NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488223443|ref|WP_002294651|]
View 

MULTISPECIES: rhodanese-like domain-containing protein [Enterococcus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
7-96 5.36e-36

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: 118.15  E-value: 5.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   7 SIKSITVPELKEKL-LENPALLDVRTPAEYRGGHIKGAKNVPLQSI-NRYDG-DKEKTVYVICQSGMRSKQAAKELKKSG 83
Cdd:COG0607    2 SVKEISPAELAELLeSEDAVLLDVREPEEFAAGHIPGAINIPLGELaERLDElPKDKPIVVYCASGGRSAQAAALLRRAG 81
                         90
                 ....*....|....
gi 488223443  84 YD-VVNVRGGMNQW 96
Cdd:COG0607   82 YTnVYNLAGGIEAW 95
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
7-96 5.36e-36

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: 118.15  E-value: 5.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   7 SIKSITVPELKEKL-LENPALLDVRTPAEYRGGHIKGAKNVPLQSI-NRYDG-DKEKTVYVICQSGMRSKQAAKELKKSG 83
Cdd:COG0607    2 SVKEISPAELAELLeSEDAVLLDVREPEEFAAGHIPGAINIPLGELaERLDElPKDKPIVVYCASGGRSAQAAALLRRAG 81
                         90
                 ....*....|....
gi 488223443  84 YD-VVNVRGGMNQW 96
Cdd:COG0607   82 YTnVYNLAGGIEAW 95
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
15-96 1.55e-31

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: 106.23  E-value: 1.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  15 ELKEKLLENPA-LLDVRTPAEYRGGHIKGAKNVPLQSINRYDG----DKEKTVYVICQSGMRSKQAAKELKKSGY-DVVN 88
Cdd:cd00158    1 ELKELLDDEDAvLLDVREPEEYAAGHIPGAINIPLSELEERAAllelDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYN 80

                 ....*...
gi 488223443  89 VRGGMNQW 96
Cdd:cd00158   81 LEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
22-96 3.23e-23

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: 85.23  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   22 ENPALLDVRTPAEYRGGHIKGAKNVPLQSINRYDGD------------KEKTVYVICQSGMRSKQAAKELKKSGY-DVVN 88
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPllellekllellKDKPIVVYCNSGNRAAAAAALLKALGYkNVYV 83

                  ....*...
gi 488223443   89 VRGGMNQW 96
Cdd:pfam00581  84 LDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
22-98 8.86e-22

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: 81.74  E-value: 8.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443    22 ENPALLDVRTPAEYRGGHIKGAKNVPLQSINRYDG----------------DKEKTVYVICQSGMRSKQAAKELKKSGY- 84
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldilefeellkrlglDKDKPVVVYCRSGNRSAKAAWLLRELGFk 82
                           90
                   ....*....|....
gi 488223443    85 DVVNVRGGMNQWFD 98
Cdd:smart00450  83 NVYLLDGGYKEWSA 96
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
7-99 4.21e-21

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 85.45  E-value: 4.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   7 SIKSITVPELKEKLLENPALLDVRTPAEYRGGHIKGAKNVP---LQS-INRYDGDKEKTVYVICQSGMRSKQAAKELKKS 82
Cdd:PRK08762   1 SIREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPrgfLELrIETHLPDRDREIVLICASGTRSAHAAATLREL 80
                         90
                 ....*....|....*...
gi 488223443  83 GY-DVVNVRGGMNQWFDR 99
Cdd:PRK08762  81 GYtRVASVAGGFSAWKDA 98
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
7-96 5.36e-36

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: 118.15  E-value: 5.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   7 SIKSITVPELKEKL-LENPALLDVRTPAEYRGGHIKGAKNVPLQSI-NRYDG-DKEKTVYVICQSGMRSKQAAKELKKSG 83
Cdd:COG0607    2 SVKEISPAELAELLeSEDAVLLDVREPEEFAAGHIPGAINIPLGELaERLDElPKDKPIVVYCASGGRSAQAAALLRRAG 81
                         90
                 ....*....|....
gi 488223443  84 YD-VVNVRGGMNQW 96
Cdd:COG0607   82 YTnVYNLAGGIEAW 95
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
15-96 1.55e-31

