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Conserved domains on  [gi|4757950|ref|NP_004349|]
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M-phase inducer phosphatase 2 isoform 2 [Homo sapiens]

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 ...
 99-369 9.71e-117

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: 346.74  E-value: 9.71e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950     99 MDSPSPMDPHMAEQTFEQAIQAASRIIrNEQFAIRRFQSMPVRLLGHSPVLRNitnSQAPDGRRkseAGSGAASSSGEDK 178
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVV-NLKMPIRRINSLPQRLLGSSPALKR---SQSLDSDI---YQPEQLSSQGENK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950    179 EN--DGFVFKMPWKPTHPSSTHAlAEWASRREAFAQRPSSAPDLMCLSPDRKMEV--EELSPLALGRFSLTPAEGDtEED 254
Cdd:pfam06617  74 ENvpEGFEFKKPTKPASRSRLRS-FNSGTAKDAFAQRPNSAPALMLSSPPPKMQEleGDSSPVFLRRSSLTSSLND-EED 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950    255 DGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQN 334
Cdd:pfam06617 152 DGFLEILDGDLENDEEVPSGMASLLTAPLVTDEIGERPTSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVKV 231

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 4757950    335 KRRRSVTPPEEQQEAEEP---KARVLRSKSLCHDEIEN 369
Cdd:pfam06617 232 KRRRSVAGTQVEAEEQEPespRSLLQRSKSLCHQEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 398-517 2.54e-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: 208.61  E-value: 2.54e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  398 LKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIApCSLDKRVILIFHCEFSS 477
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGV-ASKKKRRVLIFHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4757950  478 ERGPRMCRFIRERDRA--VNDYPSLYYPEMYILKGGYKEFFP 517
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 ...
 99-369 9.71e-117

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: 346.74  E-value: 9.71e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950     99 MDSPSPMDPHMAEQTFEQAIQAASRIIrNEQFAIRRFQSMPVRLLGHSPVLRNitnSQAPDGRRkseAGSGAASSSGEDK 178
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVV-NLKMPIRRINSLPQRLLGSSPALKR---SQSLDSDI---YQPEQLSSQGENK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950    179 EN--DGFVFKMPWKPTHPSSTHAlAEWASRREAFAQRPSSAPDLMCLSPDRKMEV--EELSPLALGRFSLTPAEGDtEED 254
Cdd:pfam06617  74 ENvpEGFEFKKPTKPASRSRLRS-FNSGTAKDAFAQRPNSAPALMLSSPPPKMQEleGDSSPVFLRRSSLTSSLND-EED 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950    255 DGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQN 334
Cdd:pfam06617 152 DGFLEILDGDLENDEEVPSGMASLLTAPLVTDEIGERPTSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVKV 231

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 4757950    335 KRRRSVTPPEEQQEAEEP---KARVLRSKSLCHDEIEN 369
Cdd:pfam06617 232 KRRRSVAGTQVEAEEQEPespRSLLQRSKSLCHQEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 398-517 2.54e-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: 208.61  E-value: 2.54e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  398 LKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIApCSLDKRVILIFHCEFSS 477
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGV-ASKKKRRVLIFHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4757950  478 ERGPRMCRFIRERDRA--VNDYPSLYYPEMYILKGGYKEFFP 517
Cdd:cd01530  80 KRGPRMARHLRNLDRElnSNRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
381-550 1.25e-40

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 152.50  E-value: 1.25e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  381 DYSKAFLLQTV-------DGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFL 453
Cdd:COG5105 217 DFFKSFSNGEVfplptlgPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  454 LKSPiapcsLDKRVILIFHCEFSSERGPRMCRFIRERDRAVN--DYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPM 531
Cdd:COG5105 297 RHKP-----LTHPRALIFHCEFSSHRAPRLAQHLRNMDRMKNpdHYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTM 371

                       170       180       190
                ....*....|....*....|....*....|
gi 4757950  532 NHEA-----------FKDELKTFRLKTRSW 550
Cdd:COG5105 372 NNAEldyrclykmdkFRRNKKFFATKNNSF 401
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 419-520 3.64e-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: 3.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950     419 DKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFL------LKSPIAPCSLDKRVILIFHCeFSSERGPRMCRFIRErdr 492
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldileFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*...
gi 4757950     493 avndypsLYYPEMYILKGGYKEFFPQHP 520
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAGP 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 419-515 2.24e-12

