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Conserved domains on  [gi|2282760990|ref|NP_001397316|]
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M-phase inducer phosphatase 1 isoform 4 [Mus musculus]

Protein Classification

rhodanese-like domain-containing protein; rhodanese domain-containing protein( domain architecture ID 10535133)

rhodanese-like domain-containing protein may have sulfurtransferase activity if an active site cysteine is present| rhodanese domain-containing protein may function as a sulfurtransferase

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 ...
 85-318 1.10e-84

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: 260.84  E-value: 1.10e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990  85 LDSPGPLDSKE----------------NLEISLTRINSLPQKLLGCSPALKRShsDSLDHDTFH---LIDQDENKEN--E 143
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPQRLLGSSPALKRS--QSLDSDIYQpeqLSSQGENKENvpE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 144 AFEFKKPIRPASRH-----IYEESKDPFTHRQNSAPARMLSSNESE----SGNFSPLFIPQSPVKATL-SDEDDGFIDLL 213
Cdd:pfam06617  79 GFEFKKPTKPASRSrlrsfNSGTAKDAFAQRPNSAPALMLSSPPPKmqelEGDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 214 DGeNMKNDEETPSCMASLWTAPLVM----RRPANLADRC---GLFDSPSPCGSSTRAVLKRADRSHEEPPRG-TKRRKSV 285
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigERPTSLVIRCrprRLFRSPSMPSPVIRPALKRPERPQDEDTPVkVKRRRSV 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2282760990 286 PSP-VKAKADVPE-PAQLPSQSLSLMSSpkgTIEN 318
Cdd:pfam06617 238 AGTqVEAEEQEPEsPRSLLQRSKSLCHQ---EIEN 269
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 347-431 1.07e-44

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.


The actual alignment was detected with superfamily member cd01530:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 121  Bit Score: 151.99  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 347 LKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTDGKRVIVVFHCEFSSE 426
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80


                  ....*
gi 2282760990 427 RGPRI 431
Cdd:cd01530    81 RGPRM 85
 
Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 85-318 1.10e-84

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: 260.84  E-value: 1.10e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990  85 LDSPGPLDSKE----------------NLEISLTRINSLPQKLLGCSPALKRShsDSLDHDTFH---LIDQDENKEN--E 143
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPQRLLGSSPALKRS--QSLDSDIYQpeqLSSQGENKENvpE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 144 AFEFKKPIRPASRH-----IYEESKDPFTHRQNSAPARMLSSNESE----SGNFSPLFIPQSPVKATL-SDEDDGFIDLL 213
Cdd:pfam06617  79 GFEFKKPTKPASRSrlrsfNSGTAKDAFAQRPNSAPALMLSSPPPKmqelEGDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 214 DGeNMKNDEETPSCMASLWTAPLVM----RRPANLADRC---GLFDSPSPCGSSTRAVLKRADRSHEEPPRG-TKRRKSV 285
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigERPTSLVIRCrprRLFRSPSMPSPVIRPALKRPERPQDEDTPVkVKRRRSV 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2282760990 286 PSP-VKAKADVPE-PAQLPSQSLSLMSSpkgTIEN 318
Cdd:pfam06617 238 AGTqVEAEEQEPEsPRSLLQRSKSLCHQ---EIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 347-431 1.07e-44

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: 151.99  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 347 LKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTDGKRVIVVFHCEFSSE 426
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80


                  ....*
gi 2282760990 427 RGPRI 431
Cdd:cd01530    81 RGPRM 85
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
342-431 8.13e-19

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 88.17  E-value: 8.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 342 GKHQDLKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVptdgKRVIVVFHC 421
Cdd:COG5105   236 GKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT----HPRALIFHC 311

                          90
                  ....*....|
gi 2282760990 422 EFSSERGPRI 431
Cdd:COG5105   312 EFSSHRAPRL 321
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 368-430 1.16e-14

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: 69.41  E-value: 1.16e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990  368 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTD-------GKRVIVVFHCeFSSERGPR 430
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlglDKDKPVVVYC-RSGNRSAK 71
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 368-425 1.50e-08

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: 51.72  E-value: 1.50e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282760990 368 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTD---GKRVIVVFHCEFSS 425
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLlelLKDKPIVVYCNSGN 64
 
Name Accession Description Interval E-value
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 85-318 1.10e-84

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: 260.84  E-value: 1.10e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990  85 LDSPGPLDSKE----------------NLEISLTRINSLPQKLLGCSPALKRShsDSLDHDTFH---LIDQDENKEN--E 143
Cdd:pfam06617   1 LDSPSPLDPNEaeetfekaiqassrvvNLKMPIRRINSLPQRLLGSSPALKRS--QSLDSDIYQpeqLSSQGENKENvpE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 144 AFEFKKPIRPASRH-----IYEESKDPFTHRQNSAPARMLSSNESE----SGNFSPLFIPQSPVKATL-SDEDDGFIDLL 213
Cdd:pfam06617  79 GFEFKKPTKPASRSrlrsfNSGTAKDAFAQRPNSAPALMLSSPPPKmqelEGDSSPVFLRRSSLTSSLnDEEDDGFLEIL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 214 DGeNMKNDEETPSCMASLWTAPLVM----RRPANLADRC---GLFDSPSPCGSSTRAVLKRADRSHEEPPRG-TKRRKSV 285
Cdd:pfam06617 159 DG-DLENDEEVPSGMASLLTAPLVTdeigERPTSLVIRCrprRLFRSPSMPSPVIRPALKRPERPQDEDTPVkVKRRRSV 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2282760990 286 PSP-VKAKADVPE-PAQLPSQSLSLMSSpkgTIEN 318
Cdd:pfam06617 238 AGTqVEAEEQEPEsPRSLLQRSKSLCHQ---EIEN 269
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 347-431 1.07e-44

