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Conserved domains on  [gi|1063741921|ref|NP_001332020|]
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C-terminal domain phosphatase-like 4 [Arabidopsis thaliana]

Protein Classification

HAD_FCP1-like and BRCT_CTDP1 domain-containing protein( domain architecture ID 12856661)

HAD_FCP1-like and BRCT_CTDP1 domain-containing protein

Graphical summary

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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 ...
 61-219 1.77e-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: 241.03  E-value: 1.77e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921  61 LQRQRKLYLVLDLDHTLLNTTILRDLKPEEEYLKsHTHSLQDgcnVSGGSLFLLEFMQMMTKLRPFVHSFLKEASEMFVM 140
Cdd:TIGR02250   1 LLREKKLHLVLDLDQTLIHTTKDPTLSEWEKYDI-EEPNSET---RRDLRKFNLGTMWYLTKLRPFLHEFLKEASKLYEM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921 141 YIYTMGDRNYARQMAKLLDPKGEYFGDRVISRDDGTVRHEKSL-DVVLGQESAVLILDDTENAWPKHKDNLIVIERYHFF 219
Cdd:TIGR02250  77 HVYTMGTRAYAQAIAKLIDPDGKYFGDRIISRDESGSPHTKSLlRLFPADESMVVIIDDREDVWPWHKRNLIQIEPYNYF 156
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 273-368 2.01e-42

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: 143.44  E-value: 2.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921 273 DVRLMLKQVRKEILKGCKIVFSRVFPTKAKPEDHPLWKMAEELGATCATEVDASVTHVVAMDVGTEKARWAVREK-KYVV 351
Cdd:cd17729     1 DVKDILPELRSKVLKGCVIVFSGVIPTGIDPERSRLWKLAESLGAKVVTDLSPRTTHLVAAKLGTEKVKQALKMPgIHVV 80

                          90
                  ....*....|....*..
gi 1063741921 352 HRGWIDAANYLWMKQPE 368
Cdd:cd17729    81 HPDWLWACAERWERVDE 97
 
Name Accession Description Interval E-value
FCP1_euk TIGR02250
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ...
 61-219 1.77e-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: 241.03  E-value: 1.77e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921  61 LQRQRKLYLVLDLDHTLLNTTILRDLKPEEEYLKsHTHSLQDgcnVSGGSLFLLEFMQMMTKLRPFVHSFLKEASEMFVM 140
Cdd:TIGR02250   1 LLREKKLHLVLDLDQTLIHTTKDPTLSEWEKYDI-EEPNSET---RRDLRKFNLGTMWYLTKLRPFLHEFLKEASKLYEM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921 141 YIYTMGDRNYARQMAKLLDPKGEYFGDRVISRDDGTVRHEKSL-DVVLGQESAVLILDDTENAWPKHKDNLIVIERYHFF 219
Cdd:TIGR02250  77 HVYTMGTRAYAQAIAKLIDPDGKYFGDRIISRDESGSPHTKSLlRLFPADESMVVIIDDREDVWPWHKRNLIQIEPYNYF 156
CPDc smart00577
catalytic domain of ctd-like phosphatases;
65-223 1.07e-51

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 169.33  E-value: 1.07e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921   65 RKLYLVLDLDHTLLNTTILRdlkpeeeylKSHTHSLQDGCNVsggsLFLLEFMQMMTKLRPFVHSFLKEASEMFVMYIYT 144
Cdd:smart00577   1 KKKTLVLDLDETLVHSTHRS---------FKEWTNRDFIVPV----LIDGHPHGVYVKKRPGVDEFLKRASELFELVVFT 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921  145 MGDRNYARQMAKLLDPKGeYFGDRVISRDDGTV---RHEKSLDVVLGQESAVLILDDTENAWPKHKDNLIVIERYHFFSS 221
Cdd:smart00577  68 AGLRMYADPVLDLLDPKK-YFGYRRLFRDECVFvkgKYVKDLSLLNRDLSKVIIIDDSPDSWPFHPENLIPIKPWFGDPD 146


                   ..
gi 1063741921  222 SC 223
Cdd:smart00577 147 DT 148
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 273-368 2.01e-42

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: 143.44  E-value: 2.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921 273 DVRLMLKQVRKEILKGCKIVFSRVFPTKAKPEDHPLWKMAEELGATCATEVDASVTHVVAMDVGTEKARWAVREK-KYVV 351
Cdd:cd17729     1 DVKDILPELRSKVLKGCVIVFSGVIPTGIDPERSRLWKLAESLGAKVVTDLSPRTTHLVAAKLGTEKVKQALKMPgIHVV 80

                          90
                  ....*....|....*..
gi 1063741921 352 HRGWIDAANYLWMKQPE 368
Cdd:cd17729    81 HPDWLWACAERWERVDE 97
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 66-213 7.62e-39

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: 135.42  E-value: 7.62e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921  66 KLYLVLDLDHTLLNTTILRDLKPEEEYlkshthslqdgcnvsgGSLFLLEFMQMMTKLRPFVHSFLKEASEMFVMYIYTM 145
Cdd:cd07521     1 KLTLVLDLDETLVHSTWKPVLSEDFKI----------------PVLPDGREHGYYVKKRPGVDEFLERLSKLYEIVIFTA 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063741921 146 GDRNYARQMAKLLDPKGeYFGDRVISRDDGTVR---HEKSLDVVLGQESAVLILDDTENAWPKHKDNLIVI 213
Cdd:cd07521    65 GTRAYADPVADKLDPNG-LFIDRRLFRDSCVYVdgnYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAIPI 134
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 69-236 4.29e-28

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: 107.71  E-value: 4.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921  69 LVLDLDHTLLNTTILRDLKpEEEYLKSHTHSLQDGcnvsggslfllefmqmmTKLRPFVHSFLKEASEMFVMYIYTMGDR 148
Cdd:pfam03031   3 LVLDLDETLVHSSFEPPLK-SDFILPVPGETHGGY-----------------VKKRPGLDEFLKELSKYYEIVIFTASSK 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921 149 NYARQMAKLLDPKGEYFGDRvISRDDGTVR---HEKSLDVVLGQESAVLILDDTENAWPKHKDNLIVIERYHFfssscRQ 225
Cdd:pfam03031  65 EYADPVLDILDPNGKLFSHR-LYRESCKFEdgvYVKDLSLLGRDLSRVVIVDNSPDSFLLQPDNGIPIPPFFG-----DP 138

                         170
                  ....*....|.
gi 1063741921 226 FDHRYKSLSEL 236
Cdd:pfam03031 139 DDNELLKLLPF 149
BRCT smart00292
breast cancer carboxy-terminal domain;
284-356 8.05e-06

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 43.52  E-value: 8.05e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063741921  284 EILKGCKIVFSRVFPtkaKPEDHPLWKMAEELGATCATEVD-ASVTHVVAMDVGTEKARW--AVREKKYVVHRGWI 356
Cdd:smart00292   2 KLFKGKTFYITGSFD---KEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKLELlkAIALGIPIVKEEWL 74
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 285-356 4.96e-05

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: 41.13  E-value: 4.96e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063741921 285 ILKGCKIVFSRvFPTKAKPEDHplwKMAEELGATCATEVDASVTHVVAMDVGTEKARWAVREKKyVVHRGWI 356
Cdd:pfam00533   5 LFSGKTFVITG-LDGLERDELK---ELIEKLGGKVTDSLSKKTTHVIVEARTKKYLKAKELGIP-IVTEEWL 71
 
Name Accession Description Interval E-value
FCP1_euk TIGR02250
FCP1-like phosphatase, phosphatase domain; This model represents the phosphatase domain of the ...
 61-219 1.77e-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: 241.03  E-value: 1.77e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921  61 LQRQRKLYLVLDLDHTLLNTTILRDLKPEEEYLKsHTHSLQDgcnVSGGSLFLLEFMQMMTKLRPFVHSFLKEASEMFVM 140
Cdd:TIGR02250   1 LLREKKLHLVLDLDQTLIHTTKDPTLSEWEKYDI-EEPNSET---RRDLRKFNLGTMWYLTKLRPFLHEFLKEASKLYEM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921 141 YIYTMGDRNYARQMAKLLDPKGEYFGDRVISRDDGTVRHEKSL-DVVLGQESAVLILDDTENAWPKHKDNLIVIERYHFF 219
Cdd:TIGR02250  77 HVYTMGTRAYAQAIAKLIDPDGKYFGDRIISRDESGSPHTKSLlRLFPADESMVVIIDDREDVWPWHKRNLIQIEPYNYF 156
CPDc smart00577
catalytic domain of ctd-like phosphatases;
65-223 1.07e-51

catalytic domain of ctd-like phosphatases;


Pssm-ID: 214729  Cd Length: 148  Bit Score: 169.33  E-value: 1.07e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921   65 RKLYLVLDLDHTLLNTTILRdlkpeeeylKSHTHSLQDGCNVsggsLFLLEFMQMMTKLRPFVHSFLKEASEMFVMYIYT 144
Cdd:smart00577   1 KKKTLVLDLDETLVHSTHRS---------FKEWTNRDFIVPV----LIDGHPHGVYVKKRPGVDEFLKRASELFELVVFT 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921  145 MGDRNYARQMAKLLDPKGeYFGDRVISRDDGTV---RHEKSLDVVLGQESAVLILDDTENAWPKHKDNLIVIERYHFFSS 221
Cdd:smart00577  68 AGLRMYADPVLDLLDPKK-YFGYRRLFRDECVFvkgKYVKDLSLLNRDLSKVIIIDDSPDSWPFHPENLIPIKPWFGDPD 146


                   ..
gi 1063741921  222 SC 223
Cdd:smart00577 147 DT 148
BRCT_CTDP1 cd17729
BRCT domain of RNA polymerase II subunit A C-terminal domain phosphatase (CTDP1) and similar ...
 273-368 2.01e-42

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: 143.44  E-value: 2.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921 273 DVRLMLKQVRKEILKGCKIVFSRVFPTKAKPEDHPLWKMAEELGATCATEVDASVTHVVAMDVGTEKARWAVREK-KYVV 351
Cdd:cd17729     1 DVKDILPELRSKVLKGCVIVFSGVIPTGIDPERSRLWKLAESLGAKVVTDLSPRTTHLVAAKLGTEKVKQALKMPgIHVV 80

                          90
                  ....*....|....*..
gi 1063741921 352 HRGWIDAANYLWMKQPE 368
Cdd:cd17729    81 HPDWLWACAERWERVDE 97
HAD_FCP1-like cd07521
human CTD phosphatase subunit 1 (CTDP1/FCP1) and related proteins; belongs to the haloacid ...
 66-213 7.62e-39

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: 135.42  E-value: 7.62e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921  66 KLYLVLDLDHTLLNTTILRDLKPEEEYlkshthslqdgcnvsgGSLFLLEFMQMMTKLRPFVHSFLKEASEMFVMYIYTM 145
Cdd:cd07521     1 KLTLVLDLDETLVHSTWKPVLSEDFKI----------------PVLPDGREHGYYVKKRPGVDEFLERLSKLYEIVIFTA 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063741921 146 GDRNYARQMAKLLDPKGeYFGDRVISRDDGTVR---HEKSLDVVLGQESAVLILDDTENAWPKHKDNLIVI 213
Cdd:cd07521    65 GTRAYADPVADKLDPNG-LFIDRRLFRDSCVYVdgnYVKDLSKLFRDLSKVVIIDDSPGSYWLQPENAIPI 134
NIF pfam03031
NLI interacting factor-like phosphatase; This family contains a number of NLI interacting ...
 69-236 4.29e-28

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: 107.71  E-value: 4.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921  69 LVLDLDHTLLNTTILRDLKpEEEYLKSHTHSLQDGcnvsggslfllefmqmmTKLRPFVHSFLKEASEMFVMYIYTMGDR 148
Cdd:pfam03031   3 LVLDLDETLVHSSFEPPLK-SDFILPVPGETHGGY-----------------VKKRPGLDEFLKELSKYYEIVIFTASSK 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921 149 NYARQMAKLLDPKGEYFGDRvISRDDGTVR---HEKSLDVVLGQESAVLILDDTENAWPKHKDNLIVIERYHFfssscRQ 225
Cdd:pfam03031  65 EYADPVLDILDPNGKLFSHR-LYRESCKFEdgvYVKDLSLLGRDLSRVVIVDNSPDSFLLQPDNGIPIPPFFG-----DP 138

                         170
                  ....*....|.
gi 1063741921 226 FDHRYKSLSEL 236
Cdd:pfam03031 139 DDNELLKLLPF 149
HIF-SF_euk TIGR02251
Dullard-like phosphatase domain; This model represents the putative phosphatase domain of a ...
 66-216 1.43e-13

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: 68.09  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921  66 KLYLVLDLDHTLLNTTILRdlkPEEEYlkshthslqDGC-NVsggsLFLLEFMQMMTKLRPFVHSFLKEASEMFVMYIYT 144
Cdd:TIGR02251   1 KKTLVLDLDETLVHSTFKM---PKVDA---------DFKvPV----LIDGKIIQVYVFKRPHVDEFLERVSKWYELVIFT 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063741921 145 MGDRNYARQMAKLLDPKGEYFgDRVISRDDGTVRHE---KSLDVVLGQESAVLILDDTENAWPKHKDNLIVIERY 216
Cdd:TIGR02251  65 ASLEEYADPVLDILDRGGKVI-SRRLYRESCVFTNGkyvKDLSLVGKDLSKVIIIDNSPYSYSLQPDNAIPIKSW 138
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 289-358 2.27e-07

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: 47.74  E-value: 2.27e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063741921 289 CKIVFSRVFPtkakPEDHPLWKMAEELGATCATEVDASVTHVVAMDV-GTEKARWAVREKKYVVHRGWIDA 358
Cdd:cd00027     1 LVICFSGLDD----EEREELKKLIEALGGKVSESLSSKVTHLIAKSPsGEKYYLAALAWGIPIVSPEWLLD 67
BRCT smart00292
breast cancer carboxy-terminal domain;
284-356 8.05e-06

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 43.52  E-value: 8.05e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063741921  284 EILKGCKIVFSRVFPtkaKPEDHPLWKMAEELGATCATEVD-ASVTHVVAMDVGTEKARW--AVREKKYVVHRGWI 356
Cdd:smart00292   2 KLFKGKTFYITGSFD---KEERDELKELIEALGGKVTSSLSsKTTTHVIVGSPEGGKLELlkAIALGIPIVKEEWL 74
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 285-356 4.96e-05

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: 41.13  E-value: 4.96e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063741921 285 ILKGCKIVFSRvFPTKAKPEDHplwKMAEELGATCATEVDASVTHVVAMDVGTEKARWAVREKKyVVHRGWI 356
Cdd:pfam00533   5 LFSGKTFVITG-LDGLERDELK---ELIEKLGGKVTDSLSKKTTHVIVEARTKKYLKAKELGIP-IVTEEWL 71
BRCT_TopBP1_rpt6 cd17727
sixth BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 286-358 1.09e-04

sixth 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 sixth BRCT domain.


Pssm-ID: 349359 [Multi-domain]  Cd Length: 75  Bit Score: 40.27  E-value: 1.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063741921 286 LKGCKIVFSrvfpTKAKPEDHPLWKMAEELGATCATEVDASVTHVVAMDVGTEKAR---WAVREKKYVVHRGWIDA 358
Cdd:cd17727     1 LKGVVICVS----KKLSKRQGELNKIAASLGAEYRWTYDESCTHFIYQGKANDTNReykSAKEQGKFIVSPHWLYA 72
BRCT_Bard1_rpt1 cd17734
first BRCT domain of BRCA1-associated RING domain protein 1 (Bard1) and similar proteins; ...
 310-366 4.94e-04

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: 38.35  E-value: 4.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063741921 310 KMAEELGATCATEVDASVTHVVamdVGTEKARWAVREKKY---VVHRGWIdaANYLWMKQ 366
Cdd:cd17734    18 KLAQLLKAKVVTEFSPEVTHVV---VPADERGVCPRTMKYlmgILAGKWI--VSFEWVEA 72
BRCT_Rad4_rpt1 cd17740
first BRCT domain of Schizosaccharomyces pombe S-M checkpoint control protein Rad4 and similar ...
 312-364 1.82e-03

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: 37.07  E-value: 1.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063741921 312 AEELGATCATEVDASVTHVVAMDVGTEKARWAVREKKY--VVHRGWIDAANYLWM 364
Cdd:cd17740    25 ASKMGAAYTADLTSDVTHLVAGQVNTTKYKFAARSRPDikVMTVEWVEHLYESWQ 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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