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: 106.23  E-value: 1.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  15 ELKEKLLENPA-LLDVRTPAEYRGGHIKGAKNVPLQSINRYDG----DKEKTVYVICQSGMRSKQAAKELKKSGY-DVVN 88
Cdd:cd00158    1 ELKELLDDEDAvLLDVREPEEYAAGHIPGAINIPLSELEERAAllelDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVYN 80

                 ....*...
gi 488223443  89 VRGGMNQW 96
Cdd:cd00158   81 LEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
22-96 3.23e-23

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: 85.23  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   22 ENPALLDVRTPAEYRGGHIKGAKNVPLQSINRYDGD------------KEKTVYVICQSGMRSKQAAKELKKSGY-DVVN 88
Cdd:pfam00581   4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPllellekllellKDKPIVVYCNSGNRAAAAAALLKALGYkNVYV 83

                  ....*...
gi 488223443   89 VRGGMNQW 96
Cdd:pfam00581  84 LDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
22-98 8.86e-22

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: 81.74  E-value: 8.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443    22 ENPALLDVRTPAEYRGGHIKGAKNVPLQSINRYDG----------------DKEKTVYVICQSGMRSKQAAKELKKSGY- 84
Cdd:smart00450   3 EKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGeldilefeellkrlglDKDKPVVVYCRSGNRSAKAAWLLRELGFk 82
                           90
                   ....*....|....
gi 488223443    85 DVVNVRGGMNQWFD 98
Cdd:smart00450  83 NVYLLDGGYKEWSA 96
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
7-99 4.21e-21

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 85.45  E-value: 4.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   7 SIKSITVPELKEKLLENPALLDVRTPAEYRGGHIKGAKNVP---LQS-INRYDGDKEKTVYVICQSGMRSKQAAKELKKS 82
Cdd:PRK08762   1 SIREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPrgfLELrIETHLPDRDREIVLICASGTRSAHAAATLREL 80
                         90
                 ....*....|....*...
gi 488223443  83 GY-DVVNVRGGMNQWFDR 99
Cdd:PRK08762  81 GYtRVASVAGGFSAWKDA 98
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
15-92 1.07e-19

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: 76.15  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  15 ELKEKLLENPALLDVRTPAEYRGGHIKGAKNVPLQSI-NRYDG-DKEKTVYVICQSGMRSKQAAKELKKSGYDVVNVRGG 92
Cdd:cd01524    5 ELDNYRADGVTLIDVRTPQEFEKGHIKGAINIPLDELrDRLNElPKDKEIIVYCAVGLRGYIAARILTQNGFKVKNLDGG 84
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
11-96 8.60e-17

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: 69.35  E-value: 8.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  11 ITVPELKEKL---LENPALLDVRTPAEYRGGHIKGAKNVPLQSINRY-----DGDKEKTVYVICQSGMRSKQAAKELKKS 82
Cdd:cd01528    2 ISVAELAEWLadeREEPVLIDVREPEELEIAFLPGFLHLPMSEIPERskeldSDNPDKDIVVLCHHGGRSMQVAQWLLRQ 81
                         90
                 ....*....|....*
gi 488223443  83 GYD-VVNVRGGMNQW 96
Cdd:cd01528   82 GFEnVYNLQGGIDAW 96
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
1-96 4.34e-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: 68.10  E-value: 4.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   1 MNLLfQSIKSITVPELKEKL--LENPALLDVRTPAEYRGGHIKGAKNVPLQSINR------------YDGDKEKTVYVIC 66
Cdd:cd01526    1 LKLL-SPEERVSVKDYKNILqaGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSkaaelkslqelpLDNDKDSPIYVVC 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488223443  67 QSGMRSKQAAKELKKSGY--DVVNVRGGMNQW 96
Cdd:cd01526   80 RRGNDSQTAVRKLKELGLerFVRDIIGGLKAW 111
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
13-98 1.02e-14

