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Conserved domains on  [gi|966927459|ref|XP_014986510|]
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M-phase inducer phosphatase 1 isoform X3 [Macaca mulatta]

Protein Classification

M-inducer_phosp and Cdc25 domain-containing protein( domain architecture ID 10273867)

M-inducer_phosp and Cdc25 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 317-435 4.89e-68

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: 213.62  E-value: 4.89e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 317 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSE 396
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 966927459 397 RGPRMCRYVRERDRLGN--EYPKLHYPELYVLKGGYKEFFM 435
Cdd:cd01530   81 RGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
M-inducer_phosp super family cl05906
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 86-288 4.92e-66

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.


The actual alignment was detected with superfamily member pfam06617:

Pssm-ID: 461962  Cd Length: 269  Bit Score: 213.84  E-value: 4.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459   86 LDSPGPLDSKE----------------NLENPMRRIHSLPQKLLGCSPALKRShsDSLDHDIF---QLIDPDENKEN--- 143
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPQRLLGSSPALKRS--QSLDSDIYqpeQLSSQGENKENvpe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459  144 ---------------------------------------LSSNERDSSERG-NFIPLFTPQSPVTATL-SDEDDGFVDLL 182
Cdd:pfam06617  79 gfefkkptkpasrsrlrsfnsgtakdafaqrpnsapalmLSSPPPKMQELEgDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459  183 DGeNLKNEEETPSCMASLWTAPLVM-----RTTNLDNRCK---LFDSPSLCSSSTRSVLKRPERSQEESPPGNTKRRKSM 254
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigeRPTSLVIRCRprrLFRSPSMPSPVIRPALKRPERPQDEDTPVKVKRRRSV 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 966927459  255 SGANPK-ESTSPEKAHETLHQSLSPASSpkgTIEN 288
Cdd:pfam06617 238 AGTQVEaEEQEPESPRSLLQRSKSLCHQ---EIEN 269
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 317-435 4.89e-68

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: 213.62  E-value: 4.89e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 317 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSE 396
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 966927459 397 RGPRMCRYVRERDRLGN--EYPKLHYPELYVLKGGYKEFFM 435
Cdd:cd01530   81 RGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 86-288 4.92e-66

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: 213.84  E-value: 4.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459   86 LDSPGPLDSKE----------------NLENPMRRIHSLPQKLLGCSPALKRShsDSLDHDIF---QLIDPDENKEN--- 143
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPQRLLGSSPALKRS--QSLDSDIYqpeQLSSQGENKENvpe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459  144 ---------------------------------------LSSNERDSSERG-NFIPLFTPQSPVTATL-SDEDDGFVDLL 182
Cdd:pfam06617  79 gfefkkptkpasrsrlrsfnsgtakdafaqrpnsapalmLSSPPPKMQELEgDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459  183 DGeNLKNEEETPSCMASLWTAPLVM-----RTTNLDNRCK---LFDSPSLCSSSTRSVLKRPERSQEESPPGNTKRRKSM 254
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigeRPTSLVIRCRprrLFRSPSMPSPVIRPALKRPERPQDEDTPVKVKRRRSV 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 966927459  255 SGANPK-ESTSPEKAHETLHQSLSPASSpkgTIEN 288
Cdd:pfam06617 238 AGTQVEaEEQEPESPRSLLQRSKSLCHQ---EIEN 269
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
312-468 8.00e-38

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 143.26  E-value: 8.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 312 GKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVptdgKRVIVVFHC 391
Cdd:COG5105  236 GKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT----HPRALIFHC 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 392 EFSSERGPRMCRYVRERDRLGNE--YPKLHYPELYVLKGGYKEFFMKCQSYCEPPSYRPMHHED-----------FKEDL 458
Cdd:COG5105  312 EFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAEldyrclykmdkFRRNK 391

                        170
                 ....*....|
gi 966927459 459 KKFRTKSRTW 468
Cdd:COG5105  392 KFFATKNNSF 401
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 338-437 6.00e-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: 90.21  E-value: 6.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459   338 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTD-------GKRVIVVFHCeFSSERGPRMCRYVRERDr 410
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlglDKDKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
gi 966927459   411 lgneypklhYPELYVLKGGYKEFFMKC 437
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 338-433 3.75e-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: 65.20  E-value: 3.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459  338 KEFVIIDCRYPYEYEGGHIKGAVNLH----MEEEVEDFLLKKPIVPTDGKRVIVVfHCEfSSERGPRMCRYVRerdRLGn 413
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPlsslSLPPLPLLELLEKLLELLKDKPIVV-YCN-SGNRAAAAAALLK---ALG- 77

