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Conserved domains on  [gi|504697852|ref|WP_014884954|]
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MULTISPECIES: rhodanese family protein [Enterobacter]

Protein Classification

rhodanese family protein( domain architecture ID 10211066)

rhodanese family protein containing rhodanese homology and DUF2892 domains, similar to Escherichia coli inner membrane protein YgaP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 3-99 8.18e-37

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


The actual alignment was detected with superfamily member cd01527:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 99  Bit Score: 122.59  E-value: 8.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   3 LPLITPQQAKARVAEGARLIDIRDTDEYAREHISGAESVPLATL-PGGLNARAGEIVLFHCQSGARTSGNADRLAQAASP 81
Cdd:cd01527    1 LTTISPNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQLeSEGLPLVGANAIIFHCRSGMRTQQNAERLAAISAG 80

                         90
                 ....*....|....*...
gi 504697852  82 aQAFVVEGGIQGWKQAGL 99
Cdd:cd01527   81 -EAYVLEGGLDAWKAAGL 97
DUF2892 pfam11127
Protein of unknown function (DUF2892); This family is conserved in bacteria. The function is ...
 113-165 6.63e-09

Protein of unknown function (DUF2892); This family is conserved in bacteria. The function is not known.


:

Pssm-ID: 463227  Cd Length: 66  Bit Score: 49.95  E-value: 6.63e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504697852  113 RQVQIAAGLLILCGVVLGYSvsSGFFLLSGFVGAGLLFAGVTGFCGMARLLKV 165
Cdd:pfam11127  10 RLLRIIVGLVLLALALLGLL--GGWGWLLGLVGAVLLLTGLTGFCPLYALLGI 60
 
Name Accession Description Interval E-value
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 3-99 8.18e-37

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: 122.59  E-value: 8.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   3 LPLITPQQAKARVAEGARLIDIRDTDEYAREHISGAESVPLATL-PGGLNARAGEIVLFHCQSGARTSGNADRLAQAASP 81
Cdd:cd01527    1 LTTISPNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQLeSEGLPLVGANAIIFHCRSGMRTQQNAERLAAISAG 80

                         90
                 ....*....|....*...
gi 504697852  82 aQAFVVEGGIQGWKQAGL 99
Cdd:cd01527   81 -EAYVLEGGLDAWKAAGL 97
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-105 8.46e-25

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: 8.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   1 MSLPLITPQQAKARVA-EGARLIDIRDTDEYAREHISGAESVPLATLPgglnARAGEI-----VLFHCQSGARtSGNADR 74
Cdd:COG0607    1 ASVKEISPAELAELLEsEDAVLLDVREPEEFAAGHIPGAINIPLGELA----ERLDELpkdkpIVVYCASGGR-SAQAAA 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 504697852  75 LAQAASPAQAFVVEGGIQGWKQAGLLTVEDK 105
Cdd:COG0607   76 LLRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
2-99 7.33e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 73.89  E-value: 7.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   2 SLPLITPQQAKARVAEGARLIDIRDTDEYAREHISGAESVPLATL----PGGLNARAGEIVLFhCQSGARTSGNADRLaQ 77
Cdd:PRK08762   1 SIREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLelriETHLPDRDREIVLI-CASGTRSAHAAATL-R 78

                         90       100
                 ....*....|....*....|..
gi 504697852  78 AASPAQAFVVEGGIQGWKQAGL 99
Cdd:PRK08762  79 ELGYTRVASVAGGFSAWKDAGL 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 16-95 1.15e-13

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: 63.27  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   16 AEGARLIDIRDTDEYAREHISGAESVPLATLPGG-----------LNARAGEIVLFHCQSGARtSGNADRLAQAASPAQA 84
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPplpllelleklLELLKDKPIVVYCNSGNR-AAAAAALLKALGYKNV 81

                          90
                  ....*....|.
gi 504697852   85 FVVEGGIQGWK 95
Cdd:pfam00581  82 YVLDGGFEAWK 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 16-99 3.52e-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: 62.09  E-value: 3.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852    16 AEGARLIDIRDTDEYAREHISGAESVPLATL---------------PGGLNARAGEIVLFHCQSGARtSGNADRLAQAAS 80
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELldrrgeldilefeelLKRLGLDKDKPVVVYCRSGNR-SAKAAWLLRELG 80

                           90
                   ....*....|....*....
gi 504697852    81 PAQAFVVEGGIQGWKQAGL 99
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGP 99
DUF2892 pfam11127
Protein of unknown function (DUF2892); This family is conserved in bacteria. The function is ...
 113-165 6.63e-09

Protein of unknown function (DUF2892); This family is conserved in bacteria. The function is not known.