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 67.98  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  13 VPELKEkLLENPALLDVRTPAEYRGGHIKGAKNVPLQSI----NRYDGDKEKTVYVICQSGMRSKQAAKELKKSGY-DVV 87
Cdd:PRK05597 265 VPRVSA-LPDGVTLIDVREPSEFAAYSIPGAHNVPLSAIregaNPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYtGMS 343
                         90
                 ....*....|.
gi 488223443  88 NVRGGMNQWFD 98
Cdd:PRK05597 344 SLDGGIEGWLD 354
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
12-96 1.45e-14

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: 63.44  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  12 TVPELKEKLLENPA--LLDVRTPAEYRGGHIKGAKNVPLQSI------------NRYDGDK---EKTVYVICQSGMRSKQ 74
Cdd:cd01519    2 SFEEVKNLPNPHPNkvLIDVREPEELKTGKIPGAINIPLSSLpdalalseeefeKKYGFPKpskDKELIFYCKAGVRSKA 81
                         90       100
                 ....*....|....*....|...
gi 488223443  75 AAKELKKSGY-DVVNVRGGMNQW 96
Cdd:cd01519   82 AAELARSLGYeNVGNYPGSWLDW 104
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
10-96 1.90e-14

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 67.04  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  10 SITVPELKEKL--LENPALLDVRTPAEYRGGHIKGAKNVPLQSINRYDG----DKEKTVYVICQSGMRSKQAAKELKKSG 83
Cdd:PRK07878 288 TITPRELKEWLdsGKKIALIDVREPVEWDIVHIPGAQLIPKSEILSGEAlaklPQDRTIVLYCKTGVRSAEALAALKKAG 367
                         90
                 ....*....|....
gi 488223443  84 Y-DVVNVRGGMNQW 96
Cdd:PRK07878 368 FsDAVHLQGGVVAW 381
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
11-96 5.74e-14

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: 61.89  E-value: 5.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  11 ITVPELKE--KLLENPALLDVRTPAEYRG--GHIKGAKNVPLQSINRYDG--DKEKTVYVICQSGMRSKQAAKELKKSGY 84
Cdd:cd01444    2 ISVDELAEllAAGEAPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGdlDRDRPVVVYCYHGNSSAQLAQALREAGF 81
                         90
                 ....*....|...
gi 488223443  85 -DVVNVRGGMNQW 96
Cdd:cd01444   82 tDVRSLAGGFEAW 94
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
6-96 4.20e-13

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 63.22  E-value: 4.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   6 QSIKSITVPELKEkLLENPA----LLDVRTPAEYRGGHIKGAKNVPLQSINRYDG-DKEKT------VYVICQSGMRSKQ 74
Cdd:PRK07411 279 AEIPEMTVTELKA-LLDSGAddfvLIDVRNPNEYEIARIPGSVLVPLPDIENGPGvEKVKEllnghrLIAHCKMGGRSAK 357
                         90       100
                 ....*....|....*....|..
gi 488223443  75 AAKELKKSGYDVVNVRGGMNQW 96
Cdd:PRK07411 358 ALGILKEAGIEGTNVKGGITAW 379
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
14-96 1.27e-11

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: 55.90  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  14 PELKEKLLENPA--LLDVRTPAEY-RGGHIKGAKNVPLQSIN-RYDGD---------KEKTVYVICQSGMRSKQAAKELK 80
Cdd:cd01447    3 PEDARALLGSPGvlLVDVRDPRELeRTGMIPGAFHAPRGMLEfWADPDspyhkpafaEDKPFVFYCASGWRSALAGKTLQ 82
                         90
                 ....*....|....*..
gi 488223443  81 KSGYD-VVNVRGGMNQW 96
Cdd:cd01447   83 DMGLKpVYNIEGGFKDW 99
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
11-96 1.42e-11

