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Conserved domains on  [gi|1937369664|ref|NP_598256|]
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M-phase inducer phosphatase 2 isoform 1 [Rattus norvegicus]

Protein Classification

M-inducer_phosp and Cdc25 domain-containing protein( domain architecture ID 10535130)

M-inducer_phosp and Cdc25 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 111-378 3.79e-115

M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer phosphatases (EC:3.1.3.48), which also contain the pfam00581 domain. These proteins are involved in the control of mitosis.


:

Pssm-ID: 461962  Cd Length: 269  Bit Score: 342.89  E-value: 3.79e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 111 MDSPSPMDPQTAERTFEQAIQAASRVIqNEQFTIKRFRSLPVRLLGHSPVLQNitnSQALDSWEkdeAGYRAASSPGEDK 190
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVV-NLKMPIRRINSLPQRLLGSSPALKR---SQSLDSDI---YQPEQLSSQGENK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 191 EN--DGYIFKMPQKLPHSSSARAlAEWASRREAFTQRPSSAPDLMCLTTDGKM--DVEEASPVA-QSSSLTPVERaCEED 265
Cdd:pfam06617  74 ENvpEGFEFKKPTKPASRSRLRS-FNSGTAKDAFAQRPNSAPALMLSSPPPKMqeLEGDSSPVFlRRSSLTSSLN-DEED 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 266 DGFVDILESDLKDDDMVPAGMENLISAPLVKKLDKEEEQDLIMFSKCQRLFRSPSMPCSVIRPILKRLERPHDRDVPVLS 345
Cdd:pfam06617 152 DGFLEILDGDLENDEEVPSGMASLLTAPLVTDEIGERPTSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVKV 231

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1937369664 346 KRRKSGT----PLEEQQLEEPKARVFRSKSLCH-EIES 378
Cdd:pfam06617 232 KRRRSVAgtqvEAEEQEPESPRSLLQRSKSLCHqEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 407-526 6.80e-64

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: 205.15  E-value: 6.80e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 407 LKYISPETMVALLTGKFSNIVEKFVIVDCRYPYEYEGGHIKNAVNLPLEPDAETFLLKHPITpCNLDKRIILIFHCEFSS 486
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGV-ASKKKRRVLIFHCEFSS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1937369664 487 ERGPRMCRFIRERDRAAN--DYPSLYYPEMYILKGGYKEFFP 526
Cdd:cd01530    80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
 
Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 111-378 3.79e-115

M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer phosphatases (EC:3.1.3.48), which also contain the pfam00581 domain. These proteins are involved in the control of mitosis.


Pssm-ID: 461962  Cd Length: 269  Bit Score: 342.89  E-value: 3.79e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 111 MDSPSPMDPQTAERTFEQAIQAASRVIqNEQFTIKRFRSLPVRLLGHSPVLQNitnSQALDSWEkdeAGYRAASSPGEDK 190
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVV-NLKMPIRRINSLPQRLLGSSPALKR---SQSLDSDI---YQPEQLSSQGENK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 191 EN--DGYIFKMPQKLPHSSSARAlAEWASRREAFTQRPSSAPDLMCLTTDGKM--DVEEASPVA-QSSSLTPVERaCEED 265
Cdd:pfam06617  74 ENvpEGFEFKKPTKPASRSRLRS-FNSGTAKDAFAQRPNSAPALMLSSPPPKMqeLEGDSSPVFlRRSSLTSSLN-DEED 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 266 DGFVDILESDLKDDDMVPAGMENLISAPLVKKLDKEEEQDLIMFSKCQRLFRSPSMPCSVIRPILKRLERPHDRDVPVLS 345
Cdd:pfam06617 152 DGFLEILDGDLENDEEVPSGMASLLTAPLVTDEIGERPTSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVKV 231

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1937369664 346 KRRKSGT----PLEEQQLEEPKARVFRSKSLCH-EIES 378
Cdd:pfam06617 232 KRRRSVAgtqvEAEEQEPESPRSLLQRSKSLCHqEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 407-526 6.80e-64