Pssm-ID: 463227  Cd Length: 66  Bit Score: 49.95  E-value: 6.63e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504697852  113 RQVQIAAGLLILCGVVLGYSvsSGFFLLSGFVGAGLLFAGVTGFCGMARLLKV 165
Cdd:pfam11127  10 RLLRIIVGLVLLALALLGLL--GGWGWLLGLVGAVLLLTGLTGFCPLYALLGI 60
 
Name Accession Description Interval E-value
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 3-99 8.18e-37

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: 122.59  E-value: 8.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   3 LPLITPQQAKARVAEGARLIDIRDTDEYAREHISGAESVPLATL-PGGLNARAGEIVLFHCQSGARTSGNADRLAQAASP 81
Cdd:cd01527    1 LTTISPNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQLeSEGLPLVGANAIIFHCRSGMRTQQNAERLAAISAG 80

                         90
                 ....*....|....*...
gi 504697852  82 aQAFVVEGGIQGWKQAGL 99
Cdd:cd01527   81 -EAYVLEGGLDAWKAAGL 97
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-105 8.46e-25

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: 8.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   1 MSLPLITPQQAKARVA-EGARLIDIRDTDEYAREHISGAESVPLATLPgglnARAGEI-----VLFHCQSGARtSGNADR 74
Cdd:COG0607    1 ASVKEISPAELAELLEsEDAVLLDVREPEEFAAGHIPGAINIPLGELA----ERLDELpkdkpIVVYCASGGR-SAQAAA 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 504697852  75 LAQAASPAQAFVVEGGIQGWKQAGLLTVEDK 105
Cdd:COG0607   76 LLRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 10-95 8.68e-17

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: 71.18  E-value: 8.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852  10 QAKARVA-EGARLIDIRDTDEYAREHISGAESVPLATLPGGLNARA---GEIVLFHCQSGARtSGNADRLAQAASPAQAF 85
Cdd:cd00158    1 ELKELLDdEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLEldkDKPIVVYCRSGNR-SARAAKLLRKAGGTNVY 79

                         90
                 ....*....|
gi 504697852  86 VVEGGIQGWK 95
Cdd:cd00158   80 NLEGGMLAWK 89
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
2-99 7.33e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 73.89  E-value: 7.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   2 SLPLITPQQAKARVAEGARLIDIRDTDEYAREHISGAESVPLATL----PGGLNARAGEIVLFhCQSGARTSGNADRLaQ 77
Cdd:PRK08762   1 SIREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLelriETHLPDRDREIVLI-CASGTRSAHAAATL-R 78

                         90       100
                 ....*....|....*....|..
gi 504697852  78 AASPAQAFVVEGGIQGWKQAGL 99
Cdd:PRK08762  79 ELGYTRVASVAGGFSAWKDAGL 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 16-95 1.15e-13

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: 63.27  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   16 AEGARLIDIRDTDEYAREHISGAESVPLATLPGG-----------LNARAGEIVLFHCQSGARtSGNADRLAQAASPAQA 84
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPplpllelleklLELLKDKPIVVYCNSGNR-AAAAAALLKALGYKNV 81

                          90
                  ....*....|.
gi 504697852   85 FVVEGGIQGWK 95
Cdd:pfam00581  82 YVLDGGFEAWK 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 16-99 3.52e-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: 62.09  E-value: 3.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852    16 AEGARLIDIRDTDEYAREHISGAESVPLATL---------------PGGLNARAGEIVLFHCQSGARtSGNADRLAQAAS 80
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELldrrgeldilefeelLKRLGLDKDKPVVVYCRSGNR-SAKAAWLLRELG 80

                           90
                   ....*....|....*....
gi 504697852    81 PAQAFVVEGGIQGWKQAGL 99
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGP 99
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 15-97 3.08e-09

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 54.88  E-value: 3.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852  15 VAEGARLIDIRDTDEYAREHISGAESVPLATLPGGLN---ARAGEIVLFHCQSGARtSGNADRLAQAASPAQAFVVEGGI 91
Cdd:PRK05597 271 LPDGVTLIDVREPSEFAAYSIPGAHNVPLSAIREGANppsVSAGDEVVVYCAAGVR-SAQAVAILERAGYTGMSSLDGGI 349


                 ....*.
gi 504697852  92 QGWKQA 97
Cdd:PRK05597 350 EGWLDS 355
DUF2892 pfam11127
Protein of unknown function (DUF2892); This family is conserved in bacteria. The function is ...
 113-165 6.63e-09

Protein of unknown function (DUF2892); This family is conserved in bacteria. The function is not known.