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: 151.99  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 347 LKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTDGKRVIVVFHCEFSSE 426
Cdd:cd01530     1 LKRISPETLARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLIFHCEFSSK 80


                  ....*
gi 2282760990 427 RGPRI 431
Cdd:cd01530    81 RGPRM 85
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 347-430 8.44e-23

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: 92.85  E-value: 8.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 347 LKYISPEIMASVLNGKFAGLIKEFVIIDCRYPyEYEGGHIKGAVNLHMeEEVEDFLLKNPIVPTDGKRVIVVFHCEFSSE 426
Cdd:cd01443     1 LKYISPEELVALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPA-QSCYQTLPQVYALFSLAGVKLAIFYCGSSQG 78


                  ....
gi 2282760990 427 RGPR 430
Cdd:cd01443    79 RGPR 82
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
342-431 8.13e-19

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 88.17  E-value: 8.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 342 GKHQDLKYISPEIMASVLNGKFAGLIKEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVptdgKRVIVVFHC 421
Cdd:COG5105   236 GKSDSIQRISVETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT----HPRALIFHC 311

                          90
                  ....*....|
gi 2282760990 422 EFSSERGPRI 431
Cdd:COG5105   312 EFSSHRAPRL 321
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 368-430 1.16e-14

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: 69.41  E-value: 1.16e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990  368 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTD-------GKRVIVVFHCeFSSERGPR 430
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEEllkrlglDKDKPVVVYC-RSGNRSAK 71
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 368-422 2.65e-09

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: 53.84  E-value: 2.65e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2282760990 368 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPivptdGKRVIVVFHCE 422
Cdd:cd00158     9 EDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLEL-----DKDKPIVVYCR 58
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 368-425 1.50e-08

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: 51.72  E-value: 1.50e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2282760990 368 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEEVEDFLLKNPIVPTD---GKRVIVVFHCEFSS 425
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLlelLKDKPIVVYCNSGN 64
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 347-429 5.72e-07

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: 48.18  E-value: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282760990 347 LKYISP-EIMASVLNGKfagliKEFVIIDCRyPYEYEGGHIKGAVN------LHMEEEVEDFLLKNpivptdgKRVIVVF 419
Cdd:cd01531     1 VSYISPaQLKGWIRNGR-----PPFQVVDVR-DEDYAGGHIKGSWHypstrfKAQLNQLVQLLSGS-------KKDTVVF 67

                          90
                  ....*....|
gi 2282760990 420 HCEFSSERGP 429
Cdd:cd01531    68 HCALSQVRGP 77
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 346-421 8.74e-07

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: 47.27  E-value: 8.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2282760990 346 DLKYISPEIMASVLNGKfaglikEFVIIDCRYPYEYEGGHIKGAVNLHMeEEVEDFLLKnpiVPTDGKrviVVFHC 421
Cdd:COG0607     2 SVKEISPAELAELLESE------DAVLLDVREPEEFAAGHIPGAINIPL-GELAERLDE---LPKDKP---IVVYC 64
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 368-400 4.48e-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: 4.48e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2282760990 368 KEFVIIDCRYPY-----EYEGGHIKGAVNLHMEEEVED 400
Cdd:COG2897     8 PDVVILDVRWDLpdgraAYEAGHIPGAVFLDLDTDLSD 45
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 348-395 1.13e-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: 1.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2282760990 348 KYISPEIMASVLNGKfaglikEFVIIDCRYPYEYEGGHIKGAVNLHME 395
Cdd:cd01518     2 TYLSPAEWNELLEDP------EVVLLDVRNDYEYDIGHFKGAVNPDVD 43
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 368-421 2.60e-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: 2.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2282760990 368 KEFVIIDCRYPYEYEG---------GHIKGAVNLHMEEEV-EDFLLKNP---------IVPTDGKRVIVvfHC 421
Cdd:COG2897   152 PDAVLVDARSPERYRGevepidpraGHIPGAVNLPWTDLLdEDGTFKSAeelralfaaLGIDPDKPVIT--YC 222
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 368-433 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        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2282760990 368 KEFVIIDCRYPYEYEGGHIKGAVNLHMEEevedflLKNPIVPTDGKRVIVVfHCEfSSERG---PRILT 433
Cdd:cd01524    12 DGVTLIDVRTPQEFEKGHIKGAINIPLDE------LRDRLNELPKDKEIIV-YCA-VGLRGyiaARILT 72
 
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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