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Conserved domains on  [gi|2461866519|ref|WP_275900426|]
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MULTISPECIES: rhodanese-like domain-containing protein [unclassified Anoxybacillus]

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]; ...
 8-99 5.91e-41

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: 130.86  E-value: 5.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   8 MVKALTEEEFRAGYRK--AQLIDVREADEYASGHILGARNIPLTQMRMRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKG 85
Cdd:COG0607     2 SVKEISPAELAELLESedAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAG 81

                          90
                  ....*....|....
gi 2461866519  86 YRDLYHLKGGFKTW 99
Cdd:COG0607    82 YTNVYNLAGGIEAW 95
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 8-99 5.91e-41

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: 130.86  E-value: 5.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   8 MVKALTEEEFRAGYRK--AQLIDVREADEYASGHILGARNIPLTQMRMRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKG 85
Cdd:COG0607     2 SVKEISPAELAELLESedAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAG 81

                          90
                  ....*....|....
gi 2461866519  86 YRDLYHLKGGFKTW 99
Cdd:COG0607    82 YTNVYNLAGGIEAW 95
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 22-99 9.82e-34

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: 112.01  E-value: 9.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  22 RKAQLIDVREADEYASGHILGARNIPLTQM--RMRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKGGFKTW 99
Cdd:cd00158     9 EDAVLLDVREPEEYAAGHIPGAINIPLSELeeRAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 23-99 5.42e-26

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: 92.52  E-value: 5.42e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   23 KAQLIDVREADEYASGHILGARNIPLT--------------QMRMRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRD 88
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSelldrrgeldilefEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKN 83

                           90
                   ....*....|.
gi 2461866519   89 LYHLKGGFKTW 99
Cdd:smart00450  84 VYLLDGGYKEW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 23-99 1.55e-25

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: 91.39  E-value: 1.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  23 KAQLIDVREADEYASGHILGARNIPLTQMRM----------RMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHL 92
Cdd:pfam00581   5 KVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLpplpllelleKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVL 84


                  ....*..
gi 2461866519  93 KGGFKTW 99
Cdd:pfam00581  85 DGGFEAW 91
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
8-99 6.23e-23

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 90.84  E-value: 6.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   8 MVKALTEEEFRAGYRK-AQLIDVREADEYASGHILGARNIPLTQMRMRMKE--LRKDQPIYLYCQSGLRSGRAAQMLYRK 84
Cdd:PRK08762    1 SIREISPAEARARAAQgAVLIDVREAHERASGQAEGALRIPRGFLELRIEThlPDRDREIVLICASGTRSAHAAATLREL 80

                          90
                  ....*....|....*
gi 2461866519  85 GYRDLYHLKGGFKTW 99
Cdd:PRK08762   81 GYTRVASVAGGFSAW 95
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 26-99 3.19e-07

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: 46.82  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  26 LIDVREADEYASGHILGARNIPL------------------------------TQMRMRMKELRK--DQP--IYLYC-QS 70
Cdd:TIGR03167   5 LIDVRSPAEFAEGHLPGAINLPLlndeeraevgtlykqvgpfaaiklglalvsPNLAAHVEQWRAfaDGPpqPLLYCwRG 84

                          90       100
                  ....*....|....*....|....*....
gi 2461866519  71 GLRSGRAAQMLYRKGYRdLYHLKGGFKTW 99
Cdd:TIGR03167  85 GMRSGSLAWLLAQIGFR-VPRLEGGYKAY 112
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 8-99 5.91e-41

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: 130.86  E-value: 5.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   8 MVKALTEEEFRAGYRK--AQLIDVREADEYASGHILGARNIPLTQMRMRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKG 85
Cdd:COG0607     2 SVKEISPAELAELLESedAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAG 81

                          90
                  ....*....|....
gi 2461866519  86 YRDLYHLKGGFKTW 99
Cdd:COG0607    82 YTNVYNLAGGIEAW 95
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 22-99 9.82e-34

