NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|13623565|gb|AAH06395|]
View 

Cell division cycle 25 homolog B (S. pombe) [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 113-383 1.67e-116

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: 1.67e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565   113 MDSPSPMDPHMAEQTFEQAIQAASRIIrNEQFAIRRFQSMPVRLLGHSPVLRNitnSQAPDGRRkseAGSGAASSSGEDK 192
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVV-NLKMPIRRINSLPQRLLGSSPALKR---SQSLDSDI---YQPEQLSSQGENK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565   193 EN--DGFVFKMPWKPTHPSSTHAlAEWASRREAFAQRPSSAPDLMCLSPDRKMEV--EELSPLALGRFSLTPAEGDtEED 268
Cdd:pfam06617  74 ENvpEGFEFKKPTKPASRSRLRS-FNSGTAKDAFAQRPNSAPALMLSSPPPKMQEleGDSSPVFLRRSSLTSSLND-EED 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565   269 DGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQN 348
Cdd:pfam06617 152 DGFLEILDGDLENDEEVPSGMASLLTAPLVTDEIGERPTSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVKV 231

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 13623565   349 KRRRSVTPPEEQQEAEEP---KARVLRSKSLCHDEIEN 383
Cdd:pfam06617 232 KRRRSVAGTQVEAEEQEPespRSLLQRSKSLCHQEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 412-531 2.38e-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: 209.00  E-value: 2.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 412 LKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIApCSLDKRVILIFHCEFSS 491
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGV-ASKKKRRVLIFHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13623565 492 ERGPRMCRFIRERDRA--VNDYPSLYYPEMYILKGGYKEFFP 531
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 ...
 113-383 1.67e-116

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: 1.67e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565   113 MDSPSPMDPHMAEQTFEQAIQAASRIIrNEQFAIRRFQSMPVRLLGHSPVLRNitnSQAPDGRRkseAGSGAASSSGEDK 192
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVV-NLKMPIRRINSLPQRLLGSSPALKR---SQSLDSDI---YQPEQLSSQGENK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565   193 EN--DGFVFKMPWKPTHPSSTHAlAEWASRREAFAQRPSSAPDLMCLSPDRKMEV--EELSPLALGRFSLTPAEGDtEED 268
Cdd:pfam06617  74 ENvpEGFEFKKPTKPASRSRLRS-FNSGTAKDAFAQRPNSAPALMLSSPPPKMQEleGDSSPVFLRRSSLTSSLND-EED 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565   269 DGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQN 348
Cdd:pfam06617 152 DGFLEILDGDLENDEEVPSGMASLLTAPLVTDEIGERPTSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVKV 231

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 13623565   349 KRRRSVTPPEEQQEAEEP---KARVLRSKSLCHDEIEN 383
Cdd:pfam06617 232 KRRRSVAGTQVEAEEQEPespRSLLQRSKSLCHQEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 412-531 2.38e-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: 209.00  E-value: 2.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 412 LKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIApCSLDKRVILIFHCEFSS 491
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGV-ASKKKRRVLIFHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13623565 492 ERGPRMCRFIRERDRA--VNDYPSLYYPEMYILKGGYKEFFP 531
Cdd:cd01530  80 KRGPRMARHLRNLDRElnSNRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
395-564 1.53e-40

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 152.50  E-value: 1.53e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 395 DYSKAFLLQTV-------DGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFL 467
Cdd:COG5105 217 DFFKSFSNGEVfplptlgPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 468 LKSPiapcsLDKRVILIFHCEFSSERGPRMCRFIRERDRAVN--DYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPM 545
Cdd:COG5105 297 RHKP-----LTHPRALIFHCEFSSHRAPRLAQHLRNMDRMKNpdHYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTM 371

                       170       180       190
                ....*....|....*....|....*....|
gi 13623565 546 NHEA-----------FKDELKTFRLKTRSW 564
Cdd:COG5105 372 NNAEldyrclykmdkFRRNKKFFATKNNSF 401
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 433-534 2.93e-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: 2.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565    433 DKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFL------LKSPIAPCSLDKRVILIFHCeFSSERGPRMCRFIRErdr 506
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldileFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*...
gi 13623565    507 avndypsLYYPEMYILKGGYKEFFPQHP 534
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAGP 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 433-529 2.30e-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: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565   433 DKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESF--LLKSPIAPCSLDKRVILIFHCEfSSERGPRMCRFIRErdravnd 510
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLKA------- 75

