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Conserved domains on  [gi|488294079|ref|WP_002365287|]
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MULTISPECIES: rhodanese-like domain-containing protein [Bacilli]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10001806)

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

CATH:  3.40.250.10
PubMed:  12151332|17454295

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 10-100 3.48e-32

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: 108.52  E-value: 3.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  10 PSISTKELQSRLSKE-ITLLDVRTPSEYRAGHIPQAINVPLNKIPA----YNKSAnEVYVICQSGMRSKNAAKILARKNY 84
Cdd:COG0607    4 KEISPAELAELLESEdAVLLDVREPEEFAAGHIPGAINIPLGELAErldeLPKDK-PIVVYCASGGRSAQAAALLRRAGY 82

                         90
                 ....*....|....*..
gi 488294079  85 -HVINVRGGMSQWSGQI 100
Cdd:COG0607   83 tNVYNLAGGIEAWKAAG 99
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 10-100 3.48e-32

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: 108.52  E-value: 3.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  10 PSISTKELQSRLSKE-ITLLDVRTPSEYRAGHIPQAINVPLNKIPA----YNKSAnEVYVICQSGMRSKNAAKILARKNY 84
Cdd:COG0607    4 KEISPAELAELLESEdAVLLDVREPEEFAAGHIPGAINIPLGELAErldeLPKDK-PIVVYCASGGRSAQAAALLRRAGY 82

                         90
                 ....*....|....*..
gi 488294079  85 -HVINVRGGMSQWSGQI 100
Cdd:COG0607   83 tNVYNLAGGIEAWKAAG 99
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 16-96 7.71e-29

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: 99.30  E-value: 7.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  16 ELQSRL-SKEITLLDVRTPSEYRAGHIPQAINVPLNKIPAYNKSAN-----EVYVICQSGMRSKNAAKILARKNY-HVIN 88
Cdd:cd00158    1 ELKELLdDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLEldkdkPIVVYCRSGNRSARAAKLLRKAGGtNVYN 80


                 ....*...
gi 488294079  89 VRGGMSQW 96
Cdd:cd00158   81 LEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 22-97 2.52e-20

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: 77.91  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079   22 SKEITLLDVRTPSEYRAGHIPQAINVPLNKIPAYNKSANE-------------VYVICQSGMRSKNAAKILARKNYH-VI 87
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLEllekllellkdkpIVVYCNSGNRAAAAAALLKALGYKnVY 82

                          90
                  ....*....|
gi 488294079   88 NVRGGMSQWS 97
Cdd:pfam00581  83 VLDGGFEAWK 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 23-97 2.71e-19

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: 75.57  E-value: 2.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079    23 KEITLLDVRTPSEYRAGHIPQAINVPLNKI------------PAYNKSAN-----EVYVICQSGMRSKNAAKILARKNY- 84
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELldrrgeldilefEELLKRLGldkdkPVVVYCRSGNRSAKAAWLLRELGFk 82

                           90
                   ....*....|...
gi 488294079    85 HVINVRGGMSQWS 97
Cdd:smart00450  83 NVYLLDGGYKEWS 95
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
10-99 1.39e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 73.12  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  10 PSISTKELQSRLSKEITLLDVRTPSEYRAGHIPQAINVPLNKIPAYNKSA-----NEVYVICQSGMRSKNAAKILARKNY 84
Cdd:PRK08762   3 REISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIETHlpdrdREIVLICASGTRSAHAAATLRELGY 82

                         90
                 ....*....|....*.
gi 488294079  85 -HVINVRGGMSQWSGQ 99
Cdd:PRK08762  83 tRVASVAGGFSAWKDA 98
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 23-92 1.59e-08

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: 50.29  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079   23 KEITLLDVRTPSEYRAGHIPQAINVPL------------------------------NKIPAYNKSA-------NEVYVI 65
Cdd:TIGR03167   1 AFDPLIDVRSPAEFAEGHLPGAINLPLlndeeraevgtlykqvgpfaaiklglalvsPNLAAHVEQWrafadgpPQPLLY 80