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: 205.15  E-value: 6.80e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 407 LKYISPETMVALLTGKFSNIVEKFVIVDCRYPYEYEGGHIKNAVNLPLEPDAETFLLKHPITpCNLDKRIILIFHCEFSS 486
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGV-ASKKKRRVLIFHCEFSS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1937369664 487 ERGPRMCRFIRERDRAAN--DYPSLYYPEMYILKGGYKEFFP 526
Cdd:cd01530    80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
390-559 5.66e-40

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 150.96  E-value: 5.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 390 DYSKAFLLQTV-------DGKHQDLKYISPETMVALLTGKFSNIVEKFVIVDCRYPYEYEGGHIKNAVNLPLEPDAETFL 462
Cdd:COG5105   217 DFFKSFSNGEVfplptlgPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 463 LKHPITpcnldKRIILIFHCEFSSERGPRMCRFIRERDRAAN--DYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPM 540
Cdd:COG5105   297 RHKPLT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNpdHYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTM 371

                         170       180       190
                  ....*....|....*....|....*....|
gi 1937369664 541 NHAA-----------FRDELRNFRLKTRSW 559
Cdd:COG5105   372 NNAEldyrclykmdkFRRNKKFFATKNNSF 401
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 428-529 3.52e-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: 91.37  E-value: 3.52e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664  428 EKFVIVDCRYPYEYEGGHIKNAVNLPLE------PDAETFLLKHPITPCNLDKRIILIFHCeFSSERGPRMCRFIRErdr 501
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSelldrrGELDILEFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*...
gi 1937369664  502 aandypsLYYPEMYILKGGYKEFFPQHP 529
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAGP 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 428-524 8.12e-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: 64.43  E-value: 8.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 428 EKFVIVDCRYPYEYEGGHIKNAVNLPLE----PDAETFLLKHPITPCNLDKRIilIFHCEfSSERGPRMCRFIRErdraa 503
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSslslPPLPLLELLEKLLELLKDKPI--VVYCN-SGNRAAAAAALLKA----- 75

                          90       100
                  ....*....|....*....|.
gi 1937369664 504 ndypsLYYPEMYILKGGYKEF 524
Cdd:pfam00581  76 -----LGYKNVYVLDGGFEAW 91
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
400-461 2.27e-04

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 43.30  E-value: 2.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369664 400 VDGKHQDLKYISPETMVALLTGkfsnivEKFVIVDCRYPYEYEGGHIKNAVNlplePDAETF 461
Cdd:PRK00142  104 IDPLENVGTYLKPKEVNELLDD------PDVVFIDMRNDYEYEIGHFENAIE----PDIETF 155
 
Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 111-378 3.79e-115

M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer phosphatases (EC:3.1.3.48), which also contain the pfam00581 domain. These proteins are involved in the control of mitosis.


Pssm-ID: 461962  Cd Length: 269  Bit Score: 342.89  E-value: 3.79e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 111 MDSPSPMDPQTAERTFEQAIQAASRVIqNEQFTIKRFRSLPVRLLGHSPVLQNitnSQALDSWEkdeAGYRAASSPGEDK 190
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVV-NLKMPIRRINSLPQRLLGSSPALKR---SQSLDSDI---YQPEQLSSQGENK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 191 EN--DGYIFKMPQKLPHSSSARAlAEWASRREAFTQRPSSAPDLMCLTTDGKM--DVEEASPVA-QSSSLTPVERaCEED 265
Cdd:pfam06617  74 ENvpEGFEFKKPTKPASRSRLRS-FNSGTAKDAFAQRPNSAPALMLSSPPPKMqeLEGDSSPVFlRRSSLTSSLN-DEED 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 266 DGFVDILESDLKDDDMVPAGMENLISAPLVKKLDKEEEQDLIMFSKCQRLFRSPSMPCSVIRPILKRLERPHDRDVPVLS 345
Cdd:pfam06617 152 DGFLEILDGDLENDEEVPSGMASLLTAPLVTDEIGERPTSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVKV 231

