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Conserved domains on  [gi|1395168549|ref|NP_001350955|]
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M-phase inducer phosphatase 3 isoform f [Homo sapiens]

Protein Classification

M-phase inducer phosphatase; rhodanese-like domain-containing protein( domain architecture ID 11885818)

M-phase inducer phosphatase is a tyrosine protein phosphatase which may function as a dosage-dependent inducer in mitotic control; rhodanese-like domain-containing protein may have sulfurtransferase activity if an active site cysteine is present

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 ...
 367-478 2.45e-56

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: 184.34  E-value: 2.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 367 VAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIvFHCEFSSERGPRMCR 446
Cdd:cd01530     9 LARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLI-FHCEFSSKRGPRMAR 87

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1395168549 447 CLREEDRSLN--QYPALYYPELYILKGGYRDFFP 478
Cdd:cd01530    88 HLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 super family cl26959
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
222-504 5.17e-38

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


The actual alignment was detected with superfamily member COG5105:

Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 144.80  E-value: 5.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 222 MCSSSANKENDN-GNLVDSEM----KYLGSPITTV-----------PKLDKNPNLGEDQAEEiSDELMEFSLKDQEAKVS 285
Cdd:COG5105   115 MTSSSANASSDNeQCPADVDQmyikKFYEIPWSSSeniefedpghdPFVDNSDNSKMNHLRG-SGKQPKCREKIAFAVWT 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 286 RS----GLYRSPSMPENLNRPRLKQVEKFKDNTipdkVKKKYFSGQGKlrkglclkkTVSLCDITITQMLEedsnqghli 361
Cdd:COG5105   194 SLqgmrGFSRAGPAPAAENSHLIDFFKSFSNGE----VFPLPTLGPGK---------SDSIQRISVETLKQ--------- 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 362 gdfskvaaLLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVpldtqKRIIIVFHCEFSSERG 441
Cdd:COG5105   252 --------VLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT-----HPRALIFHCEFSSHRA 318

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168549 442 PRMCRCLREEDRSLNQ--YPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHkteLLRC 504
Cdd:COG5105   319 PRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAEL---DYRC 380
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 367-478 2.45e-56

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: 184.34  E-value: 2.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 367 VAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIvFHCEFSSERGPRMCR 446
Cdd:cd01530     9 LARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLI-FHCEFSSKRGPRMAR 87

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1395168549 447 CLREEDRSLN--QYPALYYPELYILKGGYRDFFP 478
Cdd:cd01530    88 HLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
222-504 5.17e-38

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 144.80  E-value: 5.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 222 MCSSSANKENDN-GNLVDSEM----KYLGSPITTV-----------PKLDKNPNLGEDQAEEiSDELMEFSLKDQEAKVS 285
Cdd:COG5105   115 MTSSSANASSDNeQCPADVDQmyikKFYEIPWSSSeniefedpghdPFVDNSDNSKMNHLRG-SGKQPKCREKIAFAVWT 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 286 RS----GLYRSPSMPENLNRPRLKQVEKFKDNTipdkVKKKYFSGQGKlrkglclkkTVSLCDITITQMLEedsnqghli 361
Cdd:COG5105   194 SLqgmrGFSRAGPAPAAENSHLIDFFKSFSNGE----VFPLPTLGPGK---------SDSIQRISVETLKQ--------- 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 362 gdfskvaaLLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVpldtqKRIIIVFHCEFSSERG 441
Cdd:COG5105   252 --------VLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT-----HPRALIFHCEFSSHRA 318

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168549 442 PRMCRCLREEDRSLNQ--YPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHkteLLRC 504
Cdd:COG5105   319 PRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAEL---DYRC 380
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 380-480 4.31e-16

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: 73.65  E-value: 4.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549  380 EKFYVIDCRYPYEYLGGHIQGALN------LYSQEELFNFFLKKPIVPLDTQKRIIIVFHCeFSSERGPRMCRCLREedr 453
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNiplselLDRRGELDILEFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*..
gi 1395168549  454 slnqypaLYYPELYILKGGYRDFFPEY 480
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAG 98
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 384-476 3.96e-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: 50.95  E-value: 3.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 384 VIDCRYPYEYLGGHIQGALNLYSQEELFNF--FLKKPIVPLDTQKRIIIVFHCEfSSERGPRMCRCLReedrslnqypAL 461
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLK----------AL 76