                          90       100
                  ....*....|....*....|....*...
gi 488294079   66 C-QSGMRSKNAAKILARKNYHVINVRGG 92
Cdd:TIGR03167  81 CwRGGMRSGSLAWLLAQIGFRVPRLEGG 108
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 10-100 3.48e-32

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: 108.52  E-value: 3.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  10 PSISTKELQSRLSKE-ITLLDVRTPSEYRAGHIPQAINVPLNKIPA----YNKSAnEVYVICQSGMRSKNAAKILARKNY 84
Cdd:COG0607    4 KEISPAELAELLESEdAVLLDVREPEEFAAGHIPGAINIPLGELAErldeLPKDK-PIVVYCASGGRSAQAAALLRRAGY 82

                         90
                 ....*....|....*..
gi 488294079  85 -HVINVRGGMSQWSGQI 100
Cdd:COG0607   83 tNVYNLAGGIEAWKAAG 99
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 16-96 7.71e-29

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: 99.30  E-value: 7.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  16 ELQSRL-SKEITLLDVRTPSEYRAGHIPQAINVPLNKIPAYNKSAN-----EVYVICQSGMRSKNAAKILARKNY-HVIN 88
Cdd:cd00158    1 ELKELLdDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLEldkdkPIVVYCRSGNRSARAAKLLRKAGGtNVYN 80


                 ....*...
gi 488294079  89 VRGGMSQW 96
Cdd:cd00158   81 LEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 22-97 2.52e-20

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: 77.91  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079   22 SKEITLLDVRTPSEYRAGHIPQAINVPLNKIPAYNKSANE-------------VYVICQSGMRSKNAAKILARKNYH-VI 87
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLEllekllellkdkpIVVYCNSGNRAAAAAALLKALGYKnVY 82

                          90
                  ....*....|
gi 488294079   88 NVRGGMSQWS 97
Cdd:pfam00581  83 VLDGGFEAWK 92
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 16-97 8.45e-20

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: 76.54  E-value: 8.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  16 ELQSRLSKEITLLDVRTPSEYRAGHIPQAINVPLNKIPA-YNK--SANEVYVICQSGMRSKNAAKILARKNYHVINVRGG 92
Cdd:cd01524    5 ELDNYRADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDrLNElpKDKEIIVYCAVGLRGYIAARILTQNGFKVKNLDGG 84


                 ....*
gi 488294079  93 MSQWS 97
Cdd:cd01524   85 YKTYS 89
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 23-97 2.71e-19

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: 75.57  E-value: 2.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079    23 KEITLLDVRTPSEYRAGHIPQAINVPLNKI------------PAYNKSAN-----EVYVICQSGMRSKNAAKILARKNY- 84
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELldrrgeldilefEELLKRLGldkdkPVVVYCRSGNRSAKAAWLLRELGFk 82

                           90
                   ....*....|...
gi 488294079    85 HVINVRGGMSQWS 97
Cdd:smart00450  83 NVYLLDGGYKEWS 95
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 12-100 4.98e-18

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: 72.43  E-value: 4.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  12 ISTKELQSRL---SKEITLLDVRTPSEYRAGHIPQAINVPLNKIPAYNKS------ANEVYVICQSGMRSKNAAKILARK 82
Cdd:cd01528    2 ISVAELAEWLadeREEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKEldsdnpDKDIVVLCHHGGRSMQVAQWLLRQ 81

                         90
                 ....*....|....*....
gi 488294079  83 NY-HVINVRGGMSQWSGQI 100
Cdd:cd01528   82 GFeNVYNLQGGIDAWSLEV 100
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
10-99 1.39e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 73.12  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  10 PSISTKELQSRLSKEITLLDVRTPSEYRAGHIPQAINVPLNKIPAYNKSA-----NEVYVICQSGMRSKNAAKILARKNY 84
Cdd:PRK08762   3 REISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIETHlpdrdREIVLICASGTRSAHAAATLRELGY 82