                          90
                  ....*....|....*....
gi 13623565   511 ypsLYYPEMYILKGGYKEF 529
Cdd:pfam00581  76 ---LGYKNVYVLDGGFEAW 91
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 425-464 9.60e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 38.66  E-value: 9.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 13623565  425 TGKFSNIVDKFV-IVDCRYPYEYEGGHIKTAVNLPLERDAE 464
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 ...
 113-383 1.67e-116

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: 1.67e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565   113 MDSPSPMDPHMAEQTFEQAIQAASRIIrNEQFAIRRFQSMPVRLLGHSPVLRNitnSQAPDGRRkseAGSGAASSSGEDK 192
Cdd:pfam06617   1 LDSPSPLDPNEAEETFEKAIQASSRVV-NLKMPIRRINSLPQRLLGSSPALKR---SQSLDSDI---YQPEQLSSQGENK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565   193 EN--DGFVFKMPWKPTHPSSTHAlAEWASRREAFAQRPSSAPDLMCLSPDRKMEV--EELSPLALGRFSLTPAEGDtEED 268
Cdd:pfam06617  74 ENvpEGFEFKKPTKPASRSRLRS-FNSGTAKDAFAQRPNSAPALMLSSPPPKMQEleGDSSPVFLRRSSLTSSLND-EED 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565   269 DGFVDILESDLKDDDAVPPGMESLISAPLVKTLEKEEEKDLVMYSKCQRLFRSPSMPCSVIRPILKRLERPQDRDTPVQN 348
Cdd:pfam06617 152 DGFLEILDGDLENDEEVPSGMASLLTAPLVTDEIGERPTSLVIRCRPRRLFRSPSMPSPVIRPALKRPERPQDEDTPVKV 231

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 13623565   349 KRRRSVTPPEEQQEAEEP---KARVLRSKSLCHDEIEN 383
Cdd:pfam06617 232 KRRRSVAGTQVEAEEQEPespRSLLQRSKSLCHQEIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 412-531 2.38e-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: 209.00  E-value: 2.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 412 LKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKSPIApCSLDKRVILIFHCEFSS 491
Cdd:cd01530   1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGV-ASKKKRRVLIFHCEFSS 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13623565 492 ERGPRMCRFIRERDRA--VNDYPSLYYPEMYILKGGYKEFFP 531
Cdd:cd01530  80 KRGPRMARHLRNLDRElnSNRYPLLYYPEIYILEGGYKNFFE 121
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 412-531 5.90e-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: 5.90e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 412 LKYISPETMVALLTGKFSNIVDKFVIVDCRYPyEYEGGHIKTAVNLPLErDAESFLLKSPIApCSLDKRVILIFHCEFSS 491
Cdd:cd01443   1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQ-SCYQTLPQVYAL-FSLAGVKLAIFYCGSSQ 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 13623565 492 ERGPRMCRFIRERDRAvndyPSLYYPEMYILKGGYKEFFP 531
Cdd:cd01443  78 GRGPRAARWFADYLRK----VGESLPKSYILTGGIKAWYH 113
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
395-564 1.53e-40

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 152.50  E-value: 1.53e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 395 DYSKAFLLQTV-------DGKHQDLKYISPETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFL 467
Cdd:COG5105 217 DFFKSFSNGEVfplptlgPGKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLF 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 468 LKSPiapcsLDKRVILIFHCEFSSERGPRMCRFIRERDRAVN--DYPSLYYPEMYILKGGYKEFFPQHPNFCEPQDYRPM 545
Cdd:COG5105 297 RHKP-----LTHPRALIFHCEFSSHRAPRLAQHLRNMDRMKNpdHYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTM 371

                       170       180       190
                ....*....|....*....|....*....|
gi 13623565 546 NHEA-----------FKDELKTFRLKTRSW 564
Cdd:COG5105 372 NNAEldyrclykmdkFRRNKKFFATKNNSF 401
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 433-534 2.93e-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: 2.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565    433 DKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFL------LKSPIAPCSLDKRVILIFHCeFSSERGPRMCRFIRErdr 506
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldileFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*...
gi 13623565    507 avndypsLYYPEMYILKGGYKEFFPQHP 534
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAGP 99
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 433-529 1.98e-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: 1.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 433 DKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKspiapcSLDKRVILIFHCEfSSERGPRMCRFIRErdravndyp 512
Cdd:cd00158   9 EDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALL------ELDKDKPIVVYCR-SGNRSARAAKLLRK--------- 72

