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Conserved domains on  [gi|157830510|pdb|1C25|A]
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Chain A, CDC25A

Protein Classification

M-phase inducer phosphatase( domain architecture ID 10107435)

M-phase inducer phosphatase is a tyrosine protein phosphatase which may function as a dosage-dependent inducer in mitotic control

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 22-140 1.97e-65

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


:

Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 195.52  E-value: 1.97e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       22 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSE 101
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
1C25_A      102 RGPRMCRYVRERDRLGN--EYPKLHYPELYVLKGGYKEFFM 140
Cdd:cd01530  81 RGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 22-140 1.97e-65

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 195.52  E-value: 1.97e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       22 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSE 101
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
1C25_A      102 RGPRMCRYVRERDRLGN--EYPKLHYPELYVLKGGYKEFFM 140
Cdd:cd01530  81 RGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
17-154 2.08e-43

Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 148.26  E-value: 2.08e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       17 GKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVptdgKRVIVVFHC 96
Cdd:COG5105 236 GKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT----HPRALIFHC 311

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       97 EFSSERGPRMCRYVRERDRLGNE--YPKLHYPELYVLKGGYKEFFMKCQSYCEPPSYRPM 154
Cdd:COG5105 312 EFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTM 371
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 43-142 9.60e-22

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 84.05  E-value: 9.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A          43 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTD-------GKRVIVVFHCeFSSERGPRMCRYVRERDr 115
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlglDKDKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
1C25_A         116 lgneypklhYPELYVLKGGYKEFFMKC 142
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 43-138 2.35e-13

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 62.12  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A         43 KEFVIIDCRYPYEYEGGHIKGAVNLH----MEEEVEDFLLKKPIVPTDGKRVIVVfHCEfSSERGPRMCRYVRerdRLGn 118
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPlsslSLPPLPLLELLEKLLELLKDKPIVV-YCN-SGNRAAAAAALLK---ALG- 77

                          90       100
                  ....*....|....*....|
1C25_A        119 eypklhYPELYVLKGGYKEF 138
Cdd:pfam00581  78 ------YKNVYVLDGGFEAW 91
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
23-83 5.27e-03

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 35.98  E-value: 5.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1C25_A        23 KYISPEimasvlngKFANLI--KEFVIIDCRYPYEYEGGHIKGAVN---------LHMEEEVEDFLLKKPIV 83
Cdd:PRK00142 112 TYLKPK--------EVNELLddPDVVFIDMRNDYEYEIGHFENAIEpdietfrefPPWVEENLDPLKDKKVV 175
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 22-140 1.97e-65

Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. Cdc25A phosphatase functions to regulate S phase entry and Cdc25B is required for G2/M phase transition of the cell cycle. The Cdc25 domain binds oxyanions at the catalytic site and has the signature motif (H/YCxxxxxR).


Pssm-ID: 238788 [Multi-domain]  Cd Length: 121  Bit Score: 195.52  E-value: 1.97e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       22 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSE 101
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
1C25_A      102 RGPRMCRYVRERDRLGN--EYPKLHYPELYVLKGGYKEFFM 140
Cdd:cd01530  81 RGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
17-154 2.08e-43

Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 148.26  E-value: 2.08e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       17 GKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVptdgKRVIVVFHC 96
Cdd:COG5105 236 GKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT----HPRALIFHC 311

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       97 EFSSERGPRMCRYVRERDRLGNE--YPKLHYPELYVLKGGYKEFFMKCQSYCEPPSYRPM 154
Cdd:COG5105 312 EFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTM 371
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 22-139 3.51e-37

Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR).


Pssm-ID: 238720 [Multi-domain]  Cd Length: 113  Bit Score: 123.67  E-value: 3.51e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       22 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPyEYEGGHIKGAVNLHMEEeVEDFLLKKPIVPTDGKRVIVVFHCEFSSE 101
Cdd:cd01443   1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQS-CYQTLPQVYALFSLAGVKLAIFYCGSSQG 78

                        90       100       110
                ....*....|....*....|....*....|....*...
1C25_A      102 RGPRMCRYVRERDRLGNEYpklhYPELYVLKGGYKEFF 139
Cdd:cd01443  79 RGPRAARWFADYLRKVGES----LPKSYILTGGIKAWY 112
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 43-142 9.60e-22

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 84.05  E-value: 9.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A          43 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTD-------GKRVIVVFHCeFSSERGPRMCRYVRERDr 115
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlglDKDKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
1C25_A         116 lgneypklhYPELYVLKGGYKEFFMKC 142
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 43-138 2.43e-14

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 64.63  E-value: 2.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       43 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPivptdGKRVIVVFHCEfSSERGPRMCRYVRerdrlgneypK 122
Cdd:cd00158   9 EDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLEL-----DKDKPIVVYCR-SGNRSARAAKLLR----------K 72

                        90
                ....*....|....*.
1C25_A      123 LHYPELYVLKGGYKEF 138
Cdd:cd00158  73 AGGTNVYNLEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 43-138 2.35e-13

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 62.12  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A         43 KEFVIIDCRYPYEYEGGHIKGAVNLH----MEEEVEDFLLKKPIVPTDGKRVIVVfHCEfSSERGPRMCRYVRerdRLGn 118
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPlsslSLPPLPLLELLEKLLELLKDKPIVV-YCN-SGNRAAAAAALLK---ALG- 77

                          90       100
                  ....*....|....*....|
1C25_A        119 eypklhYPELYVLKGGYKEF 138
Cdd:pfam00581  78 ------YKNVYVLDGGFEAW 91
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 22-135 3.60e-13

Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.


Pssm-ID: 238789 [Multi-domain]  Cd Length: 113  Bit Score: 62.05  E-value: 3.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       22 LKYISPeimaSVLNGKFANLIKEFVIIDCRyPYEYEGGHIKGAVNL-------HMEEEVEDFLLKKPIVptdgkrviVVF 94
Cdd:cd01531   1 VSYISP----AQLKGWIRNGRPPFQVVDVR-DEDYAGGHIKGSWHYpstrfkaQLNQLVQLLSGSKKDT--------VVF 67

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
1C25_A       95 HCEFSSERGP----RMCRYVRERDRLGNEypklhyPELYVLKGGY 135
Cdd:cd01531  68 HCALSQVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGGF 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 21-137 8.39e-12

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 58.44  E-value: 8.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       21 DLKYISPEIMASVLNGKfanlikEFVIIDCRYPYEYEGGHIKGAVNLHMeEEVEDFLLKkpiVPTDGKrviVVFHCEfSS 100
Cdd:COG0607   2 SVKEISPAELAELLESE------DAVLLDVREPEEFAAGHIPGAINIPL-GELAERLDE---LPKDKP---IVVYCA-SG 67

                        90       100       110
                ....*....|....*....|....*....|....*..
1C25_A      101 ERGPRMCRYVRerdRLGneypklhYPELYVLKGGYKE 137
Cdd:COG0607  68 GRSAQAAALLR---RAG-------YTNVYNLAGGIEA 94
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 43-75 5.37e-05

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 41.70  E-value: 5.37e-05
                        10        20        30
                ....*....|....*....|....*....|....*...
1C25_A       43 KEFVIIDCRYPY-----EYEGGHIKGAVNLHMEEEVED 75
Cdd:COG2897   8 PDVVILDVRWDLpdgraAYEAGHIPGAVFLDLDTDLSD 45
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 43-96 3.47e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 38.02  E-value: 3.47e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1C25_A       43 KEFVIIDCRYPYEYEGGHIKGAVN---------LHMEEevEDFLLK----KPivPTDGKrviVVFHC 96
Cdd:cd01519  14 PNKVLIDVREPEELKTGKIPGAINiplsslpdaLALSE--EEFEKKygfpKP--SKDKE---LIFYC 73
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 43-96 5.37e-04

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 39.00  E-value: 5.37e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1C25_A       43 KEFVIIDCRYPYEYEG---------GHIKGAVNLHME------------EEVEDFLLKKPIvpTDGKRVIVvfHC 96
Cdd:COG2897 152 PDAVLVDARSPERYRGevepidpraGHIPGAVNLPWTdlldedgtfksaEELRALFAALGI--DPDKPVIT--YC 222
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 43-136 6.58e-04

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 36.86  E-value: 6.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       43 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEevedflLKKPIVPTDGKRVIVVfHCEfSSERGprmcrYVRERDRLGNEYpk 122
Cdd:cd01524  12 DGVTLIDVRTPQEFEKGHIKGAINIPLDE------LRDRLNELPKDKEIIV-YCA-VGLRG-----YIAARILTQNGF-- 76

                        90
                ....*....|....
1C25_A      123 lhypELYVLKGGYK 136
Cdd:cd01524  77 ----KVKNLDGGYK 86
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 28-83 1.40e-03

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 36.22  E-value: 1.40e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1C25_A       28 EIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEE------EVEDFLLKKPIV 83
Cdd:cd01528   1 QISVAELAEWLADEREEPVLIDVREPEELEIAFLPGFLHLPMSEiperskELDSDNPDKDIV 62
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 23-83 2.86e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 35.25  E-value: 2.86e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       23 KYISPEIMASVLNGKfanlikEFVIIDCRYPYEYEGGHIKGAVNLHME---------EEVEDFLLKKPIV 83
Cdd:cd01518   2 TYLSPAEWNELLEDP------EVVLLDVRNDYEYDIGHFKGAVNPDVDtfrefpfwlDENLDLLKGKKVL 65
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
23-83 5.27e-03

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 35.98  E-value: 5.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1C25_A        23 KYISPEimasvlngKFANLI--KEFVIIDCRYPYEYEGGHIKGAVN---------LHMEEEVEDFLLKKPIV 83
Cdd:PRK00142 112 TYLKPK--------EVNELLddPDVVFIDMRNDYEYEIGHFENAIEpdietfrefPPWVEENLDPLKDKKVV 175
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 28-67 5.33e-03

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 35.34  E-value: 5.33e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
1C25_A       28 EIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNL 67
Cdd:cd01446   1 TIDCAWLAALLREGGERLLLLDCRPFLEYSSSHIRGAVNV 40
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 46-135 7.82e-03

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 34.16  E-value: 7.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1C25_A       46 VIIDCRYP--YEYEGGHIKGAVNLHMeEEVEDFLlkkPIVPTDGKRVIVVFHcEFSSERGPRMCRyvrerdrlgneypKL 123
Cdd:cd01444  18 VLLDVRDPasYAALPDHIPGAIHLDE-DSLDDWL---GDLDRDRPVVVYCYH-GNSSAQLAQALR-------------EA 79

                        90
                ....*....|..
1C25_A      124 HYPELYVLKGGY 135
Cdd:cd01444  80 GFTDVRSLAGGF 91
 
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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