                         90
                 ....*....|....*.
gi 488294079  85 -HVINVRGGMSQWSGQ 99
Cdd:PRK08762  83 tRVASVAGGFSAWKDA 98
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 12-100 1.59e-16

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: 68.88  E-value: 1.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  12 ISTKELQSRL--SKEITLLDVRTPSEYRAGHIPQAINVPLNKI-------------PAYNKSANEVYVICQSGMRSKNAA 76
Cdd:cd01526   10 VSVKDYKNILqaGKKHVLLDVRPKVHFEICRLPEAINIPLSELlskaaelkslqelPLDNDKDSPIYVVCRRGNDSQTAV 89

                         90       100
                 ....*....|....*....|....*.
gi 488294079  77 KILARKNYH--VINVRGGMSQWSGQI 100
Cdd:cd01526   90 RKLKELGLErfVRDIIGGLKAWADKV 115
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 19-97 1.84e-16

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 72.60  E-value: 1.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  19 SRLSKEITLLDVRTPSEYRAGHIPQAINVPLNKI-----PAYNKSANEVYVICQSGMRSKNAAKILARKNY-HVINVRGG 92
Cdd:PRK05597 269 SALPDGVTLIDVREPSEFAAYSIPGAHNVPLSAIreganPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYtGMSSLDGG 348


                 ....*
gi 488294079  93 MSQWS 97
Cdd:PRK05597 349 IEGWL 353
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 22-97 4.44e-15

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: 64.98  E-value: 4.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  22 SKEITLLDVRTPSEYRAGHIPQAINVPLNKIP------------AYN----KSANEVYVICQSGMRSKNAAKILARKNYH 85
Cdd:cd01519   13 HPNKVLIDVREPEELKTGKIPGAINIPLSSLPdalalseeefekKYGfpkpSKDKELIFYCKAGVRSKAAAELARSLGYE 92

                         90
                 ....*....|...
gi 488294079  86 -VINVRGGMSQWS 97
Cdd:cd01519   93 nVGNYPGSWLDWA 105
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
10-100 2.98e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 63.60  E-value: 2.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  10 PSISTKELQSRL---SKEITLLDVRTPSEYRAGHIPQAINVPLNKI---PAYNK-----SANEVYVICQSGMRSKNAAKI 78
Cdd:PRK07411 282 PEMTVTELKALLdsgADDFVLIDVRNPNEYEIARIPGSVLVPLPDIengPGVEKvkellNGHRLIAHCKMGGRSAKALGI 361

                         90       100
                 ....*....|....*....|..
gi 488294079  79 LARKNYHVINVRGGMSQWSGQI 100
Cdd:PRK07411 362 LKEAGIEGTNVKGGITAWSREV 383
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 9-80 1.13e-12

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: 58.65  E-value: 1.13e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488294079   9 TPSISTKELQSRLSKEITLLDVRTPSEYRAGHIPQAINVPLNKIPAYN---KSANEVYVICQSGMRSKNAAKILA 80
Cdd:cd01527    1 LTTISPNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQLESEGlplVGANAIIFHCRSGMRTQQNAERLA 75
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 12-97 5.16e-11

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: 54.42  E-value: 5.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  12 ISTKELQSRL--SKEITLLDVRTPSEYRAGHIPQAINVPLNKIP-----------AYNKSANEVYVICQSGMRSKNAAKI 78
Cdd:cd01523    1 LDPEDLYARLlaGQPLFILDVRNESDYERWKIDGENNTPYFDPYfdfleieedilDQLPDDQEVTVICAKEGSSQFVAEL 80

                         90
                 ....*....|....*....
gi 488294079  79 LARKNYHVINVRGGMSQWS 97
Cdd:cd01523   81 LAERGYDVDYLAGGMKAWS 99
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 12-97 1.51e-10