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 58.65  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  11 ITVPELKEKL-LENPALLDVRTPAEYRG---------GHIKGAKNVP----------------LQSI-NRYDGDKEKTVY 63
Cdd:COG2897  140 ADADEVLAALgDPDAVLVDARSPERYRGevepidpraGHIPGAVNLPwtdlldedgtfksaeeLRALfAALGIDPDKPVI 219
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488223443  64 VICQSGMRSKQ---AAKELkksGYDvvNVR---GGMNQW 96
Cdd:COG2897  220 TYCGSGVRAAHtwlALELL---GYP--NVRlydGSWSEW 253
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
27-95 1.87e-11

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 55.62  E-value: 1.87e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488223443  27 LDVRTPAEYRGGHIKGAKNVPLQSINRYDG----DKEKTVYVICQSGMRSKQAAKELKKSGYDVVNVRGGMNQ 95
Cdd:PRK10287  24 IDVRVPEQYQQEHVQGAINIPLKEVKERIAtavpDKNDTVKLYCNAGRQSGQAKEILSEMGYTHAENAGGLKD 96
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
11-92 6.78e-11

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: 54.64  E-value: 6.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  11 ITVPELKEKLLENPA--LLDVRTPAEYRG-GHIKGAKNVPLQS-----IN-------RYDGDKEKTVYVICQSGMRSKQA 75
Cdd:cd01522    1 LTPAEAWALLQADPQavLVDVRTEAEWKFvGGVPDAVHVAWQVypdmeINpnflaelEEKVGKDRPVLLLCRSGNRSIAA 80
                         90
                 ....*....|....*...
gi 488223443  76 AKELKKSGY-DVVNVRGG 92
Cdd:cd01522   81 AEAAAQAGFtNVYNVLEG 98
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
8-96 1.12e-10

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: 53.64  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   8 IKSITVPELKEKLLENPALLDVRTPAEYRGGHIKGAKNVPLQSINRYDGDKEKTVYVI--CQSGMRSKQAAKELKK-SGY 84
Cdd:cd01527    1 LTTISPNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIfhCRSGMRTQQNAERLAAiSAG 80
                         90
                 ....*....|..
gi 488223443  85 DVVNVRGGMNQW 96
Cdd:cd01527   81 EAYVLEGGLDAW 92
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
9-96 4.26e-10

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 52.33  E-value: 4.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   9 KSITVPELKEKLLENPA-LLDVRTPAEYRGGHIKGAKNVPLQSINRY--DGDKEKTVYVICQSGMRSKQAAKELKKSGYD 85
Cdd:PRK00162   5 ECINVEQAHQKLQEGGAvLVDIRDPQSFAMGHAPGAFHLTNDSLGAFmrQADFDTPVMVMCYHGNSSQGAAQYLLQQGFD 84
                         90
                 ....*....|..
gi 488223443  86 VV-NVRGGMNQW 96
Cdd:PRK00162  85 VVySIDGGFEAW 96
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
11-96 5.09e-10

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: 52.25  E-value: 5.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  11 ITVPELKEkLLENP--ALLDVRTPAEYRG-----------GHIKGAKNVPLQSINRYDG-----------------DKEK 60
Cdd:cd01449    1 VTAEEVLA-NLDSGdvQLVDARSPERFRGevpeprpglrsGHIPGAVNIPWTSLLDEDGtfkspeelralfaalgiTPDK 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488223443  61 TVYVICQSGMRSKQ---AAKELkkSGYDVVNVRGGMNQW 96
Cdd:cd01449   80 PVIVYCGSGVTACVlllALELL--GYKNVRLYDGSWSEW 116
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
11-98 6.15e-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: 51.73  E-value: 6.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  11 ITVPELKEKLL--ENPALLDVRTPAEYRGGHIKGAKNVPLQSI--NRYDGD--------KEKTVYVICQSGMRSKQAAKE 78
Cdd:cd01523    1 LDPEDLYARLLagQPLFILDVRNESDYERWKIDGENNTPYFDPyfDFLEIEedildqlpDDQEVTVICAKEGSSQFVAEL 80
                         90       100
                 ....*....|....*....|
gi 488223443  79 LKKSGYDVVNVRGGMNQWFD 98
Cdd:cd01523   81 LAERGYDVDYLAGGMKAWSE 100
PLN02160 PLN02160
thiosulfate sulfurtransferase
6-100 8.94e-10