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1937369664 346 KRRKSGT----PLEEQQLEEPKARVFRSKSLCH-EIES 378
Cdd:pfam06617 232 KRRRSVAgtqvEAEEQEPESPRSLLQRSKSLCHqEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 407-526 6.80e-64

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: 205.15  E-value: 6.80e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 407 LKYISPETMVALLTGKFSNIVEKFVIVDCRYPYEYEGGHIKNAVNLPLEPDAETFLLKHPITpCNLDKRIILIFHCEFSS 486
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGV-ASKKKRRVLIFHCEFSS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1937369664 487 ERGPRMCRFIRERDRAAN--DYPSLYYPEMYILKGGYKEFFP 526
Cdd:cd01530    80 KRGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 407-526 1.00e-43

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: 151.40  E-value: 1.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 407 LKYISPETMVALLTGKFSNIVEKFVIVDCRYPyEYEGGHIKNAVNLPLEpDAETFLLKHPITpCNLDKRIILIFHCEFSS 486
Cdd:cd01443     1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQ-SCYQTLPQVYAL-FSLAGVKLAIFYCGSSQ 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1937369664 487 ERGPRMCRFIRERDRAandyPSLYYPEMYILKGGYKEFFP 526
Cdd:cd01443    78 GRGPRAARWFADYLRK----VGESLPKSYILTGGIKAWYH 113
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
390-559 5.66e-40

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 150.96  E-value: 5.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 390 DYSKAFLLQTV-------DGKHQDLKYISPETMVALLTGKFSNIVEKFVIVDCRYPYEYEGGHIKNAVNLPLEPDAETFL 462
Cdd:COG5105   217 DFFKSFSNGEVfplptlgPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 463 LKHPITpcnldKRIILIFHCEFSSERGPRMCRFIRERDRAAN--DYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPM 540
Cdd:COG5105   297 RHKPLT-----HPRALIFHCEFSSHRAPRLAQHLRNMDRMKNpdHYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTM 371

                         170       180       190
                  ....*....|....*....|....*....|
gi 1937369664 541 NHAA-----------FRDELRNFRLKTRSW 559
Cdd:COG5105   372 NNAEldyrclykmdkFRRNKKFFATKNNSF 401
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 428-529 3.52e-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: 91.37  E-value: 3.52e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664  428 EKFVIVDCRYPYEYEGGHIKNAVNLPLE------PDAETFLLKHPITPCNLDKRIILIFHCeFSSERGPRMCRFIRErdr 501
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSelldrrGELDILEFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*...
gi 1937369664  502 aandypsLYYPEMYILKGGYKEFFPQHP 529
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAGP 99
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 428-524 3.95e-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: 68.10  E-value: 3.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 428 EKFVIVDCRYPYEYEGGHIKNAVNLPLEPDAETFLLKHPitpcNLDKRIILifHCEfSSERGPRMCRFIRErdraandyp 507
Cdd:cd00158     9 EDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLEL----DKDKPIVV--YCR-SGNRSARAAKLLRK--------- 72

                          90
                  ....*....|....*..
gi 1937369664 508 sLYYPEMYILKGGYKEF 524
Cdd:cd00158    73 -AGGTNVYNLEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 428-524 8.12e-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: 64.43  E-value: 8.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 428 EKFVIVDCRYPYEYEGGHIKNAVNLPLE----PDAETFLLKHPITPCNLDKRIilIFHCEfSSERGPRMCRFIRErdraa 503
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSslslPPLPLLELLEKLLELLKDKPI--VVYCN-SGNRAAAAAALLKA----- 75

                          90       100
                  ....*....|....*....|.
gi 1937369664 504 ndypsLYYPEMYILKGGYKEF 524
Cdd:pfam00581  76 -----LGYKNVYVLDGGFEAW 91
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 407-521 1.36e-12

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: 64.36  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 407 LKYISPETMVALLTgkfsNIVEKFVIVDCRyPYEYEGGHIKNAVNLPlepdAETFL--LKHPITPCNLDKRIILIFHCEF 484
Cdd:cd01531     1 VSYISPAQLKGWIR----NGRPPFQVVDVR-DEDYAGGHIKGSWHYP----STRFKaqLNQLVQLLSGSKKDTVVFHCAL 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1937369664 485 SSERGP----RMCRFIRERDRAANDypslyyPEMYILKGGY 521
Cdd:cd01531    72 SQVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGGF 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 406-523 2.89e-10