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 55.57  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  12 ISTKELQSRL-SKEITLLDVRTPSEY---------RAGHIPQAINVP----LNKIPAYnKSANE---------------V 62
Cdd:COG2897  140 ADADEVLAALgDPDAVLVDARSPERYrgevepidpRAGHIPGAVNLPwtdlLDEDGTF-KSAEElralfaalgidpdkpV 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488294079  63 YVICQSGMRSKN---AAKILARKnyhviNVR---GGMSQWS 97
Cdd:COG2897  219 ITYCGSGVRAAHtwlALELLGYP-----NVRlydGSWSEWG 254
SelU COG2603
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ...
 9-49 2.93e-10

tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]; tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442015 [Multi-domain]  Cd Length: 341  Bit Score: 55.16  E-value: 2.93e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 488294079   9 TPSISTKELQSRLsKEITLLDVRTPSEYRAGHIPQAINVPL 49
Cdd:COG2603    2 SKRITLDDFLELL-DDDPLIDVRSPVEFAEGHIPGAINLPL 41
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 12-96 6.27e-10

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: 51.49  E-value: 6.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  12 ISTKELQ--SRLSKEITLLDVRTPSEYRA--GHIPQAINVPLNKIPAYNKSAN---EVYVICQSGMRSKNAAKILARKNY 84
Cdd:cd01444    2 ISVDELAelLAAGEAPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDLDrdrPVVVYCYHGNSSAQLAQALREAGF 81

                         90
                 ....*....|...
gi 488294079  85 H-VINVRGGMSQW 96
Cdd:cd01444   82 TdVRSLAGGFEAW 94
PLN02160 PLN02160
thiosulfate sulfurtransferase
 11-98 6.16e-09

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 49.70  E-value: 6.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  11 SISTKELQSRLSKEITLLDVRTPSEYRAGH--------IPQAINVP---------LNKIPAYNKSANEVYVICQSGMRS- 72
Cdd:PLN02160  16 SVDVSQAKTLLQSGHQYLDVRTQDEFRRGHceaakivnIPYMLNTPqgrvknqefLEQVSSLLNPADDILVGCQSGARSl 95

                         90       100
                 ....*....|....*....|....*.
gi 488294079  73 KNAAKILARKNYHVINVRGGMSQWSG 98
Cdd:PLN02160  96 KATTELVAAGYKKVRNKGGGYLAWVD 121
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 23-92 1.59e-08

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: 50.29  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079   23 KEITLLDVRTPSEYRAGHIPQAINVPL------------------------------NKIPAYNKSA-------NEVYVI 65
Cdd:TIGR03167   1 AFDPLIDVRSPAEFAEGHLPGAINLPLlndeeraevgtlykqvgpfaaiklglalvsPNLAAHVEQWrafadgpPQPLLY 80

                          90       100
                  ....*....|....*....|....*...
gi 488294079   66 C-QSGMRSKNAAKILARKNYHVINVRGG 92
Cdd:TIGR03167  81 CwRGGMRSGSLAWLLAQIGFRVPRLEGG 108
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 12-97 1.73e-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: 48.40  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  12 ISTKELQSRL-SKEITLLDVRTPSEY-----------RAGHIPQAINVP----LN-----KIPAYNKSA---------NE 61
Cdd:cd01449    1 VTAEEVLANLdSGDVQLVDARSPERFrgevpeprpglRSGHIPGAVNIPwtslLDedgtfKSPEELRALfaalgitpdKP 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488294079  62 VYVICQSGMRSknAAKILARKNYHVINVR---GGMSQWS 97
Cdd:cd01449   81 VIVYCGSGVTA--CVLLLALELLGYKNVRlydGSWSEWG 117
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 27-104 3.07e-08

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: 47.71  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  27 LLDVRTPSEYRA-GHIPQAINVPLNKIPAYNKSAN-------------EVYVICQSGMRSKNAAKILARKNY-HVINVRG 91
Cdd:cd01522   18 LVDVRTEAEWKFvGGVPDAVHVAWQVYPDMEINPNflaeleekvgkdrPVLLLCRSGNRSIAAAEAAAQAGFtNVYNVLE 97

                         90
                 ....*....|....*....
gi 488294079  92 GM------SQWSGQIKGGK 104
Cdd:cd01522   98 GFegdldaAGHRGGVNGWR 116
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 12-96 4.36e-08

Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.