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 52.01  E-value: 8.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   6 QSIKSITVPELKEKLLENPALLDVRTPAEYRGGHIKGAK--NVPLQsINRYDG---------------DKEKTVYVICQS 68
Cdd:PLN02160  12 EEVVSVDVSQAKTLLQSGHQYLDVRTQDEFRRGHCEAAKivNIPYM-LNTPQGrvknqefleqvssllNPADDILVGCQS 90
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488223443  69 GMRSKQAAKELKKSGY-DVVNVRGGMNQWFDRT 100
Cdd:PLN02160  91 GARSLKATTELVAAGYkKVRNKGGGYLAWVDHS 123
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
25-97 6.15e-09

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: 48.83  E-value: 6.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  25 ALLDVRTPAEYRGGHIKGAKNVP----------LQSINRYDGDKEKTVYviCQSGMRSKQAAKELKKSGY-DVVNVRGGM 93
Cdd:cd01529   14 ALLDVRAEDEYAAGHLPGKRSIPgaalvlrsqeLQALEAPGRATRYVLT--CDGSLLARFAAQELLALGGkPVALLDGGT 91

                 ....
gi 488223443  94 NQWF 97
Cdd:cd01529   92 SAWV 95
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
26-97 4.96e-08

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: 46.69  E-value: 4.96e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488223443  26 LLDVRTPAEYRGGHIKGAKNVP----LQSINRYDGDKEKTVYVICQSGMRSKQAAKELKKSGYDVVNVRGGMNQWF 97
Cdd:cd01534   19 RFDVRTPEEYEAGHLPGFRHTPggqlVQETDHFAPVRGARIVLADDDGVRADMTASWLAQMGWEVYVLEGGLAAAL 94
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
15-79 1.32e-07

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 47.52  E-value: 1.32e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488223443  15 ELKEKLLENPALLDVRTPAEYRGGHIKGAKNVPLQSinrydgDKEK----TVYVicqsgMRSKQAAKEL 79
Cdd:PRK11784   7 DFRALFLNDTPLIDVRSPIEFAEGHIPGAINLPLLN------DEERaevgTCYK-----QQGQFAAIAL 64
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
9-97 2.71e-07

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: 45.09  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   9 KSITVPELKEkLLENP--------ALLDVRTPaEYRGGHIKGAKNVPLQSI-----NRYDGDK-EKTVYVIC---QSGMR 71
Cdd:cd01443    2 KYISPEELVA-LLENSdsnagkdfVVVDLRRD-DYEGGHIKGSINLPAQSCyqtlpQVYALFSlAGVKLAIFycgSSQGR 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488223443  72 SKQAAKE----LKKSGYD---VVNVRGGMNQWF 97
Cdd:cd01443   80 GPRAARWfadyLRKVGESlpkSYILTGGIKAWY 112
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
11-87 5.32e-07

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: 44.59  E-value: 5.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  11 ITVPELKEKLLENPALLDVRTPAEYRGGHIKGAKNVPLQSinrydgDKEK----TVYVicQSGmrsKQAAKELkksGYDV 86
Cdd:cd01520    1 ITAEDLLALRKADGPLIDVRSPKEFFEGHLPGAINLPLLD------DEERalvgTLYK--QQG---REAAIEL---GLEL 66

                 .
gi 488223443  87 V 87
Cdd:cd01520   67 V 67
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
22-98 1.92e-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: 42.72  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  22 ENPALLDVRTPAEYRGGHIKGAKNVPLQSINRYDG---DKEKTVYVIC--QSGMRSKQAAKELKKSGYDVVNVRGGMNQW 96
Cdd:cd01521   24 PDFVLVDVRSAEAYARGHVPGAINLPHREICENATaklDKEKLFVVYCdgPGCNGATKAALKLAELGFPVKEMIGGLDWW 103

