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Conserved domains on  [gi|568963442|ref|XP_006511993|]
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M-phase inducer phosphatase 1 isoform X2 [Mus musculus]

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
M-inducer_phosp super family cl05906
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 85-325 2.08e-79

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: 249.28  E-value: 2.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442   85 LDSPGPLDSKE----------------NLEISLTRINSLP-KLLGCSPALKRShsDSLDHDTFH---LIDQDENKEN--E 142
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPqRLLGSSPALKRS--QSLDSDIYQpeqLSSQGENKENvpE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442  143 AFEFKKPIRPASRH-----IYEESKDPFTHRQNSAPARMLSSNESE----SGNFSPLFIPQSPVKATL-SDEDDGFIDLL 212
Cdd:pfam06617  79 GFEFKKPTKPASRSrlrsfNSGTAKDAFAQRPNSAPALMLSSPPPKmqelEGDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442  213 DGeNMKNDEETPSCMASLWTAPLVM----RRPANLVgpvsdpkaDRC---GLFDSPSPCGSSTRAVLKRADRSHEEPPRG 285
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigERPTSLV--------IRCrprRLFRSPSMPSPVIRPALKRPERPQDEDTPV 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 568963442  286 -TKRRKSVPSP-VKAKADVPE-PAQLPSQSLSLMSSpkgTIEN 325
Cdd:pfam06617 230 kVKRRRSVAGTqVEAEEQEPEsPRSLLQRSKSLCHQ---EIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 354-471 6.07e-67

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: 211.69  E-value: 6.07e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 354 LKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTDGKRVIVVFHCEFSSE 433
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568963442 434 RGPRMCRYVRERDRLGN--EYPKLHYPELYVLKGGYKEFF 471
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 ...
 85-325 2.08e-79

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: 249.28  E-value: 2.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442   85 LDSPGPLDSKE----------------NLEISLTRINSLP-KLLGCSPALKRShsDSLDHDTFH---LIDQDENKEN--E 142
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPqRLLGSSPALKRS--QSLDSDIYQpeqLSSQGENKENvpE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442  143 AFEFKKPIRPASRH-----IYEESKDPFTHRQNSAPARMLSSNESE----SGNFSPLFIPQSPVKATL-SDEDDGFIDLL 212
Cdd:pfam06617  79 GFEFKKPTKPASRSrlrsfNSGTAKDAFAQRPNSAPALMLSSPPPKmqelEGDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442  213 DGeNMKNDEETPSCMASLWTAPLVM----RRPANLVgpvsdpkaDRC---GLFDSPSPCGSSTRAVLKRADRSHEEPPRG 285
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigERPTSLV--------IRCrprRLFRSPSMPSPVIRPALKRPERPQDEDTPV 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 568963442  286 -TKRRKSVPSP-VKAKADVPE-PAQLPSQSLSLMSSpkgTIEN 325
Cdd:pfam06617 230 kVKRRRSVAGTqVEAEEQEPEsPRSLLQRSKSLCHQ---EIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 354-471 6.07e-67

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: 211.69  E-value: 6.07e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 354 LKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTDGKRVIVVFHCEFSSE 433
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568963442 434 RGPRMCRYVRERDRLGN--EYPKLHYPELYVLKGGYKEFF 471
Cdd:cd01530   81 RGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFF 120
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
349-505 1.90e-36

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 140.17  E-value: 1.90e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 349 GKHQDLKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVptdgKRVIVVFHC 428
Cdd:COG5105  236 GKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT----HPRALIFHC 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 429 EFSSERGPRMCRYVRERDRLGNE--YPKLHYPELYVLKGGYKEFFLKCQSHCEPPSYRPMHHED-----------FKEDL 495
Cdd:COG5105  312 EFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAEldyrclykmdkFRRNK 391

                        170
                 ....*....|
gi 568963442 496 KKFRTKSRTW 505
Cdd:COG5105  392 KFFATKNNSF 401
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 375-474 8.24e-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: 8.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442   375 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTD-------GKRVIVVFHCeFSSERGPRMCRYVRERDr 447
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlglDKDKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
gi 568963442   448 lgneypklhYPELYVLKGGYKEFFLKC 474
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 375-470 1.02e-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: 64.04  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442  375 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTD---GKRVIVVFHCEfSSERGPRMCRYVRerdRLGne 451
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLlelLKDKPIVVYCN-SGNRAAAAAALLK---ALG-- 77

                          90
                  ....*....|....*....
gi 568963442  452 ypklhYPELYVLKGGYKEF 470
Cdd:pfam00581  78 -----YKNVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 85-325 2.08e-79

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: 249.28  E-value: 2.08e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442   85 LDSPGPLDSKE----------------NLEISLTRINSLP-KLLGCSPALKRShsDSLDHDTFH---LIDQDENKEN--E 142
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPqRLLGSSPALKRS--QSLDSDIYQpeqLSSQGENKENvpE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442  143 AFEFKKPIRPASRH-----IYEESKDPFTHRQNSAPARMLSSNESE----SGNFSPLFIPQSPVKATL-SDEDDGFIDLL 212
Cdd:pfam06617  79 GFEFKKPTKPASRSrlrsfNSGTAKDAFAQRPNSAPALMLSSPPPKmqelEGDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442  213 DGeNMKNDEETPSCMASLWTAPLVM----RRPANLVgpvsdpkaDRC---GLFDSPSPCGSSTRAVLKRADRSHEEPPRG 285
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigERPTSLV--------IRCrprRLFRSPSMPSPVIRPALKRPERPQDEDTPV 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 568963442  286 -TKRRKSVPSP-VKAKADVPE-PAQLPSQSLSLMSSpkgTIEN 325
Cdd:pfam06617 230 kVKRRRSVAGTqVEAEEQEPEsPRSLLQRSKSLCHQ---EIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 354-471 6.07e-67

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: 211.69  E-value: 6.07e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 354 LKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTDGKRVIVVFHCEFSSE 433
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568963442 434 RGPRMCRYVRERDRLGN--EYPKLHYPELYVLKGGYKEFF 471
Cdd:cd01530   81 RGPRMARHLRNLDRELNsnRYPLLYYPEIYILEGGYKNFF 120
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
349-505 1.90e-36

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 140.17  E-value: 1.90e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 349 GKHQDLKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVptdgKRVIVVFHC 428
Cdd:COG5105  236 GKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT----HPRALIFHC 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 429 EFSSERGPRMCRYVRERDRLGNE--YPKLHYPELYVLKGGYKEFFLKCQSHCEPPSYRPMHHED-----------FKEDL 495
Cdd:COG5105  312 EFSSHRAPRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAEldyrclykmdkFRRNK 391

                        170
                 ....*....|
gi 568963442 496 KKFRTKSRTW 505
Cdd:COG5105  392 KFFATKNNSF 401
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 354-471 5.70e-33

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: 121.36  E-value: 5.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 354 LKYISPEIMASVLNGKFAGLIKEFVIIDCRYPyEYEGGHIKGAVNLHMEEeVEDFLLKNPIVPTDGKRVIVVFHCEFSSE 433
Cdd:cd01443    1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQS-CYQTLPQVYALFSLAGVKLAIFYCGSSQG 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568963442 434 RGPRMCRYVRERDRLGNEYpklhYPELYVLKGGYKEFF 471
Cdd:cd01443   79 RGPRAARWFADYLRKVGES----LPKSYILTGGIKAWY 112
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 375-474 8.24e-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: 8.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442   375 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTD-------GKRVIVVFHCeFSSERGPRMCRYVRERDr 447
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlglDKDKPVVVYC-RSGNRSAKAAWLLRELG- 80

                           90       100
                   ....*....|....*....|....*..
gi 568963442   448 lgneypklhYPELYVLKGGYKEFFLKC 474
Cdd:smart00450  81 ---------FKNVYLLDGGYKEWSAAG 98
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 375-470 1.79e-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: 65.78  E-value: 1.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 375 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPivptdGKRVIVVFHCEfSSERGPRMCRYVRerdrlgneypK 454
Cdd:cd00158    9 EDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLEL-----DKDKPIVVYCR-SGNRSARAAKLLR----------K 72