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: 63.27  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950    419 DKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESF--LLKSPIAPCSLDKRVILIFHCEfSSERGPRMCRFIRErdravnd 496
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLKA------- 75

                          90
                  ....*....|....*....
gi 4757950    497 ypsLYYPEMYILKGGYKEF 515
Cdd:pfam00581  76 ---LGYKNVYVLDGGFEAW 91
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 411-450 9.71e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 38.27  E-value: 9.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 4757950   411 TGKFSNIVDKFV-IVDCRYPYEYEGGHIKTAVNLPLERDAE 450
Cdd:PRK11784   5 AQDFRALFLNDTpLIDVRSPIEFAEGHIPGAINLPLLNDEE 45
 
Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 99-369 9.71e-117

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: 346.74  E-value: 9.71e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950     99 MDSPSPMDPHMAEQTFEQAIQAASRIIrNEQFAIRRFQSMPVRLLGHSPVLRNitnSQAPDGRRkseAGSGAASSSGEDK 178
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVV-NLKMPIRRINSLPQRLLGSSPALKR---SQSLDSDI---YQPEQLSSQGENK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950    179 EN--DGFVFKMPWKPTHPSSTHAlAEWASRREAFAQRPSSAPDLMCLSPDRKMEV--EELSPLALGRFSLTPAEGDtEED 254
Cdd:pfam06617  74 ENvpEGFEFKKPTKPASRSRLRS-FNSGTAKDAFAQRPNSAPALMLSSPPPKMQEleGDSSPVFLRRSSLTSSLND-EED 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950    255 DGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQN 334
Cdd:pfam06617 152 DGFLEILDGDLENDEEVPSGMASLLTAPLVTDEIGERPTSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVKV 231

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 4757950    335 KRRRSVTPPEEQQEAEEP---KARVLRSKSLCHDEIEN 369
Cdd:pfam06617 232 KRRRSVAGTQVEAEEQEPespRSLLQRSKSLCHQEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 398-517 2.54e-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: 208.61  E-value: 2.54e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  398 LKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIApCSLDKRVILIFHCEFSS 477
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGV-ASKKKRRVLIFHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 4757950  478 ERGPRMCRFIRERDRA--VNDYPSLYYPEMYILKGGYKEFFP 517
Cdd:cd01530  80 KRGPRMARHLRNLDRElnSNRYPLLYYPEIYILEGGYKNFFE 121
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 398-517 4.83e-47

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: 160.26  E-value: 4.83e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  398 LKYISPETMVALLTGKFSNIVDKFVIVDCRYPyEYEGGHIKTAVNLPLErDAESFLLKSPIApCSLDKRVILIFHCEFSS 477
Cdd:cd01443   1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQ-SCYQTLPQVYAL-FSLAGVKLAIFYCGSSQ 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4757950  478 ERGPRMCRFIRERDRAvndyPSLYYPEMYILKGGYKEFFP 517
Cdd:cd01443  78 GRGPRAARWFADYLRK----VGESLPKSYILTGGIKAWYH 113
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
381-550 1.25e-40

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 152.50  E-value: 1.25e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  381 DYSKAFLLQTV-------DGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFL 453
Cdd:COG5105 217 DFFKSFSNGEVfplptlgPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  454 LKSPiapcsLDKRVILIFHCEFSSERGPRMCRFIRERDRAVN--DYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPM 531
Cdd:COG5105 297 RHKP-----LTHPRALIFHCEFSSHRAPRLAQHLRNMDRMKNpdHYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTM 371

                       170       180       190
                ....*....|....*....|....*....|
gi 4757950  532 NHEA-----------FKDELKTFRLKTRSW 550
Cdd:COG5105 372 NNAEldyrclykmdkFRRNKKFFATKNNSF 401
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 419-520 3.64e-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: 3.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950     419 DKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFL------LKSPIAPCSLDKRVILIFHCeFSSERGPRMCRFIRErdr 492
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldileFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*...
gi 4757950     493 avndypsLYYPEMYILKGGYKEFFPQHP 520
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAGP 99
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 419-515 1.93e-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: 68.87  E-value: 1.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  419 DKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKspiapcSLDKRVILIFHCEfSSERGPRMCRFIRErdravndyp 498
Cdd:cd00158   9 EDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALL------ELDKDKPIVVYCR-SGNRSARAAKLLRK--------- 72