Pssm-ID: 463227  Cd Length: 66  Bit Score: 49.95  E-value: 6.63e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504697852  113 RQVQIAAGLLILCGVVLGYSvsSGFFLLSGFVGAGLLFAGVTGFCGMARLLKV 165
Cdd:pfam11127  10 RLLRIIVGLVLLALALLGLL--GGWGWLLGLVGAVLLLTGLTGFCPLYALLGI 60
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 6-98 1.77e-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: 49.73  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   6 ITPQQAKARVAE-GARLIDIRDTDEYARE-HISGAESVPLATL-----PGGLNA----RAGEIVLFHCQSGARtSGNADR 74
Cdd:cd01447    1 LSPEDARALLGSpGVLLVDVRDPRELERTgMIPGAFHAPRGMLefwadPDSPYHkpafAEDKPFVFYCASGWR-SALAGK 79

                         90       100
                 ....*....|....*....|....
gi 504697852  75 LAQAASPAQAFVVEGGIQGWKQAG 98
Cdd:cd01447   80 TLQDMGLKPVYNIEGGFKDWKEAG 103
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 5-94 6.62e-08

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: 48.56  E-value: 6.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   5 LITPQQAKARVAegARLIDIRDTDeYAREHISGAESVP-------LATLPGGLNARAGEIVLFHC-QSGARTSGNADRLA 76
Cdd:cd01443   12 LLENSDSNAGKD--FVVVDLRRDD-YEGGHIKGSINLPaqscyqtLPQVYALFSLAGVKLAIFYCgSSQGRGPRAARWFA 88

                         90       100
                 ....*....|....*....|...
gi 504697852  77 QA-----ASPAQAFVVEGGIQGW 94
Cdd:cd01443   89 DYlrkvgESLPKSYILTGGIKAW 111
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 6-94 1.80e-07

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 49.71  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   6 ITPQQAKARVAEGAR--LIDIRDTDEYAREHISGAESVP---------LATLPgglnarAGEIVLFHCQSGARTsgnADR 74
Cdd:PRK07878 289 ITPRELKEWLDSGKKiaLIDVREPVEWDIVHIPGAQLIPkseilsgeaLAKLP------QDRTIVLYCKTGVRS---AEA 359

                         90       100
                 ....*....|....*....|..
gi 504697852  75 LA--QAASPAQAFVVEGGIQGW 94
Cdd:PRK07878 360 LAalKKAGFSDAVHLQGGVVAW 381
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 6-97 2.01e-07

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: 47.32  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   6 ITPQQAKARVA--EGARLIDIRDTDE-YAREHISGAESVPLATLPGG---------LNARAG--EIVLFHCQSGARTSGn 71
Cdd:cd01522    1 LTPAEAWALLQadPQAVLVDVRTEAEwKFVGGVPDAVHVAWQVYPDMeinpnflaeLEEKVGkdRPVLLLCRSGNRSIA- 79

                         90       100
                 ....*....|....*....|....*.
gi 504697852  72 ADRLAQAASPAQAFVVEGGIQGWKQA 97
Cdd:cd01522   80 AAEAAAQAGFTNVYNVLEGFEGDLDA 105
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 6-95 2.78e-07

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: 46.49  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   6 ITPQQAKARVAEG--ARLIDIRDTDEYA--REHISGA---ESVPLATLpGGLNARAGEIVLFhCQSGARTSGNADRLAQA 78
Cdd:cd01444    2 ISVDELAELLAAGeaPVLLDVRDPASYAalPDHIPGAihlDEDSLDDW-LGDLDRDRPVVVY-CYHGNSSAQLAQALREA 79

                         90
                 ....*....|....*..
gi 504697852  79 ASPaQAFVVEGGIQGWK 95
Cdd:cd01444   80 GFT-DVRSLAGGFEAWR 95
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
6-99 7.81e-07