                 ..
gi 488223443  97 FD 98
Cdd:cd01521  104 KR 105
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
5-49 7.03e-06

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: 41.44  E-value: 7.03e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 488223443   5 FQSIKSITVPELKEKLLENPA----LLDVRTPAEYRGGHIKGAKNVPLQ 49
Cdd:cd01530    1 LKRISPETLARLLQGKYDNFFdkyiIIDCRFPYEYNGGHIKGAVNLSTK 49
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
8-96 7.56e-06

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: 41.25  E-value: 7.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443   8 IKSITVPELKEKLLENP---ALLDVRTpAEYRGGHIKGAKNVPLQSI---------NRYDGDKEKTVYVICQSGMRSKQA 75
Cdd:cd01531    1 VSYISPAQLKGWIRNGRppfQVVDVRD-EDYAGGHIKGSWHYPSTRFkaqlnqlvqLLSGSKKDTVVFHCALSQVRGPSA 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 488223443  76 AKEL------KKSGYDVVNV---RGGMNQW 96
Cdd:cd01531   80 ARKFlryldeEDLETSKFEVyvlHGGFNAW 109
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
10-96 1.75e-04

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: 37.44  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  10 SITVPELKEKLL--ENPALLDVRTPAEYRGGHIKGAKNVP----LQSINRYDGDKEKTVYVICQSGMRSKQAAKELKKSG 83
Cdd:cd01533   11 SVSADELAALQArgAPLVVLDGRRFDEYRKMTIPGSVSCPgaelVLRVGELAPDPRTPIVVNCAGRTRSIIGAQSLINAG 90
                         90
                 ....*....|....*
gi 488223443  84 Y--DVVNVRGGMNQW 96
Cdd:cd01533   91 LpnPVAALRNGTQGW 105
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
14-92 2.08e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 37.17  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  14 PELKEKLLENP--ALLDVRTPAEYRGGHIKGAKNVPLQSINRY--------DGDKEKTVYVICQSGMRSKQAAKELKKSG 83
Cdd:cd01518    6 PAEWNELLEDPevVLLDVRNDYEYDIGHFKGAVNPDVDTFREFpfwldenlDLLKGKKVLMYCTGGIRCEKASAYLKERG 85
                         90
                 ....*....|
gi 488223443  84 Y-DVVNVRGG 92
Cdd:cd01518   86 FkNVYQLKGG 95
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
15-87 5.84e-04

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 37.13  E-value: 5.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  15 ELKEKLLENPAL-LDVRTPAEYRGGHIKGAKNVPLQS--------INRYDGDKEKTVYVICQSGMRSKQAAKELKKSGYD 85
Cdd:PRK00142 118 EVNELLDDPDVVfIDMRNDYEYEIGHFENAIEPDIETfrefppwvEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFK 197

                 ..
gi 488223443  86 VV 87
Cdd:PRK00142 198 EV 199
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
10-53 3.41e-03

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: 34.57  E-value: 3.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488223443  10 SITVPELKEKLLENPA---LLDVRTPAEYRGGHIKGAKNVPLQSINR 53
Cdd:cd01446    1 TIDCAWLAALLREGGErllLLDCRPFLEYSSSHIRGAVNVCCPTILR 47
RHOD_Kc cd01525
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the ...
18-94 6.36e-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: 6.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488223443  18 EKLLENP----ALLDVRTPAEYRGGHIKGAKNVPLQSINRYDGD-------------KEKTVYVICQSGMRSKQAAKELK 80
Cdd:cd01525    7 IRLLDNSpaklAAVDIRSSPDFRRGHIEGSINIPFSSVFLKEGEleqlptvprlenyKGKIIVIVSHSHKHAALFAAFLV 86
                         90
                 ....*....|....*
gi 488223443  81 KSGYDVVNV-RGGMN 94
Cdd:cd01525   87 KCGVPRVCIlDGGIN 101
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH