E-value: 2.53e-06
|
||||||||
Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
476-505 | 3.66e-06 | ||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 44.20 E-value: 3.66e-06
|
||||||||
TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
410-500 | 3.71e-06 | ||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 50.40 E-value: 3.71e-06
|
||||||||
ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
474-503 | 4.12e-06 | ||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 43.73 E-value: 4.12e-06
|
||||||||
PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
420-524 | 5.29e-06 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.58 E-value: 5.29e-06
|
||||||||
PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
408-563 | 8.79e-06 | ||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 49.48 E-value: 8.79e-06
|
||||||||
TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
409-508 | 9.21e-06 | ||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 49.24 E-value: 9.21e-06
|
||||||||
Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
475-514 | 1.12e-05 | ||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 1.12e-05
|
||||||||
PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
405-512 | 1.31e-05 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 48.52 E-value: 1.31e-05
|
||||||||
Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
442-470 | 1.88e-05 | ||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 41.86 E-value: 1.88e-05
|
||||||||
PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
409-527 | 2.30e-05 | ||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 47.71 E-value: 2.30e-05
|
||||||||
BRCT | smart00292 | breast cancer carboxy-terminal domain; |
650-748 | 2.57e-05 | ||||
breast cancer carboxy-terminal domain; Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 43.13 E-value: 2.57e-05
|
||||||||
Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
428-480 | 3.56e-05 | ||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.95 E-value: 3.56e-05
|
||||||||
PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
416-504 | 5.73e-05 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.14 E-value: 5.73e-05
|
||||||||
Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
408-440 | 5.77e-05 | ||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 5.77e-05
|
||||||||
PHA02946 | PHA02946 | ankyin-like protein; Provisional |
418-521 | 7.43e-05 | ||||
ankyin-like protein; Provisional Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 45.82 E-value: 7.43e-05
|
||||||||
BRCT_2 | pfam16589 | BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found ... |
649-757 | 1.60e-04 | ||||
BRCT domain, a BRCA1 C-terminus domain; This BRCT domain, a BRCA1 C-terminus region, is found on many RAP1 proteins, usually at the very N-terminus. The function in human at least of a BRCT is to contribute to the heterogeneity of the telomere DNA length, but that may not be its general function, which remains unknown. Pssm-ID: 465186 [Multi-domain] Cd Length: 84 Bit Score: 40.81 E-value: 1.60e-04
|
||||||||
Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
479-511 | 1.62e-04 | ||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 41.25 E-value: 1.62e-04
|
||||||||
BRCT | pfam00533 | BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
556-621 | 1.64e-04 | ||||
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants. Pssm-ID: 425736 [Multi-domain] Cd Length: 75 Bit Score: 40.74 E-value: 1.64e-04
|
||||||||
Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
408-437 | 1.68e-04 | ||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.16 E-value: 1.68e-04
|
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BRCT_TopBP1_rpt7 | cd17738 | seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA ... |
556-622 | 2.62e-04 | ||||
seventh BRCT domain of DNA topoisomerase 2-binding protein 1; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the seventh BRCT domain. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is missing in this group. Pssm-ID: 349370 [Multi-domain] Cd Length: 75 Bit Score: 39.86 E-value: 2.62e-04
|
||||||||
BRCT_nibrin | cd17741 | BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage ... |
550-622 | 3.52e-04 | ||||
BRCT domain of nibrin and similar proteins; Nibrin (NBN), also termed Nijmegen breakage syndrome protein 1 (NBS1), or cell cycle regulatory protein p95, is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The BRCT (Breast Cancer Suppressor Protein BRCA1, carboxy-terminal) domain is found within many DNA damage repair and cell cycle checkpoint proteins. The unique diversity of this domain superfamily allows BRCT modules to interact forming homo/hetero BRCT multimers, BRCT-non-BRCT interactions, and interactions within DNA strand breaks. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is absent in this group. Pssm-ID: 349372 [Multi-domain] Cd Length: 74 Bit Score: 39.51 E-value: 3.52e-04
|
||||||||
ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
408-437 | 7.92e-04 | ||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 7.92e-04
|
||||||||
PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
413-578 | 1.24e-03 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 42.17 E-value: 1.24e-03
|
||||||||
PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
405-496 | 1.39e-03 | ||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 41.79 E-value: 1.39e-03
|
||||||||
PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
405-462 | 1.86e-03 | ||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 41.55 E-value: 1.86e-03
|
||||||||
BRCT_CTDP1 | cd17729 | BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ... |
566-627 | 2.68e-03 | ||||
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar proteins; CTDP1 (EC 3.1.3.16), also termed TFIIF-associating CTD phosphatase, or TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1), promotes the activity of RNA polymerase II through processively dephosphorylating 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. It plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation. Pssm-ID: 349361 [Multi-domain] Cd Length: 97 Bit Score: 37.90 E-value: 2.68e-03
|
||||||||
Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
477-503 | 3.37e-03 | ||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.70 E-value: 3.37e-03
|
||||||||
PHA02716 | PHA02716 | CPXV016; CPX019; EVM010; Provisional |
421-512 | 6.51e-03 | ||||
CPXV016; CPX019; EVM010; Provisional Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 39.90 E-value: 6.51e-03
|
||||||||
PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
455-514 | 9.48e-03 | ||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 39.24 E-value: 9.48e-03
|
||||||||
Blast search parameters | ||||
|