Pssm-ID: 238724 [Multi-domain]  Cd Length: 103  Bit Score: 47.04  E-value: 4.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  12 ISTKELQSRL-SKEITLLDVRTPSEY-RAGHIPQAINVPLNKI--------PAYNK---SANEVYVICQSGMRSKNAAKI 78
Cdd:cd01447    1 LSPEDARALLgSPGVLLVDVRDPRELeRTGMIPGAFHAPRGMLefwadpdsPYHKPafaEDKPFVFYCASGWRSALAGKT 80

                         90
                 ....*....|....*....
gi 488294079  79 LARKNY-HVINVRGGMSQW 96
Cdd:cd01447   81 LQDMGLkPVYNIEGGFKDW 99
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 11-100 1.26e-07

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 47.78  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  11 SISTKELQSRLS--KEITLLDVRTPSEYRAGHIPQAINVPLNKIPAYNKSAN-----EVYVICQSGMRSKNAAKILARKN 83
Cdd:PRK07878 288 TITPRELKEWLDsgKKIALIDVREPVEWDIVHIPGAQLIPKSEILSGEALAKlpqdrTIVLYCKTGVRSAEALAALKKAG 367

                         90
                 ....*....|....*...
gi 488294079  84 YH-VINVRGGMSQWSGQI 100
Cdd:PRK07878 368 FSdAVHLQGGVVAWAKQV 385
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 28-95 2.40e-07

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 44.84  E-value: 2.40e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488294079  28 LDVRTPSEYRAGHIPQAINVPLNKIPAYNKSA-----NEVYVICQSGMRSKNAAKILARKNY-HVINVrGGMSQ 95
Cdd:PRK10287  24 IDVRVPEQYQQEHVQGAINIPLKEVKERIATAvpdknDTVKLYCNAGRQSGQAKEILSEMGYtHAENA-GGLKD 96
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 21-49 2.95e-07

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 46.75  E-value: 2.95e-07
                         10        20
                 ....*....|....*....|....*....
gi 488294079  21 LSKEITLLDVRTPSEYRAGHIPQAINVPL 49
Cdd:PRK11784  12 FLNDTPLIDVRSPIEFAEGHIPGAINLPL 40
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 25-96 8.47e-07

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: 43.50  E-value: 8.47e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488294079  25 ITLLDVRTPSEYRAGHIPQAINVPLNKIPAYNK---SANEVYVICQSGMRSKNAAKI---LARKNYHVINVRGGMSQW 96
Cdd:cd01521   26 FVLVDVRSAEAYARGHVPGAINLPHREICENATaklDKEKLFVVYCDGPGCNGATKAalkLAELGFPVKEMIGGLDWW 103
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
12-96 1.13e-06

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 43.47  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  12 ISTKELQSRL-SKEITLLDVRTPSEYRAGHIPQAINVPLNKIPAYNKSAN---EVYVICQSGMRSKNAAKILARKNYH-V 86
Cdd:PRK00162   7 INVEQAHQKLqEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADfdtPVMVMCYHGNSSQGAAQYLLQQGFDvV 86

                         90
                 ....*....|
gi 488294079  87 INVRGGMSQW 96
Cdd:PRK00162  87 YSIDGGFEAW 96
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 27-48 3.17e-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: 42.07  E-value: 3.17e-06
                         10        20
                 ....*....|....*....|..
gi 488294079  27 LLDVRTPSEYRAGHIPQAINVP 48
Cdd:cd01534   19 RFDVRTPEEYEAGHLPGFRHTP 40
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 9-48 4.25e-06

Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 2nd repeat which does contain the putative catalytic Cys residue.


