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Conserved domains on  [gi|1937370077|ref|NP_598255|]
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M-phase inducer phosphatase 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 ...
 86-329 2.67e-86

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: 267.39  E-value: 2.67e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077  86 LDSPGPLDSKE----------------NLEISLRRINCLPQKLLGCSPALKRShsDSLDHDIF---QLIDQDENKEN--E 144
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPQRLLGSSPALKRS--QSLDSDIYqpeQLSSQGENKENvpE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 145 AFEFKKPIRPASRGCLNAHVHEESKDPFTHRQNSAPARMLSSNESDISE-SGNFSPLFTPQSPVKATL-SDEDDGFIDLL 222
Cdd:pfam06617  79 GFEFKKPTKPASRSRLRSFNSGTAKDAFAQRPNSAPALMLSSPPPKMQElEGDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 223 DGeNLKNDEETPSCMSSLWTAPLVM----RRPTNLADRC---GLFDspsPCSSTSSCSTRAVKRADRSHEESPRG-TKRR 294
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigERPTSLVIRCrprRLFR---SPSMPSPVIRPALKRPERPQDEDTPVkVKRR 234

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1937370077 295 KSSEASPVKADVPEPTQ---LPHQSLSLTSFpkgTIEN 329
Cdd:pfam06617 235 RSVAGTQVEAEEQEPESprsLLQRSKSLCHQ---EIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 358-475 1.03e-66

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: 211.31  E-value: 1.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 358 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEEFLLKKPIVPADGKRVIVVFHCEFSSE 437
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1937370077 438 RGPRMCRYVRERDRL--GNEYPKLHYPELYVLKGGYKEFF 475
Cdd:cd01530    81 RGPRMARHLRNLDRElnSNRYPLLYYPEIYILEGGYKNFF 120
 
Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 86-329 2.67e-86

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: 267.39  E-value: 2.67e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077  86 LDSPGPLDSKE----------------NLEISLRRINCLPQKLLGCSPALKRShsDSLDHDIF---QLIDQDENKEN--E 144
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPQRLLGSSPALKRS--QSLDSDIYqpeQLSSQGENKENvpE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 145 AFEFKKPIRPASRGCLNAHVHEESKDPFTHRQNSAPARMLSSNESDISE-SGNFSPLFTPQSPVKATL-SDEDDGFIDLL 222
Cdd:pfam06617  79 GFEFKKPTKPASRSRLRSFNSGTAKDAFAQRPNSAPALMLSSPPPKMQElEGDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 223 DGeNLKNDEETPSCMSSLWTAPLVM----RRPTNLADRC---GLFDspsPCSSTSSCSTRAVKRADRSHEESPRG-TKRR 294
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigERPTSLVIRCrprRLFR---SPSMPSPVIRPALKRPERPQDEDTPVkVKRR 234

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1937370077 295 KSSEASPVKADVPEPTQ---LPHQSLSLTSFpkgTIEN 329
Cdd:pfam06617 235 RSVAGTQVEAEEQEPESprsLLQRSKSLCHQ---EIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 358-475 1.03e-66

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: 211.31  E-value: 1.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 358 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEEFLLKKPIVPADGKRVIVVFHCEFSSE 437
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1937370077 438 RGPRMCRYVRERDRL--GNEYPKLHYPELYVLKGGYKEFF 475
Cdd:cd01530    81 RGPRMARHLRNLDRElnSNRYPLLYYPEIYILEGGYKNFF 120
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
353-509 5.73e-37

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 141.72  E-value: 5.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 353 GKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEEFLLKKPIVpadgKRVIVVFHC 432
Cdd:COG5105   236 GKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT----HPRALIFHC 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 433 EFSSERGPRMCRYVRERDRLGNE--YPKLHYPELYVLKGGYKEFFLKCQSHCEPPSYRPMHHED-----------FKEDL 499
Cdd:COG5105   312 EFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAEldyrclykmdkFRRNK 391

                         170
                  ....*....|
gi 1937370077 500 KKFRTKSRTW 509
Cdd:COG5105   392 KFFATKNNSF 401
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 379-478 1.06e-21

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: 89.83  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077  379 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEEFLLKKPIVPAD-------GKRVIVVFHCeFSSERGPRMCRYVRERDr 451
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlglDKDKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
gi 1937370077  452 lgneypklhYPELYVLKGGYKEFFLKC 478
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 379-474 8.94e-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: 64.04  E-value: 8.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 379 KEFVIIDCRYPYEYEGGHIKGAVNLH----MEEEVEEFLLKKPIVPADGKRVIVVfHCEfSSERGPRMCRYVRerdRLGn 454
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPlsslSLPPLPLLELLEKLLELLKDKPIVV-YCN-SGNRAAAAAALLK---ALG- 77

                          90       100
                  ....*....|....*....|
gi 1937370077 455 eypklhYPELYVLKGGYKEF 474
Cdd:pfam00581  78 ------YKNVYVLDGGFEAW 91
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
359-419 6.13e-03

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 38.67  E-value: 6.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937370077 359 KYISPEimasvlngKFANLI--KEFVIIDCRYPYEYEGGHIKGAVNLHME------EEVEEFL--LK-KPIV 419
Cdd:PRK00142  112 TYLKPK--------EVNELLddPDVVFIDMRNDYEYEIGHFENAIEPDIEtfrefpPWVEENLdpLKdKKVV 175
 
Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 86-329 2.67e-86

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: 267.39  E-value: 2.67e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077  86 LDSPGPLDSKE----------------NLEISLRRINCLPQKLLGCSPALKRShsDSLDHDIF---QLIDQDENKEN--E 144
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPQRLLGSSPALKRS--QSLDSDIYqpeQLSSQGENKENvpE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 145 AFEFKKPIRPASRGCLNAHVHEESKDPFTHRQNSAPARMLSSNESDISE-SGNFSPLFTPQSPVKATL-SDEDDGFIDLL 222
Cdd:pfam06617  79 GFEFKKPTKPASRSRLRSFNSGTAKDAFAQRPNSAPALMLSSPPPKMQElEGDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 223 DGeNLKNDEETPSCMSSLWTAPLVM----RRPTNLADRC---GLFDspsPCSSTSSCSTRAVKRADRSHEESPRG-TKRR 294
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigERPTSLVIRCrprRLFR---SPSMPSPVIRPALKRPERPQDEDTPVkVKRR 234

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1937370077 295 KSSEASPVKADVPEPTQ---LPHQSLSLTSFpkgTIEN 329
Cdd:pfam06617 235 RSVAGTQVEAEEQEPESprsLLQRSKSLCHQ---EIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 358-475 1.03e-66

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: 211.31  E-value: 1.03e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 358 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEEFLLKKPIVPADGKRVIVVFHCEFSSE 437
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1937370077 438 RGPRMCRYVRERDRL--GNEYPKLHYPELYVLKGGYKEFF 475
Cdd:cd01530    81 RGPRMARHLRNLDRElnSNRYPLLYYPEIYILEGGYKNFF 120
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
353-509 5.73e-37

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 141.72  E-value: 5.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 353 GKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEEFLLKKPIVpadgKRVIVVFHC 432
Cdd:COG5105   236 GKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT----HPRALIFHC 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 433 EFSSERGPRMCRYVRERDRLGNE--YPKLHYPELYVLKGGYKEFFLKCQSHCEPPSYRPMHHED-----------FKEDL 499
Cdd:COG5105   312 EFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAEldyrclykmdkFRRNK 391

                         170
                  ....*....|
gi 1937370077 500 KKFRTKSRTW 509
Cdd:COG5105   392 KFFATKNNSF 401
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 358-475 2.32e-34

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: 125.21  E-value: 2.32e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 358 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPyEYEGGHIKGAVNLHMEEeVEEFLLKKPIVPADGKRVIVVFHCEFSSE 437
Cdd:cd01443     1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQS-CYQTLPQVYALFSLAGVKLAIFYCGSSQG 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1937370077 438 RGPRMCRYVRERDRLGNEYpklhYPELYVLKGGYKEFF 475
Cdd:cd01443    79 RGPRAARWFADYLRKVGES----LPKSYILTGGIKAWY 112
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 379-478 1.06e-21

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: 89.83  E-value: 1.06e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077  379 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEEFLLKKPIVPAD-------GKRVIVVFHCeFSSERGPRMCRYVRERDr 451
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlglDKDKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
gi 1937370077  452 lgneypklhYPELYVLKGGYKEFFLKC 478
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 379-474 7.23e-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: 66.94  E-value: 7.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 379 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEEFLLKKPivpadGKRVIVVFHCEfSSERGPRMCRYVRerdrlgneypK 458
Cdd:cd00158     9 EDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLEL-----DKDKPIVVYCR-SGNRSARAAKLLR----------K 72

                          90
                  ....*....|....*.
gi 1937370077 459 LHYPELYVLKGGYKEF 474
Cdd:cd00158    73 AGGTNVYNLEGGMLAW 88
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 358-482 2.17e-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: 66.67  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 358 LKYISPeimaSVLNGKFANLIKEFVIIDCRyPYEYEGGHIKGAVNL---HMEEEVEEFLLKKpivpADGKRVIVVFHCEF 434
Cdd:cd01531     1 VSYISP----AQLKGWIRNGRPPFQVVDVR-DEDYAGGHIKGSWHYpstRFKAQLNQLVQLL----SGSKKDTVVFHCAL 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1937370077 435 SSERGP----RMCRYVRERDRLGNEypklhyPELYVLKGGykefFLKCQSHC 482
Cdd:cd01531    72 SQVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGG----FNAWESSY 113
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 379-474 8.94e-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: 64.04  E-value: 8.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 379 KEFVIIDCRYPYEYEGGHIKGAVNLH----MEEEVEEFLLKKPIVPADGKRVIVVfHCEfSSERGPRMCRYVRerdRLGn 454
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPlsslSLPPLPLLELLEKLLELLKDKPIVV-YCN-SGNRAAAAAALLK---ALG- 77

                          90       100
                  ....*....|....*....|
gi 1937370077 455 eypklhYPELYVLKGGYKEF 474
Cdd:pfam00581  78 ------YKNVYVLDGGFEAW 91
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 357-473 1.06e-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: 58.83  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 357 DLKYISPEIMASVLNGKfanlikEFVIIDCRYPYEYEGGHIKGAVNL---HMEEEVEEFLLKKPIvpadgkrvivVFHCE 433
Cdd:COG0607     2 SVKEISPAELAELLESE------DAVLLDVREPEEFAAGHIPGAINIplgELAERLDELPKDKPI----------VVYCA 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1937370077 434 fSSERGPRMCRYVRerdRLGneypklhYPELYVLKGGYKE 473
Cdd:COG0607    66 -SGGRSAQAAALLR---RAG-------YTNVYNLAGGIEA 94
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 379-472 1.28e-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: 38.02  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 379 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEeveeflLKKPIVPADGKRVIVVfHCEfSSERGprmcrYVRERDRLGNEYpk 458
Cdd:cd01524    12 DGVTLIDVRTPQEFEKGHIKGAINIPLDE------LRDRLNELPKDKEIIV-YCA-VGLRG-----YIAARILTQNGF-- 76

                          90
                  ....*....|....
gi 1937370077 459 lhypELYVLKGGYK 472
Cdd:cd01524    77 ----KVKNLDGGYK 86
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 359-419 1.36e-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: 38.33  E-value: 1.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937370077 359 KYISPEIMASVLNGKfanlikEFVIIDCRYPYEYEGGHIKGAVNLHME---------EEVEEFLLKKPIV 419
Cdd:cd01518     2 TYLSPAEWNELLEDP------EVVLLDVRNDYEYDIGHFKGAVNPDVDtfrefpfwlDENLDLLKGKKVL 65
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 379-409 2.83e-03

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 39.77  E-value: 2.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1937370077 379 KEFVIIDCRYPY-----EYEGGHIKGAVNLHMEEEV 409
Cdd:COG2897     8 PDVVILDVRWDLpdgraAYEAGHIPGAVFLDLDTDL 43
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 379-432 3.29e-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: 37.25  E-value: 3.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937370077 379 KEFVIIDCRYPYEYEGGHIKGAVN---------LHMEEevEEFLLK----KPivPADGKrviVVFHC 432
Cdd:cd01519    14 PNKVLIDVREPEELKTGKIPGAINiplsslpdaLALSE--EEFEKKygfpKP--SKDKE---LIFYC 73
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 379-432 3.90e-03

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 39.39  E-value: 3.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937370077 379 KEFVIIDCRYPYEYEG---------GHIKGAVNLHME------------EEVEEFLLKKPIVPadGKRVIVvfHC 432
Cdd:COG2897   152 PDAVLVDARSPERYRGevepidpraGHIPGAVNLPWTdlldedgtfksaEELRALFAALGIDP--DKPVIT--YC 222
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 364-419 5.08e-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: 36.60  E-value: 5.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937370077 364 EIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEE------EVEEFLLKKPIV 419
Cdd:cd01528     1 QISVAELAEWLADEREEPVLIDVREPEELEIAFLPGFLHLPMSEiperskELDSDNPDKDIV 62
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
359-419 6.13e-03

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 38.67  E-value: 6.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937370077 359 KYISPEimasvlngKFANLI--KEFVIIDCRYPYEYEGGHIKGAVNLHME------EEVEEFL--LK-KPIV 419
Cdd:PRK00142  112 TYLKPK--------EVNELLddPDVVFIDMRNDYEYEIGHFENAIEPDIEtfrefpPWVEENLdpLKdKKVV 175
 
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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