                          90
                  ....*....|....*
gi 1395168549 462 YYPELYILKGGYRDF 476
Cdd:pfam00581  77 GYKNVYVLDGGFEAW 91
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 380-475 8.45e-08

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: 50.35  E-value: 8.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 380 EKFYVIDCRYPYEYLGGHIQGALNLYSQEelfnffLKKPIVPLDTQKRiiIVFHCEfSSERGPRMCRCLReedrslnqyp 459
Cdd:COG0607    18 EDAVLLDVREPEEFAAGHIPGAINIPLGE------LAERLDELPKDKP--IVVYCA-SGGRSAQAAALLR---------- 78

                          90
                  ....*....|....*.
gi 1395168549 460 ALYYPELYILKGGYRD 475
Cdd:COG0607    79 RAGYTNVYNLAGGIEA 94
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 288-347 9.12e-06

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: 47.44  E-value: 9.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168549 288 GLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVK-KKYFSG-------QGKLRKGLCLKKTVSLCDITI 347
Cdd:pfam06617 200 RLFRSPSMPSPVIRPALKRPERPQDEDTPVKVKrRRSVAGtqveaeeQEPESPRSLLQRSKSLCHQEI 267
 
Name Accession Description Interval E-value
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 367-478 2.45e-56

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: 184.34  E-value: 2.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 367 VAALLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVPLDTQKRIIIvFHCEFSSERGPRMCR 446
Cdd:cd01530     9 LARLLQGKYDNFFDKYIIIDCRFPYEYNGGHIKGAVNLSTKDELEEFFLDKPGVASKKKRRVLI-FHCEFSSKRGPRMAR 87

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1395168549 447 CLREEDRSLN--QYPALYYPELYILKGGYRDFFP 478
Cdd:cd01530    88 HLRNLDRELNsnRYPLLYYPEIYILEGGYKNFFE 121
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
222-504 5.17e-38

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 144.80  E-value: 5.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 222 MCSSSANKENDN-GNLVDSEM----KYLGSPITTV-----------PKLDKNPNLGEDQAEEiSDELMEFSLKDQEAKVS 285
Cdd:COG5105   115 MTSSSANASSDNeQCPADVDQmyikKFYEIPWSSSeniefedpghdPFVDNSDNSKMNHLRG-SGKQPKCREKIAFAVWT 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 286 RS----GLYRSPSMPENLNRPRLKQVEKFKDNTipdkVKKKYFSGQGKlrkglclkkTVSLCDITITQMLEedsnqghli 361
Cdd:COG5105   194 SLqgmrGFSRAGPAPAAENSHLIDFFKSFSNGE----VFPLPTLGPGK---------SDSIQRISVETLKQ--------- 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 362 gdfskvaaLLSGKFQGLIEKFYVIDCRYPYEYLGGHIQGALNLYSQEELFNFFLKKPIVpldtqKRIIIVFHCEFSSERG 441
Cdd:COG5105   252 --------VLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKKLGLLFRHKPLT-----HPRALIFHCEFSSHRA 318

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395168549 442 PRMCRCLREEDRSLNQ--YPALYYPELYILKGGYRDFFPEYMELCEPQSYCPMHHQDHkteLLRC 504
Cdd:COG5105   319 PRLAQHLRNMDRMKNPdhYPLLTYPEVYILEGGYKKFYSNYPDLCDPKGYVTMNNAEL---DYRC 380
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 369-478 9.86e-24

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: 95.94  E-value: 9.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 369 ALLSGKFQGLIEKFYVIDCRYPyEYLGGHIQGALNLYSQEelFNFFLKKPIVPLDTQKRIIIVFHCEFSSERGPRMCRCL 448
Cdd:cd01443    11 ALLENSDSNAGKDFVVVDLRRD-DYEGGHIKGSINLPAQS--CYQTLPQVYALFSLAGVKLAIFYCGSSQGRGPRAARWF 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 1395168549 449 REEDRSlnqyPALYYPELYILKGGYRDFFP 478
Cdd:cd01443    88 ADYLRK----VGESLPKSYILTGGIKAWYH 113
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 380-480 4.31e-16

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: 73.65  E-value: 4.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549  380 EKFYVIDCRYPYEYLGGHIQGALN------LYSQEELFNFFLKKPIVPLDTQKRIIIVFHCeFSSERGPRMCRCLREedr 453
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNiplselLDRRGELDILEFEELLKRLGLDKDKPVVVYC-RSGNRSAKAAWLLRE--- 78

                           90       100
                   ....*....|....*....|....*..
gi 1395168549  454 slnqypaLYYPELYILKGGYRDFFPEY 480
Cdd:smart00450  79 -------LGFKNVYLLDGGYKEWSAAG 98
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 368-473 5.63e-10

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: 56.65  E-value: 5.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 368 AALLSGKFQGLIEKFYVIDCRyPYEYLGGHIQGALNLYSQEelfnfFLKKP---IVPLDTQKRIIIVFHCEFSSERGP-- 442
Cdd:cd01531     6 PAQLKGWIRNGRPPFQVVDVR-DEDYAGGHIKGSWHYPSTR-----FKAQLnqlVQLLSGSKKDTVVFHCALSQVRGPsa 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1395168549 443 --RMCRCLREEDRSLNQypalyyPELYILKGGY 473
Cdd:cd01531    80 arKFLRYLDEEDLETSK------FEVYVLHGGF 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 380-474 2.34e-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: 54.23  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 380 EKFYVIDCRYPYEYLGGHIQGALNLysqeELFNFFLKKPIVPLDTQKRiiIVFHCEfSSERGPRMCRCLREedrslnqyp 459
Cdd:cd00158     9 EDAVLLDVREPEEYAAGHIPGAINI----PLSELEERAALLELDKDKP--IVVYCR-SGNRSARAAKLLRK--------- 72

                          90
                  ....*....|....*
gi 1395168549 460 aLYYPELYILKGGYR 474
Cdd:cd00158    73 -AGGTNVYNLEGGML 86
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 384-476 3.96e-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: 50.95  E-value: 3.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 384 VIDCRYPYEYLGGHIQGALNLYSQEELFNF--FLKKPIVPLDTQKRIIIVFHCEfSSERGPRMCRCLReedrslnqypAL 461
Cdd:pfam00581   8 LIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpLLELLEKLLELLKDKPIVVYCN-SGNRAAAAAALLK----------AL 76

                          90
                  ....*....|....*
gi 1395168549 462 YYPELYILKGGYRDF 476
Cdd:pfam00581  77 GYKNVYVLDGGFEAW 91
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 380-475 8.45e-08

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: 50.35  E-value: 8.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395168549 380 EKFYVIDCRYPYEYLGGHIQGALNLYSQEelfnffLKKPIVPLDTQKRiiIVFHCEfSSERGPRMCRCLReedrslnqyp 459
Cdd:COG0607    18 EDAVLLDVREPEEFAAGHIPGAINIPLGE------LAERLDELPKDKP--IVVYCA-SGGRSAQAAALLR---------- 78

                          90
                  ....*....|....*.
gi 1395168549 460 ALYYPELYILKGGYRD 475
Cdd:COG0607    79 RAGYTNVYNLAGGIEA 94
M-inducer_phosp pfam06617
M-phase inducer phosphatase; This family represents a region within eukaryotic M-phase inducer ...
 288-347 9.12e-06

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: 47.44  E-value: 9.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395168549 288 GLYRSPSMPENLNRPRLKQVEKFKDNTIPDKVK-KKYFSG-------QGKLRKGLCLKKTVSLCDITI 347
Cdd:pfam06617 200 RLFRSPSMPSPVIRPALKRPERPQDEDTPVKVKrRRSVAGtqveaeeQEPESPRSLLQRSKSLCHQEI 267
 
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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