                        90
                ....*....|....*..
gi 13623565 513 sLYYPEMYILKGGYKEF 529
Cdd:cd00158  73 -AGGTNVYNLEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 433-529 2.30e-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: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565   433 DKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESF--LLKSPIAPCSLDKRVILIFHCEfSSERGPRMCRFIRErdravnd 510
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLKA------- 75

                          90
                  ....*....|....*....
gi 13623565   511 ypsLYYPEMYILKGGYKEF 529
Cdd:pfam00581  76 ---LGYKNVYVLDGGFEAW 91
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 412-526 1.01e-11

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: 1.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 412 LKYISPETMVALLTgkfsNIVDKFVIVDCRyPYEYEGGHIKTAVNLPlerdAESFLLKSP--IAPCSLDKRVILIFHCEF 489
Cdd:cd01531   1 VSYISPAQLKGWIR----NGRPPFQVVDVR-DEDYAGGHIKGSWHYP----STRFKAQLNqlVQLLSGSKKDTVVFHCAL 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 13623565 490 SSERGP----RMCRFIRERDRAVNDypslyyPEMYILKGGY 526
Cdd:cd01531  72 SQVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGGF 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 411-528 4.70e-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: 4.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 411 DLKYISPETMVALLTGkfsnivDKFVIVDCRYPYEYEGGHIKTAVNLPLERdaesflLKSPIAPCSLDKRVILifHCEfS 490
Cdd:COG0607   2 SVKEISPAELAELLES------EDAVLLDVREPEEFAAGHIPGAINIPLGE------LAERLDELPKDKPIVV--YCA-S 66

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 13623565 491 SERGPRMCRFIRERDravndypslyYPEMYILKGGYKE 528
Cdd:COG0607  67 GGRSAQAAALLRRAG----------YTNVYNLAGGIEA 94
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 415-537 1.33e-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: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 415 ISPETMVALLTGKfsniVDKFVIVDCRYPYEYEGGHIKTAVNLP-----LERDAESFLLKSPIAPC-------SLDKRVI 482
Cdd:cd01446   2 IDCAWLAALLREG----GERLLLLDCRPFLEYSSSHIRGAVNVCcptilRRRLQGGKILLQQLLSCpedrdrlRRGESLA 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13623565 483 LIFHCEFSSERGPR------------MCRFIRERDRAvndypslyypemYILKGGYKEFFPQHPNFC 537
Cdd:cd01446  78 VVVYDESSSDRERLredstaesvlgkLLRKLQEGCSV------------YLLKGGFEQFSSEFPELC 132
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 436-487 2.13e-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: 2.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13623565 436 VIVDCRYPYEYEGGHIKTAVNLPLER-------DAESFLLKSPIAPCSLDKRviLIFHC 487
Cdd:cd01519  17 VLIDVREPEELKTGKIPGAINIPLSSlpdalalSEEEFEKKYGFPKPSKDKE--LIFYC 73
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 433-460 3.18e-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: 3.18e-03
                        10        20
                ....*....|....*....|....*...
gi 13623565 433 DKFVIVDCRYPYEYEGGHIKTAVNLPLE 460
Cdd:cd01524  12 DGVTLIDVRTPQEFEKGHIKGAINIPLD 39
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 418-487 4.43e-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: 4.43e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13623565 418 ETMVALLTGKFSNIVDKFVIVDCRYPYEYEGGHIKTAVNLPLERDAESFLLKspiapcsLDKRVILIFHC 487
Cdd:cd01521   9 ETDCWDVAIALKNGKPDFVLVDVRSAEAYARGHVPGAINLPHREICENATAK-------LDKEKLFVVYC 71
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 433-462 5.11e-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: 5.11e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 13623565 433 DKFVIVDCRYPY-----EYEGGHIKTAVNLPLERD 462
Cdd:COG2897   8 PDVVILDVRWDLpdgraAYEAGHIPGAVFLDLDTD 42
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 425-464 9.60e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 38.66  E-value: 9.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 13623565  425 TGKFSNIVDKFV-IVDCRYPYEYEGGHIKTAVNLPLERDAE 464
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH