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Conserved domains on  [gi|918389994|ref|WP_052442269|]
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rhodanese-like domain-containing protein [Mesobacillus selenatarsenatis]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10068911)

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

CATH:  3.40.250.10
PubMed:  12151332|17454295
SCOP:  4000452

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 231-311 9.36e-24

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: 93.52  E-value: 9.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 231 KQDGLLLVDLRAAKEYAAGHIPGAINIAYNSLAELEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGY-EAYAMKDGMR 309
Cdd:cd00158    7 DDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYNLEGGML 86


                 ..
gi 918389994 310 VW 311
Cdd:cd00158   87 AW 88
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 62-157 4.68e-21

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: 86.56  E-value: 4.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  62 ESISAEEIFEKMilnYDPSYFIVDVRDTAAFAAGHIEGSVNIPYSMTADpnQIANLPKDKKILVICYSGHTASQTSALWN 141
Cdd:COG0607    4 KEISPAELAELL---ESEDAVLLDVREPEEFAAGHIPGAINIPLGELAE--RLDELPKDKPIVVYCASGGRSAQAAALLR 78

                         90
                 ....*....|....*..
gi 918389994 142 MLGYD-AIPMVNGMGGW 157
Cdd:COG0607   79 RAGYTnVYNLAGGIEAW 95
 
Name Accession Description Interval E-value
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 231-311 9.36e-24

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: 93.52  E-value: 9.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 231 KQDGLLLVDLRAAKEYAAGHIPGAINIAYNSLAELEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGY-EAYAMKDGMR 309
Cdd:cd00158    7 DDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYNLEGGML 86


                 ..
gi 918389994 310 VW 311
Cdd:cd00158   87 AW 88
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 231-311 4.18e-23

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: 92.34  E-value: 4.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 231 KQDGLLLVDLRAAKEYAAGHIPGAINIAYNSLAelEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGYE-AYAMKDGMR 309
Cdd:COG0607   16 ESEDAVLLDVREPEEFAAGHIPGAINIPLGELA--ERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTnVYNLAGGIE 93


                 ..
gi 918389994 310 VW 311
Cdd:COG0607   94 AW 95
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 62-157 4.68e-21

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: 86.56  E-value: 4.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  62 ESISAEEIFEKMilnYDPSYFIVDVRDTAAFAAGHIEGSVNIPYSMTADpnQIANLPKDKKILVICYSGHTASQTSALWN 141
Cdd:COG0607    4 KEISPAELAELL---ESEDAVLLDVREPEEFAAGHIPGAINIPLGELAE--RLDELPKDKPIVVYCASGGRSAQAAALLR 78

                         90
                 ....*....|....*..
gi 918389994 142 MLGYD-AIPMVNGMGGW 157
Cdd:COG0607   79 RAGYTnVYNLAGGIEAW 95
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 78-157 2.63e-20

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: 84.27  E-value: 2.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  78 DPSYFIVDVRDTAAFAAGHIEGSVNIPYSMTADPNQIANLPKDKKILVICYSGHTASQT-SALWNMLGYDAIPMVNGMGG 156
Cdd:cd00158    8 DEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAaKLLRKAGGTNVYNLEGGMLA 87


                 .
gi 918389994 157 W 157
Cdd:cd00158   88 W 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 231-311 2.32e-17

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: 76.37  E-value: 2.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  231 KQDGLLLVDLRAAKEYAAGHIPGAINIAYNSL--------AELEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGY-EA 301
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLslpplpllELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYkNV 81

                          90
                  ....*....|
gi 918389994  302 YAMKDGMRVW 311
Cdd:pfam00581  82 YVLDGGFEAW 91
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 78-159 1.03e-16

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: 74.44  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994   78 DPSYFIVDVRDTAAFAAGHIEGSVNIPYSMTADPN--------QIANLPKDKKILVICYSGHTASQTSALWNMLGYDAIP 149
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpllelleKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82

                          90
                  ....*....|
gi 918389994  150 MVNgmGGWTS 159
Cdd:pfam00581  83 VLD--GGFEA 90
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 231-311 6.02e-15

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: 69.80  E-value: 6.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994   231 KQDGLLLVDLRAAKEYAAGHIPGAINIAYNSL------------AELEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLG 298
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELldrrgeldilefEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90
                   ....*....|....
gi 918389994   299 YE-AYAMKDGMRVW 311
Cdd:smart00450  81 FKnVYLLDGGYKEW 94
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 78-159 5.54e-13

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: 64.40  E-value: 5.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994    78 DPSYFIVDVRDTAAFAAGHIEGSVNIPYSMTADP------------NQIANLPKDKKILVICYSGHTASQTSALWNMLGY 145
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRrgeldilefeelLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....
gi 918389994   146 DAIPMVNgmGGWTS 159
Cdd:smart00450  82 KNVYLLD--GGYKE 93
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
233-315 2.41e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 61.18  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 233 DGLLLVDLRAAKEYAAGHIPGAINIAYNSL-AELEQlKKLSPEKKIVLIDHDGTMSSKAARILNMLGYE-AYAMKDGMRV 310
Cdd:PRK08762  16 QGAVLIDVREAHERASGQAEGALRIPRGFLeLRIET-HLPDRDREIVLICASGTRSAHAAATLRELGYTrVASVAGGFSA 94


                 ....*
gi 918389994 311 WTSNA 315
Cdd:PRK08762  95 WKDAG 99
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
83-153 1.95e-07

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 48.86  E-value: 1.95e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 918389994  83 IVDVRDTAAFAAGHIEGSVNIPYSMTADPNQIANLpkDKKILVICYSGHTaSQTSA--LWNMlGYDAIPMVNG 153
Cdd:PRK00162  23 LVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADF--DTPVMVMCYHGNS-SQGAAqyLLQQ-GFDVVYSIDG 91
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 233-311 7.32e-04

tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274463 [Multi-domain]  Cd Length: 311  Bit Score: 41.04  E-value: 7.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  233 DGLLLVDLRAAKEYAAGHIPGAINI-------------------------------AYNSLAELEQLKKLSPEKKIVLId 281
Cdd:TIGR03167   1 AFDPLIDVRSPAEFAEGHLPGAINLpllndeeraevgtlykqvgpfaaiklglalvSPNLAAHVEQWRAFADGPPQPLL- 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 918389994  282 H--DGTMSSKA-ARILNMLGYEAYAMKDGMRVW 311
Cdd:TIGR03167  80 YcwRGGMRSGSlAWLLAQIGFRVPRLEGGYKAY 112
 
Name Accession Description Interval E-value
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 231-311 9.36e-24

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: 93.52  E-value: 9.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 231 KQDGLLLVDLRAAKEYAAGHIPGAINIAYNSLAELEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGY-EAYAMKDGMR 309
Cdd:cd00158    7 DDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYNLEGGML 86


                 ..
gi 918389994 310 VW 311
Cdd:cd00158   87 AW 88
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 231-311 4.18e-23

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: 92.34  E-value: 4.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 231 KQDGLLLVDLRAAKEYAAGHIPGAINIAYNSLAelEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGYE-AYAMKDGMR 309
Cdd:COG0607   16 ESEDAVLLDVREPEEFAAGHIPGAINIPLGELA--ERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTnVYNLAGGIE 93


                 ..
gi 918389994 310 VW 311
Cdd:COG0607   94 AW 95
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 62-157 4.68e-21

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: 86.56  E-value: 4.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  62 ESISAEEIFEKMilnYDPSYFIVDVRDTAAFAAGHIEGSVNIPYSMTADpnQIANLPKDKKILVICYSGHTASQTSALWN 141
Cdd:COG0607    4 KEISPAELAELL---ESEDAVLLDVREPEEFAAGHIPGAINIPLGELAE--RLDELPKDKPIVVYCASGGRSAQAAALLR 78

                         90
                 ....*....|....*..
gi 918389994 142 MLGYD-AIPMVNGMGGW 157
Cdd:COG0607   79 RAGYTnVYNLAGGIEAW 95
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 78-157 2.63e-20

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: 84.27  E-value: 2.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  78 DPSYFIVDVRDTAAFAAGHIEGSVNIPYSMTADPNQIANLPKDKKILVICYSGHTASQT-SALWNMLGYDAIPMVNGMGG 156
Cdd:cd00158    8 DEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPIVVYCRSGNRSARAaKLLRKAGGTNVYNLEGGMLA 87


                 .
gi 918389994 157 W 157
Cdd:cd00158   88 W 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 231-311 2.32e-17

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: 76.37  E-value: 2.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  231 KQDGLLLVDLRAAKEYAAGHIPGAINIAYNSL--------AELEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGY-EA 301
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLslpplpllELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYkNV 81

                          90
                  ....*....|
gi 918389994  302 YAMKDGMRVW 311
Cdd:pfam00581  82 YVLDGGFEAW 91
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 78-159 1.03e-16

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: 74.44  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994   78 DPSYFIVDVRDTAAFAAGHIEGSVNIPYSMTADPN--------QIANLPKDKKILVICYSGHTASQTSALWNMLGYDAIP 149
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPlpllelleKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82

                          90
                  ....*....|
gi 918389994  150 MVNgmGGWTS 159
Cdd:pfam00581  83 VLD--GGFEA 90
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 231-311 6.02e-15

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: 69.80  E-value: 6.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994   231 KQDGLLLVDLRAAKEYAAGHIPGAINIAYNSL------------AELEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLG 298
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELldrrgeldilefEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90
                   ....*....|....
gi 918389994   299 YE-AYAMKDGMRVW 311
Cdd:smart00450  81 FKnVYLLDGGYKEW 94
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 78-159 5.54e-13

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: 64.40  E-value: 5.54e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994    78 DPSYFIVDVRDTAAFAAGHIEGSVNIPYSMTADP------------NQIANLPKDKKILVICYSGHTASQTSALWNMLGY 145
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRrgeldilefeelLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....
gi 918389994   146 DAIPMVNgmGGWTS 159
Cdd:smart00450  82 KNVYLLD--GGYKE 93
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 64-157 9.61e-13

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 63.43  E-value: 9.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  64 ISAEEIFEKMILNYDPsyFIVDVRDTAAFAA--GHIEGSvnIPYSMTADPNQIANLPKDKKILVICYSGHTASQTSALWN 141
Cdd:cd01444    2 ISVDELAELLAAGEAP--VLLDVRDPASYAAlpDHIPGA--IHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALR 77

                         90
                 ....*....|....*..
gi 918389994 142 MLGY-DAIPMVNGMGGW 157
Cdd:cd01444   78 EAGFtDVRSLAGGFEAW 94
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 73-165 2.74e-11

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 59.67  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  73 MILNYDPSYFIVDVRDTAAFAAGHIEGSVNIPYSmTADPNQIANLPKDKKILVICYSGHTASQTSALWNM--LGYDAIPM 150
Cdd:cd01521   18 ALKNGKPDFVLVDVRSAEAYARGHVPGAINLPHR-EICENATAKLDKEKLFVVYCDGPGCNGATKAALKLaeLGFPVKEM 96

                         90
                 ....*....|....*
gi 918389994 151 VNGMGGWTsDENLGT 165
Cdd:cd01521   97 IGGLDWWK-REGYAT 110
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 233-311 8.56e-11

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: 57.66  E-value: 8.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 233 DGLLLVDLRAAKEYAAGHIPGAINIaynSLAEL-EQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGYEAYAMKDGMRVW 311
Cdd:cd01524   12 DGVTLIDVRTPQEFEKGHIKGAINI---PLDELrDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFKVKNLDGGYKTY 88
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
233-315 2.41e-10

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 61.18  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 233 DGLLLVDLRAAKEYAAGHIPGAINIAYNSL-AELEQlKKLSPEKKIVLIDHDGTMSSKAARILNMLGYE-AYAMKDGMRV 310
Cdd:PRK08762  16 QGAVLIDVREAHERASGQAEGALRIPRGFLeLRIET-HLPDRDREIVLICASGTRSAHAAATLRELGYTrVASVAGGFSA 94


                 ....*
gi 918389994 311 WTSNA 315
Cdd:PRK08762  95 WKDAG 99
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 78-323 2.50e-10

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 60.19  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  78 DPSYFIVDVRDT-----AAFAAGHIEGSVNIPYS------------MTADPNQIANL-------PKDkkiLVICYSGHTA 133
Cdd:COG2897    7 DPDVVILDVRWDlpdgrAAYEAGHIPGAVFLDLDtdlsdprspgrhPLPSPEAFAALlgalgisNDT---TVVVYDDGGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 134 SQTSALWNML---GYDAIPMVNGmgGWTSDENLGTPLpqktfdyEVEATETKAGNYDL-PAPATKKYTDETAAILGSADd 209
Cdd:COG2897   84 LFAARAWWLLryaGHEDVRVLDG--GLAAWKAAGLPL-------ETGPPTPAPGDFTArPDPELLADADEVLAALGDPD- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 210 ylktglppimkpaaiqesiknkqdgLLLVDLRAAKEYA---------AGHIPGAINIAYNSL----------AELEQL-- 268
Cdd:COG2897  154 -------------------------AVLVDARSPERYRgevepidprAGHIPGAVNLPWTDLldedgtfksaEELRALfa 208

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 918389994 269 -KKLSPEKKIVLIDHDGTMSSKAARILNMLGYEAYAMKDG-MRVWTSNAEingiLPI 323
Cdd:COG2897  209 aLGIDPDKPVITYCGSGVRAAHTWLALELLGYPNVRLYDGsWSEWGSDPD----LPV 261
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 81-134 3.96e-10

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: 55.74  E-value: 3.96e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 918389994  81 YFIVDVRDTAAFAAGHIEGSVNIPYSMTADpnQIANLPKDKKILVICYSG---HTAS 134
Cdd:cd01524   14 VTLIDVRTPQEFEKGHIKGAINIPLDELRD--RLNELPKDKEIIVYCAVGlrgYIAA 68
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 64-157 4.91e-10

Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.


Pssm-ID: 238781 [Multi-domain]  Cd Length: 100  Bit Score: 55.96  E-value: 4.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  64 ISAEEIFEKmILNYDPsYFIVDVRDTAAFAAGHIEGSVNIPY------SMTADPNQIANLPKDKKILVICYSGHTASQTS 137
Cdd:cd01523    1 LDPEDLYAR-LLAGQP-LFILDVRNESDYERWKIDGENNTPYfdpyfdFLEIEEDILDQLPDDQEVTVICAKEGSSQFVA 78

                         90       100
                 ....*....|....*....|
gi 918389994 138 ALWNMLGYDAIPMVNGMGGW 157
Cdd:cd01523   79 ELLAERGYDVDYLAGGMKAW 98
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 72-158 2.85e-09

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: 53.81  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  72 KMILNYDPSYFIVDVRDTAAFAAGHIEGSVNIPY-----SMTADPNQIANL------PKDKKILVICYSGHTASQTSALW 140
Cdd:cd01519    7 KNLPNPHPNKVLIDVREPEELKTGKIPGAINIPLsslpdALALSEEEFEKKygfpkpSKDKELIFYCKAGVRSKAAAELA 86

                         90
                 ....*....|....*...
gi 918389994 141 NMLGYDAIpmVNGMGGWT 158
Cdd:cd01519   87 RSLGYENV--GNYPGSWL 102
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 228-312 5.51e-09

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 53.13  E-value: 5.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 228 IKNKQDGLLLVDLRAAKEYAAGHIPGAINIAYNSLAElEQLKKLSPEKKIVlIDHDG---TMSSKAARILNMLGYEAYAM 304
Cdd:cd01521   19 LKNGKPDFVLVDVRSAEAYARGHVPGAINLPHREICE-NATAKLDKEKLFV-VYCDGpgcNGATKAALKLAELGFPVKEM 96


                 ....*...
gi 918389994 305 KDGMRVWT 312
Cdd:cd01521   97 IGGLDWWK 104
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 59-160 6.23e-09

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 53.47  E-value: 6.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  59 KPAESISAEEIfeKMILNYDPSYFIVDVRDTAAFAAGHIEGSVNIPYS--MTADPNQIANLP------KDKKILVICYSG 130
Cdd:cd01526    5 SPEERVSVKDY--KNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSelLSKAAELKSLQElpldndKDSPIYVVCRRG 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 918389994 131 HTaSQTSA--LWNMLGYDAI-PMVNGMGGWTSD 160
Cdd:cd01526   83 ND-SQTAVrkLKELGLERFVrDIIGGLKAWADK 114
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 230-300 4.82e-08

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: 50.35  E-value: 4.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 230 NKQDGLLLVDLRAAKEYAAGHIPGAINIAYNSLAELEQL-----------KKLSPEKKIVLIDHDGTMSSKAARILNMLG 298
Cdd:cd01519   11 NPHPNKVLIDVREPEELKTGKIPGAINIPLSSLPDALALseeefekkygfPKPSKDKELIFYCKAGVRSKAAAELARSLG 90


                 ..
gi 918389994 299 YE 300
Cdd:cd01519   91 YE 92
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 64-158 6.84e-08

Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.


Pssm-ID: 238726 [Multi-domain]  Cd Length: 118  Bit Score: 50.32  E-value: 6.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  64 ISAEEIFEKMIlnyDPSYFIVDVRDTAAFA-----------AGHIEGSVNIPYS--MTAD-----PNQI------ANLPK 119
Cdd:cd01449    1 VTAEEVLANLD---SGDVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPWTslLDEDgtfksPEELralfaaLGITP 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 918389994 120 DKKILVICYSGHTASQTSALWNMLGYDAIPMVNgmGGWT 158
Cdd:cd01449   78 DKPVIVYCGSGVTACVLLLALELLGYKNVRLYD--GSWS 114
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 234-307 1.25e-07

Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.


Pssm-ID: 238787 [Multi-domain]  Cd Length: 96  Bit Score: 49.21  E-value: 1.25e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 918389994 234 GLLLVDLRAAKEYAAGHIPGAINIAYNSL----AELEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGYEAYAMKDG 307
Cdd:cd01529   12 GTALLDVRAEDEYAAGHLPGKRSIPGAALvlrsQELQALEAPGRATRYVLTCDGSLLARFAAQELLALGGKPVALLDG 89
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
83-153 1.95e-07

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 48.86  E-value: 1.95e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 918389994  83 IVDVRDTAAFAAGHIEGSVNIPYSMTADPNQIANLpkDKKILVICYSGHTaSQTSA--LWNMlGYDAIPMVNG 153
Cdd:PRK00162  23 LVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADF--DTPVMVMCYHGNS-SQGAAqyLLQQ-GFDVVYSIDG 91
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 221-323 5.47e-07

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 48.07  E-value: 5.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 221 PAAIQESIKNKQDGLLLvDLRAAKEYAAGHIPGAINI--------AYNSLAELEQLKKLSPEKKIVLIDHDGTMSSKAAR 292
Cdd:cd01526   12 VKDYKNILQAGKKHVLL-DVRPKVHFEICRLPEAINIplsellskAAELKSLQELPLDNDKDSPIYVVCRRGNDSQTAVR 90

                         90       100       110
                 ....*....|....*....|....*....|...
gi 918389994 293 ILNMLGYEAYA--MKDGMRVWTsnAEINGILPI 323
Cdd:cd01526   91 KLKELGLERFVrdIIGGLKAWA--DKVDPTFPL 121
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 215-314 9.19e-07

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, and similar uncharacterized putative rhodanese-related sulfurtransferases.


Pssm-ID: 238785 [Multi-domain]  Cd Length: 99  Bit Score: 46.71  E-value: 9.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 215 LPPImKPAAIQESIKnkqDGLLLVDLRAAKEYAAGHIPGAINIaynSLAELEQ--LKKLSPEKKIVLIDHDGTMSSKAAR 292
Cdd:cd01527    1 LTTI-SPNDACELLA---QGAVLVDIREPDEYLRERIPGARLV---PLSQLESegLPLVGANAIIFHCRSGMRTQQNAER 73

                         90       100
                 ....*....|....*....|..
gi 918389994 293 ILNMLGYEAYAMKDGMRVWTSN 314
Cdd:cd01527   74 LAAISAGEAYVLEGGLDAWKAA 95
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 236-311 2.39e-06

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 45.33  E-value: 2.39e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 918389994 236 LLVDLRAAKEYAA--GHIPGAINIAYNSLAELeqLKKLSPEKKIVLIDHDGTMSSKAARILNMLGY-EAYAMKDGMRVW 311
Cdd:cd01444   18 VLLDVRDPASYAAlpDHIPGAIHLDEDSLDDW--LGDLDRDRPVVVYCYHGNSSAQLAQALREAGFtDVRSLAGGFEAW 94
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 235-313 5.37e-06

Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 3rd repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238792 [Multi-domain]  Cd Length: 95  Bit Score: 44.38  E-value: 5.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 918389994 235 LLLVDLRAAKEYAAGHIPGAINIAYNSLAELEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGYEAYAMKDGMRVWTS 313
Cdd:cd01534   17 VYRFDVRTPEEYEAGHLPGFRHTPGGQLVQETDHFAPVRGARIVLADDDGVRADMTASWLAQMGWEVYVLEGGLAAALA 95
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 63-157 1.41e-05

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 46.62  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  63 SISAEEIfeKMILNYDPSYFIVDVRDTAAFAAGHIEGSVNIPYSMTADPNQIANLPKDKKILVICYSGHTASQTSALWNM 142
Cdd:PRK07878 288 TITPREL--KEWLDSGKKIALIDVREPVEWDIVHIPGAQLIPKSEILSGEALAKLPQDRTIVLYCKTGVRSAEALAALKK 365

                         90
                 ....*....|....*.
gi 918389994 143 LGY-DAIPMVNGMGGW 157
Cdd:PRK07878 366 AGFsDAVHLQGGVVAW 381
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 237-311 2.32e-05

Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 43.38  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 237 LVDLRAAKEYAAGHIPGAINIAYNS-----------LAELEQLKKL------SPEKKIVLIDHDGTMSskAAR---ILNM 296
Cdd:cd01448   25 LPDRDGRKEYLEGHIPGAVFFDLDEdlddkspgphmLPSPEEFAELlgslgiSNDDTVVVYDDGGGFF--AARawwTLRY 102

                         90
                 ....*....|....*.
gi 918389994 297 LGYEAYAMKDG-MRVW 311
Cdd:cd01448  103 FGHENVRVLDGgLQAW 118
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 221-311 3.28e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.