                          90       100
                  ....*....|....*....|
gi 966927459  414 eypklhYPELYVLKGGYKEF 433
Cdd:pfam00581  78 ------YKNVYVLDGGFEAW 91
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
318-398 1.74e-03

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 40.22  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 318 KYISPEimasvlngKFANLI--KEFVIIDCRYPYEYEGGHIKGAVN---------LHMEEEVEDFLLKKPIVP--TDGKR 384
Cdd:PRK00142 112 TYLKPK--------EVNELLddPDVVFIDMRNDYEYEIGHFENAIEpdietfrefPPWVEENLDPLKDKKVVMycTGGIR 183

                         90
                 ....*....|....*...
gi 966927459 385 vivvfhCE-FSS---ERG 398
Cdd:PRK00142 184 ------CEkASAwmkHEG 195
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 317-435 4.89e-68

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: 213.62  E-value: 4.89e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 317 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTDGKRVIVVFHCEFSSE 396
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 966927459 397 RGPRMCRYVRERDRLGN--EYPKLHYPELYVLKGGYKEFFM 435
Cdd:cd01530   81 RGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 86-288 4.92e-66

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: 213.84  E-value: 4.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459   86 LDSPGPLDSKE----------------NLENPMRRIHSLPQKLLGCSPALKRShsDSLDHDIF---QLIDPDENKEN--- 143
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPQRLLGSSPALKRS--QSLDSDIYqpeQLSSQGENKENvpe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459  144 ---------------------------------------LSSNERDSSERG-NFIPLFTPQSPVTATL-SDEDDGFVDLL 182
Cdd:pfam06617  79 gfefkkptkpasrsrlrsfnsgtakdafaqrpnsapalmLSSPPPKMQELEgDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459  183 DGeNLKNEEETPSCMASLWTAPLVM-----RTTNLDNRCK---LFDSPSLCSSSTRSVLKRPERSQEESPPGNTKRRKSM 254
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigeRPTSLVIRCRprrLFRSPSMPSPVIRPALKRPERPQDEDTPVKVKRRRSV 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 966927459  255 SGANPK-ESTSPEKAHETLHQSLSPASSpkgTIEN 288
Cdd:pfam06617 238 AGTQVEaEEQEPESPRSLLQRSKSLCHQ---EIEN 269
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
312-468 8.00e-38

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 143.26  E-value: 8.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 312 GKHQDLKYISPEIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVptdgKRVIVVFHC 391
Cdd:COG5105  236 GKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT----HPRALIFHC 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 392 EFSSERGPRMCRYVRERDRLGNE--YPKLHYPELYVLKGGYKEFFMKCQSYCEPPSYRPMHHED-----------FKEDL 458
Cdd:COG5105  312 EFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAEldyrclykmdkFRRNK 391

                        170
                 ....*....|
gi 966927459 459 KKFRTKSRTW 468
Cdd:COG5105  392 KFFATKNNSF 401
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 317-434 1.28e-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: 125.60  E-value: 1.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 317 LKYISPEIMASVLNGKFANLIKEFVIIDCRYPyEYEGGHIKGAVNLHMEEeVEDFLLKKPIVPTDGKRVIVVFHCEFSSE 396
Cdd:cd01443    1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQS-CYQTLPQVYALFSLAGVKLAIFYCGSSQG 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 966927459 397 RGPRMCRYVRERDRLGNEYpklhYPELYVLKGGYKEFF 434
Cdd:cd01443   79 RGPRAARWFADYLRKVGES----LPKSYILTGGIKAWY 112
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 338-437 6.00e-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: 90.21  E-value: 6.00e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459   338 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPIVPTD-------GKRVIVVFHCeFSSERGPRMCRYVRERDr 410
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlglDKDKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
gi 966927459   411 lgneypklhYPELYVLKGGYKEFFMKC 437
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 338-433 1.10e-13

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: 66.55  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 338 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKKPivptdGKRVIVVFHCEfSSERGPRMCRYVRerdrlgneypK 417
Cdd:cd00158    9 EDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLEL-----DKDKPIVVYCR-SGNRSARAAKLLR----------K 72

                         90
                 ....*....|....*.
gi 966927459 418 LHYPELYVLKGGYKEF 433
Cdd:cd00158   73 AGGTNVYNLEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 338-433 3.75e-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: 65.20  E-value: 3.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459  338 KEFVIIDCRYPYEYEGGHIKGAVNLH----MEEEVEDFLLKKPIVPTDGKRVIVVfHCEfSSERGPRMCRYVRerdRLGn 413
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPlsslSLPPLPLLELLEKLLELLKDKPIVV-YCN-SGNRAAAAAALLK---ALG- 77