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 45.40  E-value: 7.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   6 ITPQQAKA-RVAEGARLIDIRDTDEYAREHISGAESVPLATLPGGLNARAGEI-VLFHCQSGARTSGNADRLAQaaspaQ 83
Cdd:PRK00162   7 INVEQAHQkLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTpVMVMCYHGNSSQGAAQYLLQ-----Q 81

                         90       100
                 ....*....|....*....|
gi 504697852  84 AF----VVEGGIQGWKQAGL 99
Cdd:PRK00162  82 GFdvvySIDGGFEAWRRTFP 101
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 20-79 1.36e-06

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: 44.95  E-value: 1.36e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504697852  20 RLIDIRDTDEYAREHISGAESVPLATLPGGLNARAGEI--------------VLFHCQSGARtSGNADRLAQAA 79
Cdd:cd01519   17 VLIDVREPEELKTGKIPGAINIPLSSLPDALALSEEEFekkygfpkpskdkeLIFYCKAGVR-SKAAAELARSL 89
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 16-101 2.52e-06

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: 44.27  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852  16 AEGARLIDIRDTDEYAREHISGAESVPLATLPGGLNARAGEIVLF-------HCQSGARTsgnADRLAQAASPAQafVVE 88
Cdd:cd01521   23 KPDFVLVDVRSAEAYARGHVPGAINLPHREICENATAKLDKEKLFvvycdgpGCNGATKA---ALKLAELGFPVK--EMI 97

                         90
                 ....*....|...
gi 504697852  89 GGIQGWKQAGLLT 101
Cdd:cd01521   98 GGLDWWKREGYAT 110
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 6-67 2.67e-06

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: 43.41  E-value: 2.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504697852   6 ITPQQAKARVAEGARLIDIRDTDEYAREHISGAESVPLATlpggLNARAGEI-----VLFHCQSGAR 67
Cdd:cd01524    1 VQWHELDNYRADGVTLIDVRTPQEFEKGHIKGAINIPLDE----LRDRLNELpkdkeIIVYCAVGLR 63
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
1-97 5.30e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 45.50  E-value: 5.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   1 MSLPLITPQQAKARVAEGAR---LIDIRDTDEYAREHISGAESVPLATLPGG---------LNaraGEIVLFHCQSGARt 68
Cdd:PRK07411 279 AEIPEMTVTELKALLDSGADdfvLIDVRNPNEYEIARIPGSVLVPLPDIENGpgvekvkelLN---GHRLIAHCKMGGR- 354

                         90       100
                 ....*....|....*....|....*....
gi 504697852  69 SGNADRLAQAASpAQAFVVEGGIQGWKQA 97
Cdd:PRK07411 355 SAKALGILKEAG-IEGTNVKGGITAWSRE 382
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 4-98 1.20e-05

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: 42.45  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   4 PLITPQQAKARVAEGARLI--DIRDTDEYAREHISGAESVPlatlPGGLNARAGEI-------VLFHCQSGARTSGNADR 74
Cdd:cd01533   10 PSVSADELAALQARGAPLVvlDGRRFDEYRKMTIPGSVSCP----GAELVLRVGELapdprtpIVVNCAGRTRSIIGAQS 85

                         90       100
                 ....*....|....*....|....
gi 504697852  75 LAQAASPAQAFVVEGGIQGWKQAG 98
Cdd:cd01533   86 LINAGLPNPVAALRNGTQGWTLAG 109
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 6-98 1.63e-05

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: 42.02  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   6 ITPQQAKARVAEGAR---LIDIRDTDeYAREHISGAESVPLATLPGGLNARAGEI-------VLFHC-QSGARTSGNADR 74
Cdd:cd01531    4 ISPAQLKGWIRNGRPpfqVVDVRDED-YAGGHIKGSWHYPSTRFKAQLNQLVQLLsgskkdtVVFHCaLSQVRGPSAARK 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 504697852  75 LAQAASPA-------QAFVVEGGIQGWKQAG 98
Cdd:cd01531   83 FLRYLDEEdletskfEVYVLHGGFNAWESSY 113
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 17-94 1.71e-05

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: 41.51  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852  17 EGARLIDIRDTDEYAREHISGAESVPLATLP-------GGLNARAGEIVLFHCQSGARTSGNADRLAQAASPaQAFVVEG 89
Cdd:cd01529   11 PGTALLDVRAEDEYAAGHLPGKRSIPGAALVlrsqelqALEAPGRATRYVLTCDGSLLARFAAQELLALGGK-PVALLDG 89