Pssm-ID: 238781 [Multi-domain]  Cd Length: 100  Bit Score: 42.48  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 221 PAAIQESIKNKQDgLLLVDLRAAKEYAAGHIPGAINIAYNSLAE-----LEQLKKLSPEKKIVL-IDHDGTMSSKAARIL 294
Cdd:cd01523    3 PEDLYARLLAGQP-LFILDVRNESDYERWKIDGENNTPYFDPYFdfleiEEDILDQLPDDQEVTvICAKEGSSQFVAELL 81

                         90
                 ....*....|....*..
gi 918389994 295 NMLGYEAYAMKDGMRVW 311
Cdd:cd01523   82 AERGYDVDYLAGGMKAW 98
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
231-311 3.38e-05

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 42.32  E-value: 3.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 231 KQDGLLLVDLRAAKEYAAGHIPGAINIAYNSLAELEQLKKLspEKKIVLIDHDGTMSSKAARILNMLGYEA-YAMKDGMR 309
Cdd:PRK00162  17 QEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADF--DTPVMVMCYHGNSSQGAAQYLLQQGFDVvYSIDGGFE 94


                 ..
gi 918389994 310 VW 311
Cdd:PRK00162  95 AW 96
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 232-307 3.63e-05

Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.


Pssm-ID: 238726 [Multi-domain]  Cd Length: 118  Bit Score: 42.62  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 232 QDGLLLVDLRAAKEYA-----------AGHIPGAINIAYNSL-------AELEQLKKL------SPEKKIVLIDHDGTMS 287
Cdd:cd01449   12 SGDVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPWTSLldedgtfKSPEELRALfaalgiTPDKPVIVYCGSGVTA 91

                         90       100
                 ....*....|....*....|
gi 918389994 288 SKAARILNMLGYEAYAMKDG 307
Cdd:cd01449   92 CVLLLALELLGYKNVRLYDG 111
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 83-130 8.65e-05

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: 41.24  E-value: 8.65e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 918389994  83 IVDVRDTAaFAAGHIEGSVNIP-YSMTADPNQIANLPK-DKKILVICYSG 130
Cdd:cd01443   26 VVDLRRDD-YEGGHIKGSINLPaQSCYQTLPQVYALFSlAGVKLAIFYCG 74
RHOD_Kc cd01525
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the ...
 70-140 8.81e-05

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the rhodanese-like domains found C-terminal of the serine/threonine protein kinases catalytic (S_TKc) domain and the Tre-2, BUB2p, Cdc16p (TBC) domain. The putative active site Cys residue is not present in this CD.


Pssm-ID: 238783 [Multi-domain]  Cd Length: 105  Bit Score: 41.29  E-value: 8.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 918389994  70 FEKMILNYDPSYFIVDVRDTAAFAAGHIEGSVNIPYS--MTADP-----NQIANLPKDKKILVICYSGHtaSQTSALW 140
Cdd:cd01525    6 VIRLLDNSPAKLAAVDIRSSPDFRRGHIEGSINIPFSsvFLKEGeleqlPTVPRLENYKGKIIVIVSHS--HKHAALF 81
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
83-167 9.99e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 43.85  E-value: 9.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  83 IVDVRDTAAFAAGHIEGSVNIPYS-MTADPNQiaNLP-KDKKILVICYSGHTASQTSALWNMLGYDAIPMVNgmGGWTSD 160
Cdd:PRK08762  20 LIDVREAHERASGQAEGALRIPRGfLELRIET--HLPdRDREIVLICASGTRSAHAAATLRELGYTRVASVA--GGFSAW 95


                 ....*..
gi 918389994 161 ENLGTPL 167
Cdd:PRK08762  96 KDAGLPL 102
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 218-262 1.06e-04

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 41.50  E-value: 1.06e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 918389994 218 IMKPAAIQESIKNKQDGLLLVDLRAAKEYAAGHIPGAINIAYNSL 262
Cdd:cd01446    1 TIDCAWLAALLREGGERLLLLDCRPFLEYSSSHIRGAVNVCCPTI 45
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 233-311 1.14e-04

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 43.71  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 233 DGLLLVDLRAAKEYAAGHIPGAINIAYNSLAELEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGYEA-YAMKDGMRVW 311
Cdd:PRK05597 273 DGVTLIDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGmSSLDGGIEGW 352
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 64-126 1.47e-04

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: 40.86  E-value: 1.47e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 918389994  64 ISAEEIFeKMILNYDPSYFIVDVRDTAaFAAGHIEGSVNIPYSMT-ADPNQIA-NLPKDKKILVI 126
Cdd:cd01531    4 ISPAQLK-GWIRNGRPPFQVVDVRDED-YAGGHIKGSWHYPSTRFkAQLNQLVqLLSGSKKDTVV 66
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 236-307 1.82e-04

Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.


Pssm-ID: 238780 [Multi-domain]  Cd Length: 117  Bit Score: 40.39  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 236 LLVDLRAAKE-YAAGHIPGAINIAYNS----------LAELEqlKKLSPEKKIVLIDHDGTMSSKAARILNMLGY-EAYA 303
Cdd:cd01522   17 VLVDVRTEAEwKFVGGVPDAVHVAWQVypdmeinpnfLAELE--EKVGKDRPVLLLCRSGNRSIAAAEAAAQAGFtNVYN 94


                 ....
gi 918389994 304 MKDG 307
Cdd:cd01522   95 VLEG 98
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
217-312 1.91e-04

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 42.80  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 217 PIMKPAAIQESIKNKQDGLLLVDLRAAKEYAAGHIPGAINIAYNSLAE---LEQLKKLSPEKKIVLIDHDGTMSSKAARI 293
Cdd:PRK07411 282 PEMTVTELKALLDSGADDFVLIDVRNPNEYEIARIPGSVLVPLPDIENgpgVEKVKELLNGHRLIAHCKMGGRSAKALGI 361

                         90
                 ....*....|....*....
gi 918389994 294 LNMLGYEAYAMKDGMRVWT 312
Cdd:PRK07411 362 LKEAGIEGTNVKGGITAWS 380
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 233-257 2.46e-04

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 42.51  E-value: 2.46e-04
                         10        20
                 ....*....|....*....|....*
gi 918389994 233 DGLLLVDLRAAKEYAAGHIPGAINI 257
Cdd:PRK11784  14 NDTPLIDVRSPIEFAEGHIPGAINL 38
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 219-282 2.65e-04

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: 40.09  E-value: 2.65e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 918389994 219 MKPAAIQESIKNKQDGLLLVDLRAaKEYAAGHIPGAINIAYNSL-AELEQL-KKLSPEKKIVLIDH 282
Cdd:cd01531    4 ISPAQLKGWIRNGRPPFQVVDVRD-EDYAGGHIKGSWHYPSTRFkAQLNQLvQLLSGSKKDTVVFH 68
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 221-311 3.34e-04

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: 39.30  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 221 PAAIQESIKNKQDGLLLVDLRAAKEYAAGHIPGAINIAYNSLAE-LEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGY 299
Cdd:cd01528    4 VAELAEWLADEREEPVLIDVREPEELEIAFLPGFLHLPMSEIPErSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQGF 83

                         90
                 ....*....|...
gi 918389994 300 EA-YAMKDGMRVW 311
Cdd:cd01528   84 ENvYNLQGGIDAW 96
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 61-157 4.08e-04

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 41.78  E-value: 4.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  61 AESISAEEIFEKMILNYDPSYFIVDVRDTAAFAAGHIEGSVNIPYS-MTADPNQIANLPKDkKILVICYSGHTASQTSAL 139
Cdd:PRK05597 255 ISGGFGEVLDVPRVSALPDGVTLIDVREPSEFAAYSIPGAHNVPLSaIREGANPPSVSAGD-EVVVYCAAGVRSAQAVAI 333

                         90
                 ....*....|....*....
gi 918389994 140 WNMLGY-DAIPMVNGMGGW 157
Cdd:PRK05597 334 LERAGYtGMSSLDGGIEGW 352
RHOD_Kc cd01525
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the ...
 224-282 4.22e-04

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the rhodanese-like domains found C-terminal of the serine/threonine protein kinases catalytic (S_TKc) domain and the Tre-2, BUB2p, Cdc16p (TBC) domain. The putative active site Cys residue is not present in this CD.


Pssm-ID: 238783 [Multi-domain]  Cd Length: 105  Bit Score: 39.36  E-value: 4.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 918389994 224 IQESIKNKQDGLLLVDLRAAKEYAAGHIPGAINI----AYNSLAELEQLKKLSP-----EKKIVLIDH 282
Cdd:cd01525    6 VIRLLDNSPAKLAAVDIRSSPDFRRGHIEGSINIpfssVFLKEGELEQLPTVPRlenykGKIIVIVSH 73
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 216-311 4.58e-04

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: 39.31  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 216 PPIMKpAAIQESIKNKQDGLLLVDLRAaKEYAAGHIPGAINIAYNSLAE--LEQLKKLSPEKKIVLIDHDGTMS---SKA 290
Cdd:cd01443    6 PEELV-ALLENSDSNAGKDFVVVDLRR-DDYEGGHIKGSINLPAQSCYQtlPQVYALFSLAGVKLAIFYCGSSQgrgPRA 83

                         90       100
                 ....*....|....*....|....*...
gi 918389994 291 AR----ILNMLGY---EAYAMKDGMRVW 311
Cdd:cd01443   84 ARwfadYLRKVGEslpKSYILTGGIKAW 111
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 64-156 5.98e-04

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: 38.53  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  64 ISAEEIFEKMIlNYDPSYFIVDVRDTAAFAAGHIEGSVNIPYSMTAD-PNQIANLPKDKKILVICYSGHTASQTSALWNM 142
Cdd:cd01528    2 ISVAELAEWLA-DEREEPVLIDVREPEELEIAFLPGFLHLPMSEIPErSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLR 80

                         90
                 ....*....|....
gi 918389994 143 LGYDAIpmVNGMGG 156
Cdd:cd01528   81 QGFENV--YNLQGG 92
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 75-145 6.96e-04

Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.


Pssm-ID: 238780 [Multi-domain]  Cd Length: 117  Bit Score: 38.85  E-value: 6.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  75 LNYDPSYFIVDVRdTAA--FAAGHIEGSVNIP----YSMTADPNQIANL----PKDKKILVICYSGHTASQTSALWNMLG 144
Cdd:cd01522   10 LQADPQAVLVDVR-TEAewKFVGGVPDAVHVAwqvyPDMEINPNFLAELeekvGKDRPVLLLCRSGNRSIAAAEAAAQAG 88


                 .
gi 918389994 145 Y 145
Cdd:cd01522   89 F 89
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 233-311 7.32e-04

tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274463 [Multi-domain]  Cd Length: 311  Bit Score: 41.04  E-value: 7.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994  233 DGLLLVDLRAAKEYAAGHIPGAINI-------------------------------AYNSLAELEQLKKLSPEKKIVLId 281
Cdd:TIGR03167   1 AFDPLIDVRSPAEFAEGHLPGAINLpllndeeraevgtlykqvgpfaaiklglalvSPNLAAHVEQWRAFADGPPQPLL- 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 918389994  282 H--DGTMSSKA-ARILNMLGYEAYAMKDGMRVW 311
Cdd:TIGR03167  80 YcwRGGMRSGSlAWLLAQIGFRVPRLEGGYKAY 112
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 228-311 1.69e-03

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 40.08  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 918389994 228 IKNKQDG---LLLVDLRAAKEYAAGHIPGAINIAYNSLAELEQLKKLSPEKKIVLIDHDGTMSSKAARILNMLGY-EAYA 303
Cdd:PRK07878 294 LKEWLDSgkkIALIDVREPVEWDIVHIPGAQLIPKSEILSGEALAKLPQDRTIVLYCKTGVRSAEALAALKKAGFsDAVH 373


                 ....*...
gi 918389994 304 MKDGMRVW 311
Cdd:PRK07878 374 LQGGVVAW 381
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 237-257 1.71e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.


Pssm-ID: 238778 [Multi-domain]  Cd Length: 128  Bit Score: 38.04  E-value: 1.71e-03
                         10        20
                 ....*....|....*....|.
gi 918389994 237 LVDLRAAKEYAAGHIPGAINI 257
Cdd:cd01520   16 LIDVRSPKEFFEGHLPGAINL 36
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 230-282 3.63e-03

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: 36.81  E-value: 3.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 918389994 230 NKQDGLLLVDLRAAKEYAAGHIPGAINIayNSLAELEQL-----KKLSPEKKIVLIDH 282
Cdd:cd01530   19 NFFDKYIIIDCRFPYEYNGGHIKGAVNL--STKDELEEFfldkpGVASKKKRRVLIFH 74
 
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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