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: 57.67  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 406 DLKYISPETMVALLTGkfsnivEKFVIVDCRYPYEYEGGHIKNAVNLPLEpDAETFLLKHPitpcnLDKRIILifHCEfS 485
Cdd:COG0607     2 SVKEISPAELAELLES------EDAVLLDVREPEEFAAGHIPGAINIPLG-ELAERLDELP-----KDKPIVV--YCA-S 66

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1937369664 486 SERGPRMCRFIRERDraandypslyYPEMYILKGGYKE 523
Cdd:COG0607    67 GGRSAQAAALLRRAG----------YTNVYNLAGGIEA 94
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 410-532 2.96e-05

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: 43.81  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369664 410 ISPETMVALLTGKfsniVEKFVIVDCRYPYEYEGGHIKNAVNLPLePD------AETFLLKHPITPCN-------LDKRI 476
Cdd:cd01446     2 IDCAWLAALLREG----GERLLLLDCRPFLEYSSSHIRGAVNVCC-PTilrrrlQGGKILLQQLLSCPedrdrlrRGESL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369664 477 ILIFHCEFSSERGPR------------MCRFIRERDRAandypslyypemYILKGGYKEFFPQHPNFC 532
Cdd:cd01446    77 AVVVYDESSSDRERLredstaesvlgkLLRKLQEGCSV------------YLLKGGFEQFSSEFPELC 132
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
400-461 2.27e-04

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 43.30  E-value: 2.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369664 400 VDGKHQDLKYISPETMVALLTGkfsnivEKFVIVDCRYPYEYEGGHIKNAVNlplePDAETF 461
Cdd:PRK00142  104 IDPLENVGTYLKPKEVNELLDD------PDVVFIDMRNDYEYEIGHFENAIE----PDIETF 155
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 408-461 3.76e-04

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: 39.87  E-value: 3.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1937369664 408 KYISPETMVALLTGKfsniveKFVIVDCRYPYEYEGGHIKNAVNlplePDAETF 461
Cdd:cd01518     2 TYLSPAEWNELLEDP------EVVLLDVRNDYEYDIGHFKGAVN----PDVDTF 45
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 428-455 2.54e-03

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: 37.25  E-value: 2.54e-03
                          10        20
                  ....*....|....*....|....*...
gi 1937369664 428 EKFVIVDCRYPYEYEGGHIKNAVNLPLE 455
Cdd:cd01524    12 DGVTLIDVRTPQEFEKGHIKGAINIPLD 39
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 420-459 3.56e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 39.81  E-value: 3.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1937369664 420 TGKFSNIVEKFV-IVDCRYPYEYEGGHIKNAVNLPLEPDAE 459
Cdd:PRK11784    5 AQDFRALFLNDTpLIDVRSPIEFAEGHIPGAINLPLLNDEE 45
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 413-453 8.00e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 36.56  E-value: 8.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1937369664 413 ETMVALLTGKFSNIVEKFVIVDCRYPYEYEGGHIKNAVNLP 453
Cdd:cd01521     9 ETDCWDVAIALKNGKPDFVLVDVRSAEAYARGHVPGAINLP 49
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 431-482 8.14e-03

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: 36.09  E-value: 8.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1937369664 431 VIVDCRYPYEYEGGHIKNAVNLPLE--PDA-----ETFLLKHPITPCNLDKRiiLIFHC 482
Cdd:cd01519    17 VLIDVREPEELKTGKIPGAINIPLSslPDAlalseEEFEKKYGFPKPSKDKE--LIFYC 73
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 428-457 9.53e-03

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 38.23  E-value: 9.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1937369664 428 EKFVIVDCRYPY-----EYEGGHIKNAVNLPLEPD 457
Cdd:COG2897     8 PDVVILDVRWDLpdgraAYEAGHIPGAVFLDLDTD 42
 
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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