                 ....*
gi 504697852  90 GIQGW 94
Cdd:cd01529   90 GTSAW 94
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 7-109 1.37e-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: 40.18  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   7 TPQQAKARVAEGArLIDIRDTDEYAREHISGAESVPLATLPGGLN-ARAGEIVLFHCQSGARTSGNADRLAqAASPAQAF 85
Cdd:cd01535    1 TLAAWLGEGGQTA-VVDVTASANYVKRHIPGAWWVLRAQLAQALEkLPAAERYVLTCGSSLLARFAAADLA-ALTVKPVF 78

                         90       100
                 ....*....|....*....|....
gi 504697852  86 VVEGGIQGWKQAGLLTVEDKSQPL 109
Cdd:cd01535   79 VLEGGTAAWIAAGLPVESGETRLA 102
PLN02160 PLN02160
thiosulfate sulfurtransferase
 10-108 1.52e-04

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 39.68  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852  10 QAKARVAEGARLIDIRDTDEYAREHisgAESVPLATLPGGLNARAGEI------------------VLFHCQSGARTSGN 71
Cdd:PLN02160  21 QAKTLLQSGHQYLDVRTQDEFRRGH---CEAAKIVNIPYMLNTPQGRVknqefleqvssllnpaddILVGCQSGARSLKA 97

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 504697852  72 ADRLAqAASPAQAFVVEGGIQGWKQAGLLTVEDKSQP 108
Cdd:PLN02160  98 TTELV-AAGYKKVRNKGGGYLAWVDHSFPINQEEEEP 133
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 22-75 8.14e-04

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 37.13  E-value: 8.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504697852  22 IDIRDTDEYAREHISGAESVPLATLP---GGLNARAGEIVLFHCQSGaRTSGNADRL 75
Cdd:PRK10287  24 IDVRVPEQYQQEHVQGAINIPLKEVKeriATAVPDKNDTVKLYCNAG-RQSGQAKEI 79
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 6-94 3.80e-03

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: 35.16  E-value: 3.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   6 ITPQQAKARVAEGARL--IDIRDTDEYAREHISGAESVPLATLPGGLNARAGEI---------VLFHCQSGARTSGNADR 74
Cdd:cd01523    1 LDPEDLYARLLAGQPLfiLDVRNESDYERWKIDGENNTPYFDPYFDFLEIEEDIldqlpddqeVTVICAKEGSSQFVAEL 80

                         90       100
                 ....*....|....*....|
gi 504697852  75 LAQAAspAQAFVVEGGIQGW 94
Cdd:cd01523   81 LAERG--YDVDYLAGGMKAW 98
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 21-95 6.76e-03

Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 1st repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238790 [Multi-domain]  Cd Length: 92  Bit Score: 34.39  E-value: 6.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504697852  21 LIDIRDTDEYAREHISGAESVPLATL----PGGLNARAGEIVLFHCQSGARTSGNADRLAQAASPAQAFVVEGGIQGWK 95
Cdd:cd01532   13 LIDVREEDPFAQSHPLWAANLPLSRLeldaWVRIPRRDTPIVVYGEGGGEDLAPRAARRLSELGYTDVALLEGGLQGWR 91
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 6-95 7.40e-03

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: 34.98  E-value: 7.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852   6 ITPQQAKARVAEGAR--LIDIRDTDEYAREHISGAESVPLATL------------PGGLNARAGEIVLFhCQSGaRTSGN 71
Cdd:cd01526   10 VSVKDYKNILQAGKKhvLLDVRPKVHFEICRLPEAINIPLSELlskaaelkslqeLPLDNDKDSPIYVV-CRRG-NDSQT 87

                         90       100
                 ....*....|....*....|....*.
gi 504697852  72 ADRLAQAASPaQAFVVE--GGIQGWK 95
Cdd:cd01526   88 AVRKLKELGL-ERFVRDiiGGLKAWA 112
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 16-94 8.23e-03

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: 34.37  E-value: 8.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697852  16 AEGAR---LIDIRDTDEYAREHISGAESvplatLPGG---------LNARAGEIVLFHcQSGARTSGNADRLAQAASPaq 83
Cdd:cd01534   11 AEGDRtvyRFDVRTPEEYEAGHLPGFRH-----TPGGqlvqetdhfAPVRGARIVLAD-DDGVRADMTASWLAQMGWE-- 82

                         90
                 ....*....|.
gi 504697852  84 AFVVEGGIQGW 94
Cdd:cd01534   83 VYVLEGGLAAA 93
 
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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