                         90
                 ....*....|....*.
gi 568963442 455 LHYPELYVLKGGYKEF 470
Cdd:cd00158   73 AGGTNVYNLEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 375-470 1.02e-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: 64.04  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442  375 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTD---GKRVIVVFHCEfSSERGPRMCRYVRerdRLGne 451
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLlelLKDKPIVVYCN-SGNRAAAAAALLK---ALG-- 77

                          90
                  ....*....|....*....
gi 568963442  452 ypklhYPELYVLKGGYKEF 470
Cdd:pfam00581  78 -----YKNVYVLDGGFEAW 91
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 354-478 2.11e-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: 60.89  E-value: 2.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 354 LKYISP-EIMASVLNGKfagliKEFVIIDCRyPYEYEGGHIKGAVN------LHMEEEVEDFLLKNpivptdgKRVIVVF 426
Cdd:cd01531    1 VSYISPaQLKGWIRNGR-----PPFQVVDVR-DEDYAGGHIKGSWHypstrfKAQLNQLVQLLSGS-------KKDTVVF 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568963442 427 HCEFSSERGP----RMCRYVRERDRLGNEypklhyPELYVLKGGykefFLKCQSHC 478
Cdd:cd01531   68 HCALSQVRGPsaarKFLRYLDEEDLETSK------FEVYVLHGG----FNAWESSY 113
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 353-469 1.36e-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: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 353 DLKYISPEIMASVLNGKfaglikEFVIIDCRYPYEYEGGHIKGAVNLHMeEEVEDFLLKnpiVPTDGKrviVVFHCEfSS 432
Cdd:COG0607    2 SVKEISPAELAELLESE------DAVLLDVREPEEFAAGHIPGAINIPL-GELAERLDE---LPKDKP---IVVYCA-SG 67

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568963442 433 ERGPRMCRYVRerdRLGneypklhYPELYVLKGGYKE 469
Cdd:COG0607   68 GRSAQAAALLR---RAG-------YTNVYNLAGGIEA 94
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 375-407 5.47e-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: 5.47e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 568963442 375 KEFVIIDCRYPY-----EYEGGHIKGAVNLHMEEEVED 407
Cdd:COG2897    8 PDVVILDVRWDLpdgraAYEAGHIPGAVFLDLDTDLSD 45
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 355-466 1.20e-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: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 355 KYISPEIMASVLNGKfaglikEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVE--DFLLKNPIVPTDGKrvIVVF-----H 427
Cdd:cd01518    2 TYLSPAEWNELLEDP------EVVLLDVRNDYEYDIGHFKGAVNPDVDTFREfpFWLDENLDLLKGKK--VLMYctggiR 73

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 568963442 428 CEFSSErgprmcrYVRERdrlGNEypklhypELYVLKGG 466
Cdd:cd01518   74 CEKASA-------YLKER---GFK-------NVYQLKGG 95
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 375-468 2.33e-03

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 37.25  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568963442 375 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEevedflLKNPIVPTDGKRVIVVfHCEfSSERGprmcrYVRERDRLGNEYpk 454
Cdd:cd01524   12 DGVTLIDVRTPQEFEKGHIKGAINIPLDE------LRDRLNELPKDKEIIV-YCA-VGLRG-----YIAARILTQNGF-- 76

                         90
                 ....*....|....
gi 568963442 455 lhypELYVLKGGYK 468
Cdd:cd01524   77 ----KVKNLDGGYK 86
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 375-428 3.17e-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: 3.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568963442 375 KEFVIIDCRYPYEYEG---------GHIKGAVNLHMEEEV-EDFLLKNP---------IVPTDGKRVIVvfHC 428
Cdd:COG2897  152 PDAVLVDARSPERYRGevepidpraGHIPGAVNLPWTDLLdEDGTFKSAeelralfaaLGIDPDKPVIT--YC 222
 
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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