                        90
                ....*....|....*..
gi 4757950  499 sLYYPEMYILKGGYKEF 515
Cdd:cd00158  73 -AGGTNVYNLEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 419-515 2.24e-12

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: 63.27  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950    419 DKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESF--LLKSPIAPCSLDKRVILIFHCEfSSERGPRMCRFIRErdravnd 496
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLKA------- 75

                          90
                  ....*....|....*....
gi 4757950    497 ypsLYYPEMYILKGGYKEF 515
Cdd:pfam00581  76 ---LGYKNVYVLDGGFEAW 91
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 398-512 9.86e-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: 62.05  E-value: 9.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  398 LKYISPETMVALLTgkfsNIVDKFVIVDCRyPYEYEGGHIKTAVNLPlerdAESFLLKSP--IAPCSLDKRVILIFHCEF 475
Cdd:cd01531   1 VSYISPAQLKGWIR----NGRPPFQVVDVR-DEDYAGGHIKGSWHYP----STRFKAQLNqlVQLLSGSKKDTVVFHCAL 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 4757950  476 SSERGP----RMCRFIRERDRAVNDypslyyPEMYILKGGY 512
Cdd:cd01531  72 SQVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGGF 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 397-514 4.57e-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: 56.90  E-value: 4.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  397 DLKYISPETMVALLTGkfsnivDKFVIVDCRYPYEYEGGHIKTAVNLPLERdaesflLKSPIAPCSLDKRVILifHCEfS 476
Cdd:COG0607   2 SVKEISPAELAELLES------EDAVLLDVREPEEFAAGHIPGAINIPLGE------LAERLDELPKDKPIVV--YCA-S 66

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 4757950  477 SERGPRMCRFIRERDravndypslyYPEMYILKGGYKE 514
Cdd:COG0607  67 GGRSAQAAALLRRAG----------YTNVYNLAGGIEA 94
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 401-523 1.32e-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: 44.97  E-value: 1.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  401 ISPETMVALLTGKfsniVDKFVIVDCRYPYEYEGGHIKTAVNLP-----LERDAESFLLKSPIAPC-------SLDKRVI 468
Cdd:cd01446   2 IDCAWLAALLREG----GERLLLLDCRPFLEYSSSHIRGAVNVCcptilRRRLQGGKILLQQLLSCpedrdrlRRGESLA 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757950  469 LIFHCEFSSERGPR------------MCRFIRERDRAvndypslyypemYILKGGYKEFFPQHPNFC 523
Cdd:cd01446  78 VVVYDESSSDRERLredstaesvlgkLLRKLQEGCSV------------YLLKGGFEQFSSEFPELC 132
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 422-473 2.10e-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: 38.02  E-value: 2.10e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4757950  422 VIVDCRYPYEYEGGHIKTAVNLPLER-------DAESFLLKSPIAPCSLDKRviLIFHC 473
Cdd:cd01519  17 VLIDVREPEELKTGKIPGAINIPLSSlpdalalSEEEFEKKYGFPKPSKDKE--LIFYC 73
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 419-446 3.10e-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: 36.86  E-value: 3.10e-03
                        10        20
                ....*....|....*....|....*...
gi 4757950  419 DKFVIVDCRYPYEYEGGHIKTAVNLPLE 446
Cdd:cd01524  12 DGVTLIDVRTPQEFEKGHIKGAINIPLD 39
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 404-473 4.31e-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: 37.33  E-value: 4.31e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757950  404 ETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKspiapcsLDKRVILIFHC 473
Cdd:cd01521   9 ETDCWDVAIALKNGKPDFVLVDVRSAEAYARGHVPGAINLPHREICENATAK-------LDKEKLFVVYC 71
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 419-448 4.96e-03

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: 4.96e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 4757950  419 DKFVIVDCRYPY-----EYEGGHIKTAVNLPLERD 448
Cdd:COG2897   8 PDVVILDVRWDLpdgraAYEAGHIPGAVFLDLDTD 42
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 411-450 9.71e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 38.27  E-value: 9.71e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 4757950   411 TGKFSNIVDKFV-IVDCRYPYEYEGGHIKTAVNLPLERDAE 450
Cdd:PRK11784   5 AQDFRALFLNDTpLIDVRSPIEFAEGHIPGAINLPLLNDEE 45
 
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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