Pssm-ID: 238791 [Multi-domain]  Cd Length: 109  Bit Score: 41.68  E-value: 4.25e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 488294079   9 TPSISTKELQSRLSK--EITLLDVRTPSEYRAGHIPQAINVP 48
Cdd:cd01533    9 TPSVSADELAALQARgaPLVVLDGRRFDEYRKMTIPGSVSCP 50
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 18-96 5.64e-06

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: 41.12  E-value: 5.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  18 QSRLSKEITLLDVRTPSEYRAGHIPQAINVP---------LNKIPAYNKSANEVYVICQSGMRSKNAAKILARKNYH-VI 87
Cdd:cd01529    6 LGEHEPGTALLDVRAEDEYAAGHLPGKRSIPgaalvlrsqELQALEAPGRATRYVLTCDGSLLARFAAQELLALGGKpVA 85


                 ....*....
gi 488294079  88 NVRGGMSQW 96
Cdd:cd01529   86 LLDGGTSAW 94
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 12-49 1.92e-05

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: 40.36  E-value: 1.92e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 488294079  12 ISTKELQSRLSKEITLLDVRTPSEYRAGHIPQAINVPL 49
Cdd:cd01520    1 ITAEDLLALRKADGPLIDVRSPKEFFEGHLPGAINLPL 38
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 17-51 7.53e-05

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 39.77  E-value: 7.53e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 488294079  17 LQSRLSKE-ITLLDVRT-----PSEYRAGHIPQAINVPLNK 51
Cdd:COG2897    1 LAAHLDDPdVVILDVRWdlpdgRAAYEAGHIPGAVFLDLDT 41
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 11-52 7.57e-05

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: 38.80  E-value: 7.57e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488294079  11 SISTKELQSRLSKE---ITLLDVRTPSEYRAGHIPQAINVPLNKI 52
Cdd:cd01446    1 TIDCAWLAALLREGgerLLLLDCRPFLEYSSSHIRGAVNVCCPTI 45
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 23-96 9.05e-04

Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 4th repeat which, in general, contains the putative catalytic Cys residue.


Pssm-ID: 238793 [Multi-domain]  Cd Length: 145  Bit Score: 36.33  E-value: 9.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  23 KEITLLDVRTPSEYRAGHIPQAINV-------PLNKIPAynksANEVYVICQSGMRSKNAAKILARKNYHVINV-RGGMS 94
Cdd:cd01535   10 GQTAVVDVTASANYVKRHIPGAWWVlraqlaqALEKLPA----AERYVLTCGSSLLARFAAADLAALTVKPVFVlEGGTA 85


                 ..
gi 488294079  95 QW 96
Cdd:cd01535   86 AW 87
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 23-48 1.29e-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: 35.27  E-value: 1.29e-03
                         10        20
                 ....*....|....*....|....*.
gi 488294079  23 KEITLLDVRTPSEYRAGHIPQAINVP 48
Cdd:cd01530   22 DKYIIIDCRFPYEYNGGHIKGAVNLS 47
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 11-93 1.99e-03

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 36.01  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488294079  11 SISTKELQSRLSKEITLLDVRTPSEYRAGHIPQA---INVPLNKI--------PAYNKSANEVYVICQSGMRSKNAAKIL 79
Cdd:PRK05600 273 TDTTSLIDATLNGSATLLDVREPHEVLLKDLPEGgasLKLPLSAItddadilhALSPIDGDNVVVYCASGIRSADFIEKY 352

                         90
                 ....*....|....*.
gi 488294079  80 ARKNYH--VINVRGGM 93
Cdd:PRK05600 353 SHLGHEltLHNLPGGV 368
RHOD_Kc cd01525
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the ...
 12-48 6.42e-03

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: 33.20  E-value: 6.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 488294079  12 ISTKELQSRLSK---EITLLDVRTPSEYRAGHIPQAINVP 48
Cdd:cd01525    1 ISVYDVIRLLDNspaKLAAVDIRSSPDFRRGHIEGSINIP 40
 
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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