                          90       100
                  ....*....|....*....|
gi 966927459  414 eypklhYPELYVLKGGYKEF 433
Cdd:pfam00581  78 ------YKNVYVLDGGFEAW 91
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 317-430 4.18e-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: 62.82  E-value: 4.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 317 LKYISPeimaSVLNGKFANLIKEFVIIDCRyPYEYEGGHIKGAVNL-------HMEEEVEDFLLKKPIVptdgkrviVVF 389
Cdd:cd01531    1 VSYISP----AQLKGWIRNGRPPFQVVDVR-DEDYAGGHIKGSWHYpstrfkaQLNQLVQLLSGSKKDT--------VVF 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 966927459 390 HCEFSSERGP----RMCRYVRERDRLGNEypklhyPELYVLKGGY 430
Cdd:cd01531   68 HCALSQVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGGF 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 316-432 1.26e-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: 58.44  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 316 DLKYISPEIMASVLNGKfanlikEFVIIDCRYPYEYEGGHIKGAVNLHMeEEVEDFLLKkpiVPTDGKrviVVFHCEfSS 395
Cdd:COG0607    2 SVKEISPAELAELLESE------DAVLLDVREPEEFAAGHIPGAINIPL-GELAERLDE---LPKDKP---IVVYCA-SG 67

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966927459 396 ERGPRMCRYVRerdRLGneypklhYPELYVLKGGYKE 432
Cdd:COG0607   68 GRSAQAAALLR---RAG-------YTNVYNLAGGIEA 94
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 318-429 1.07e-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: 41.41  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 318 KYISPEIMASVLNGKfanlikEFVIIDCRYPYEYEGGHIKGAVNLHME---------EEVEDFLLKKPIVP--TDGKRvi 386
Cdd:cd01518    2 TYLSPAEWNELLEDP------EVVLLDVRNDYEYDIGHFKGAVNPDVDtfrefpfwlDENLDLLKGKKVLMycTGGIR-- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966927459 387 vvfhCEFSSErgprmcrYVRERdrlGNEypklhypELYVLKGG 429
Cdd:cd01518   74 ----CEKASA-------YLKER---GFK-------NVYQLKGG 95
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 338-370 4.95e-04

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 41.70  E-value: 4.95e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 966927459 338 KEFVIIDCRYPY-----EYEGGHIKGAVNLHMEEEVED 370
Cdd:COG2897    8 PDVVILDVRWDLpdgraAYEAGHIPGAVFLDLDTDLSD 45
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 338-431 1.04e-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: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 338 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEevedflLKKPIVPTDGKRVIVVfHCEfSSERGprmcrYVRERDRLGNEYpk 417
Cdd:cd01524   12 DGVTLIDVRTPQEFEKGHIKGAINIPLDE------LRDRLNELPKDKEIIV-YCA-VGLRG-----YIAARILTQNGF-- 76

                         90
                 ....*....|....
gi 966927459 418 lhypELYVLKGGYK 431
Cdd:cd01524   77 ----KVKNLDGGYK 86
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
318-398 1.74e-03

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 40.22  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966927459 318 KYISPEimasvlngKFANLI--KEFVIIDCRYPYEYEGGHIKGAVN---------LHMEEEVEDFLLKKPIVP--TDGKR 384
Cdd:PRK00142 112 TYLKPK--------EVNELLddPDVVFIDMRNDYEYEIGHFENAIEpdietfrefPPWVEENLDPLKDKKVVMycTGGIR 183

                         90
                 ....*....|....*...
gi 966927459 385 vivvfhCE-FSS---ERG 398
Cdd:PRK00142 184 ------CEkASAwmkHEG 195
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 338-391 2.18e-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: 37.63  E-value: 2.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966927459 338 KEFVIIDCRYPYEYEGGHIKGAVN---------LHMEEevEDFLLK----KPivPTDGKrviVVFHC 391
Cdd:cd01519   14 PNKVLIDVREPEELKTGKIPGAINiplsslpdaLALSE--EEFEKKygfpKP--SKDKE---LIFYC 73
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 338-391 4.34e-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: 4.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966927459 338 KEFVIIDCRYPYEYEG---------GHIKGAVNLHME------------EEVEDFLLKKPIvpTDGKRVIVvfHC 391
Cdd:COG2897  152 PDAVLVDARSPERYRGevepidpraGHIPGAVNLPWTdlldedgtfksaEELRALFAALGI--DPDKPVIT--YC 222
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 323-378 6.22e-03

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


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 36.22  E-value: 6.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966927459 323 EIMASVLNGKFANLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEE------EVEDFLLKKPIV 378
Cdd:cd01528    1 QISVAELAEWLADEREEPVLIDVREPEELEIAFLPGFLHLPMSEiperskELDSDNPDKDIV 62
 
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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