protein serine/threonine phosphatase [Saccharomyces cerevisiae S288C]
Protein Classification
HAD_FCP1-like and BRCT_CTDP1 domain-containing protein( domain architecture ID 13089339)
HAD_FCP1-like and BRCT_CTDP1 domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| FCP1_euk | TIGR02250 | FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ... |
169-345 | 8.01e-79 | ||||
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the humanRNA polymerase II subunit A C-terminal domain phosphatase (FCP1) and closely related phosphatases from eukaryotes including plants, fungi, and slime mold. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDDppphW). This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in the human NLI interacting factor-like phosphatases, and together both are detected by the pfam03031. : Pssm-ID: 131304 Cd Length: 156 Bit Score: 249.12 E-value: 8.01e-79
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| BRCT_CTDP1 | cd17729 | BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ... |
491-588 | 6.14e-38 | ||||
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: 136.12 E-value: 6.14e-38
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| Biotinyl_lipoyl_domains super family | cl11404 | Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the ... |
88-112 | 5.16e-03 | ||||
Biotinyl_lipoyl_domains are present in biotin-dependent carboxylases/decarboxylases, the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases, and the H-protein of the glycine cleavage system (GCS). These domains transport CO2, acyl, or methylamine, respectively, between components of the complex/protein via a biotinyl or lipoyl group, which is covalently attached to a highly conserved lysine residue. The actual alignment was detected with superfamily member cd06849: Pssm-ID: 448245 [Multi-domain] Cd Length: 74 Bit Score: 36.23 E-value: 5.16e-03
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| Name | Accession | Description | Interval | E-value | ||||
| FCP1_euk | TIGR02250 | FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ... |
169-345 | 8.01e-79 | ||||
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the humanRNA polymerase II subunit A C-terminal domain phosphatase (FCP1) and closely related phosphatases from eukaryotes including plants, fungi, and slime mold. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDDppphW). This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in the human NLI interacting factor-like phosphatases, and together both are detected by the pfam03031. Pssm-ID: 131304 Cd Length: 156 Bit Score: 249.12 E-value: 8.01e-79
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| CPDc | smart00577 | catalytic domain of ctd-like phosphatases; |
173-349 | 1.55e-43 | ||||
catalytic domain of ctd-like phosphatases; Pssm-ID: 214729 Cd Length: 148 Bit Score: 153.92 E-value: 1.55e-43
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| HAD_FCP1-like | cd07521 | human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ... |
174-339 | 6.51e-41 | ||||
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319823 Cd Length: 134 Bit Score: 145.82 E-value: 6.51e-41
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| BRCT_CTDP1 | cd17729 | BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ... |
491-588 | 6.14e-38 | ||||
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: 136.12 E-value: 6.14e-38
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| NIF | pfam03031 | NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ... |
175-358 | 1.94e-24 | ||||
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain. Pssm-ID: 397254 Cd Length: 160 Bit Score: 100.00 E-value: 1.94e-24
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| BRCT | pfam00533 | BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
500-580 | 2.71e-13 | ||||
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: 65.39 E-value: 2.71e-13
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| BRCT | smart00292 | breast cancer carboxy-terminal domain; |
502-580 | 1.83e-10 | ||||
breast cancer carboxy-terminal domain; Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 57.39 E-value: 1.83e-10
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| lipoyl_domain | cd06849 | Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
88-112 | 5.16e-03 | ||||
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue. Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 36.23 E-value: 5.16e-03
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| AceF | COG0508 | Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
84-112 | 5.89e-03 | ||||
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 36.20 E-value: 5.89e-03
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| Name | Accession | Description | Interval | E-value | ||||
| FCP1_euk | TIGR02250 | FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ... |
169-345 | 8.01e-79 | ||||
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the humanRNA polymerase II subunit A C-terminal domain phosphatase (FCP1) and closely related phosphatases from eukaryotes including plants, fungi, and slime mold. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDDppphW). This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in the human NLI interacting factor-like phosphatases, and together both are detected by the pfam03031. Pssm-ID: 131304 Cd Length: 156 Bit Score: 249.12 E-value: 8.01e-79
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| CPDc | smart00577 | catalytic domain of ctd-like phosphatases; |
173-349 | 1.55e-43 | ||||
catalytic domain of ctd-like phosphatases; Pssm-ID: 214729 Cd Length: 148 Bit Score: 153.92 E-value: 1.55e-43
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| HAD_FCP1-like | cd07521 | human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ... |
174-339 | 6.51e-41 | ||||
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid dehalogenase-like superfamily; Human CTDP1/FCP1 is a protein phosphatase which dephosphorylates the phosphorylated C terminus (CTD) of RNA polymerase II. CTD phosphorylation is a key mechanism of regulation of gene expression in eukaryotes. CTDP1/FCP1 may have other roles in in transcription regulation independent of its phosphatase activity. This family also includes human translocase of inner mitochondrial membrane 50 (TIMM50), CTD small phosphatase like (CTDSPL) and CTD small phosphatase like 2 (CTDSPL2), Saccharomyces cerevisiae (nuclear envelope morphology protein 1) Nem1p, and Xenopus Dullard. Yeast Nem1p in complex with Spo7p dephosphorylates the nuclear membrane-associated phosphatidic acid phosphatase, Smp2p, which may be part of a signaling cascade playing a role in nuclear membrane biogenesis. Xenopus Dullard is a potential regulator of neural tube development. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319823 Cd Length: 134 Bit Score: 145.82 E-value: 6.51e-41
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| BRCT_CTDP1 | cd17729 | BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ... |
491-588 | 6.14e-38 | ||||
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: 136.12 E-value: 6.14e-38
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| NIF | pfam03031 | NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ... |
175-358 | 1.94e-24 | ||||
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting factor isoforms and also an N-terminal regions of RNA polymerase II CTC phosphatase and FCP1 serine phosphatase. This region has been identified as the minimal phosphatase domain. Pssm-ID: 397254 Cd Length: 160 Bit Score: 100.00 E-value: 1.94e-24
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| BRCT | pfam00533 | BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ... |
500-580 | 2.71e-13 | ||||
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: 65.39 E-value: 2.71e-13
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| HIF-SF_euk | TIGR02251 | Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ... |
174-325 | 5.12e-12 | ||||
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a family of eukaryotic proteins including "Dullard", and the NLI interacting factor (NIF)-like phosphatases. This domain is a member of the haloacid dehalogenase (HAD) superfamily by virtue of a conserved set of three catalytic motifs and a conserved fold as predicted by PSIPRED. The third motif in this family is distinctive (hhhhDNxPxxa) and aparrently lacking the last aspartate. This domain is classified as a "Class III" HAD, since there is no large "cap" domain found between motifs 1 and 2 or motifs 2 and 3. This domain is related to domains found in FCP1-like phosphatases (TIGR02250), and together both are detected by the pfam03031. Pssm-ID: 274055 Cd Length: 162 Bit Score: 64.62 E-value: 5.12e-12
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| BRCT | cd00027 | C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ... |
507-579 | 5.33e-11 | ||||
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: 58.53 E-value: 5.33e-11
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| BRCT | smart00292 | breast cancer carboxy-terminal domain; |
502-580 | 1.83e-10 | ||||
breast cancer carboxy-terminal domain; Pssm-ID: 214602 [Multi-domain] Cd Length: 78 Bit Score: 57.39 E-value: 1.83e-10
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| BRCT_PAXIP1_rpt2 | cd17710 | second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ... |
510-588 | 1.12e-08 | ||||
second BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the second BRCT domain. Pssm-ID: 349342 [Multi-domain] Cd Length: 81 Bit Score: 52.62 E-value: 1.12e-08
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| BRCT_TopBP1_rpt2_like | cd17731 | second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
502-580 | 1.31e-08 | ||||
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; 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 second BRCT domain. Pssm-ID: 349363 [Multi-domain] Cd Length: 77 Bit Score: 52.16 E-value: 1.31e-08
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| BRCT_Rev1 | cd17719 | BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha ... |
545-593 | 2.42e-08 | ||||
BRCT domain of DNA repair protein Rev1 and similar proteins; REV1, also termed alpha integrin-binding protein 80, or AIBP80, or Rev1-like terminal deoxycytidyl transferase, is a DNA template-dependent dCMP transferase required for mutagenesis induced by UV light. Pssm-ID: 349351 [Multi-domain] Cd Length: 87 Bit Score: 51.80 E-value: 2.42e-08
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| BRCT_XRCC1_rpt1 | cd17725 | First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar ... |
507-591 | 2.47e-07 | ||||
First (central) BRCT domain in X-ray repair cross-complementing protein 1 (XRCC1) and similar proteins; XRCC1 is a DNA repair protein that corrects defective DNA strand-break repair and sister chromatid exchange following treatment with ionizing radiation and alkylating agents. It forms homodimers and interacts with polynucleotide kinase (PNK), DNA polymerase-beta (POLB), DNA ligase III (LIG3), APTX, APLF, and APEX1. XRCC1 contains an N-terminal XRCC1-specific domain and two BRCT domains. This family corresponds to the first one. Pssm-ID: 349357 [Multi-domain] Cd Length: 80 Bit Score: 48.81 E-value: 2.47e-07
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| BRCT_BRC1_like_rpt2 | cd18436 | second BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar ... |
511-580 | 5.15e-07 | ||||
second BRCT domain of Schizosaccharomyces pombe BRCT-containing protein 1 (BRC1) and similar proteins; Schizosaccharomyces pombe BRC1 is required for mitotic fidelity, specifically in the G2 phase of the cell cycle. It plays a role in chromatin organization. The family also includes Cryptococcus neoformans DNA ligase 4 (LIG4, also known as DNA ligase IV or polydeoxyribonucleotide synthase [ATP] 4), which is involved in dsDNA break repair, and plays a role in non-homologous integration (NHI) pathways where it is required in the final step of non-homologus end-joining. Members in this family contains six BRCT domains. This family corresponds to the second repeat. Pssm-ID: 349389 [Multi-domain] Cd Length: 75 Bit Score: 47.61 E-value: 5.15e-07
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| BRCT_Rad4_rpt1 | cd17740 | first BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar ... |
522-583 | 2.28e-06 | ||||
first BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins; Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples the S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the first one. Pssm-ID: 349371 Cd Length: 82 Bit Score: 45.93 E-value: 2.28e-06
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| BRCT_TopBP1_rpt5 | cd18434 | fifth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ... |
545-588 | 6.37e-06 | ||||
fifth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; 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 fifth BRCT domain. Pssm-ID: 349387 Cd Length: 89 Bit Score: 44.99 E-value: 6.37e-06
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| BRCT_Rad4_rpt2 | cd17746 | second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and ... |
522-580 | 1.09e-04 | ||||
second BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar proteins; Rad4, also termed P74, or protein cut5, is an essential component for DNA replication and the checkpoint control system which couples S and M phases. It may directly or indirectly interact with chromatin proteins to form the complex required for the initiation and/or progression of DNA synthesis. Rad4 contains four BRCT repeats. The family corresponds to the second one. Pssm-ID: 349377 [Multi-domain] Cd Length: 91 Bit Score: 41.45 E-value: 1.09e-04
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| BRCT_CHS5_like | cd17742 | BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed ... |
534-584 | 3.28e-04 | ||||
BRCT domain of yeast chitin biosynthesis protein CHS5 and similar proteins; CHS5, also termed protein CAL3, is a component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. It is also involved in targeting FUS1 to sites of polarized growth. Pssm-ID: 349373 [Multi-domain] Cd Length: 77 Bit Score: 39.62 E-value: 3.28e-04
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| BRCT_PAXIP1_rpt4 | cd17730 | fourth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also ... |
534-583 | 4.59e-04 | ||||
fourth BRCT domain of PAX-interacting protein 1 (PAXIP1) and similar proteins; PAXIP1, also termed PAX transactivation activation domain-interacting protein (PTIP), is involved in DNA damage response and in transcriptional regulation through histone methyltransferase (HMT) complexes. It also facilitates ATM-mediated activation of p53 and promotes cellular resistance to ionizing radiation. PAXIP1 contains six BRCT repeats. This family corresponds to the fourth BRCT domain. Pssm-ID: 349362 [Multi-domain] Cd Length: 73 Bit Score: 39.15 E-value: 4.59e-04
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| BRCT_microcephalin_rpt1 | cd17716 | first (N-terminal) BRCT domain of microcephalin and similar proteins; Microcephalin is a DNA ... |
534-586 | 1.83e-03 | ||||
first (N-terminal) 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 first repeat. Pssm-ID: 349348 [Multi-domain] Cd Length: 78 Bit Score: 37.56 E-value: 1.83e-03
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| PTCB-BRCT | pfam12738 | twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. ... |
533-575 | 2.16e-03 | ||||
twin BRCT domain; This is a BRCT domain that appears in duplicate in most member sequences. BRCT domains are peptide- and phosphopeptide-binding modules. BRCT domains are present in a number of proteins involved in DNA checkpoint controls and DNA repair. Pssm-ID: 463687 [Multi-domain] Cd Length: 63 Bit Score: 37.18 E-value: 2.16e-03
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| lipoyl_domain | cd06849 | Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
88-112 | 5.16e-03 | ||||
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue. Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 36.23 E-value: 5.16e-03
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| AceF | COG0508 | Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
84-112 | 5.89e-03 | ||||
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 36.20 E-value: 5.89e-03
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