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: 112.01  E-value: 9.82e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  22 RKAQLIDVREADEYASGHILGARNIPLTQM--RMRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKGGFKTW 99
Cdd:cd00158     9 EDAVLLDVREPEEYAAGHIPGAINIPLSELeeRAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 25-99 5.01e-26

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: 92.33  E-value: 5.01e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2461866519  25 QLIDVREADEYASGHILGARNIPLTQMRMRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYrDLYHLKGGFKTW 99
Cdd:cd01524    15 TLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGF-KVKNLDGGYKTY 88
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 23-99 5.42e-26

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: 92.52  E-value: 5.42e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   23 KAQLIDVREADEYASGHILGARNIPLT--------------QMRMRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRD 88
Cdd:smart00450   4 KVVLLDVRSPEEYEGGHIPGAVNIPLSelldrrgeldilefEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKN 83

                           90
                   ....*....|.
gi 2461866519   89 LYHLKGGFKTW 99
Cdd:smart00450  84 VYLLDGGYKEW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 23-99 1.55e-25

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: 91.39  E-value: 1.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  23 KAQLIDVREADEYASGHILGARNIPLTQMRM----------RMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHL 92
Cdd:pfam00581   5 KVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLpplpllelleKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVL 84


                  ....*..
gi 2461866519  93 KGGFKTW 99
Cdd:pfam00581  85 DGGFEAW 91
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
8-99 6.23e-23

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 90.84  E-value: 6.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   8 MVKALTEEEFRAGYRK-AQLIDVREADEYASGHILGARNIPLTQMRMRMKE--LRKDQPIYLYCQSGLRSGRAAQMLYRK 84
Cdd:PRK08762    1 SIREISPAEARARAAQgAVLIDVREAHERASGQAEGALRIPRGFLELRIEThlPDRDREIVLICASGTRSAHAAATLREL 80

                          90
                  ....*....|....*
gi 2461866519  85 GYRDLYHLKGGFKTW 99
Cdd:PRK08762   81 GYTRVASVAGGFSAW 95
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 20-103 3.95e-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: 72.81  E-value: 3.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  20 GYRKAQLIDVREADEYASGHILGARNIPLTQMRMRMKEL---RKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKGGF 96
Cdd:cd01528    14 EREEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELdsdNPDKDIVVLCHHGGRSMQVAQWLLRQGFENVYNLQGGI 93


                  ....*..
gi 2461866519  97 KTWTGKV 103
Cdd:cd01528    94 DAWSLEV 100
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 7-99 1.02e-17

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 76.45  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   7 RMVKALTEEEFRAGYRKAQLIDVREADEYASGHILGARNIPLTQMRMRMKELRKDQP--IYLYCQSGLRSGRAAQMLYRK 84
Cdd:PRK05597  258 GFGEVLDVPRVSALPDGVTLIDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSAGdeVVVYCAAGVRSAQAVAILERA 337

                          90
                  ....*....|....*
gi 2461866519  85 GYRDLYHLKGGFKTW 99
Cdd:PRK05597  338 GYTGMSSLDGGIEGW 352
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 9-99 1.48e-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: 66.14  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   9 VKALTEEEfragyRKAQLIDVREADEYASGHILGARNIPLTQ----MRMRMKELRK---------DQPIYLYCQSGLRSG 75
Cdd:cd01519     6 VKNLPNPH-----PNKVLIDVREPEELKTGKIPGAINIPLSSlpdaLALSEEEFEKkygfpkpskDKELIFYCKAGVRSK 80

                          90       100
                  ....*....|....*....|....
gi 2461866519  76 RAAQMLYRKGYRDLYHLKGGFKTW 99
Cdd:cd01519    81 AAAELARSLGYENVGNYPGSWLDW 104
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 22-103 1.09e-14

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 67.81  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  22 RKAQLIDVREADEYASGHILGARNIPLTQMRM--RMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKGGFKTW 99
Cdd:PRK07878  302 KKIALIDVREPVEWDIVHIPGAQLIPKSEILSgeALAKLPQDRTIVLYCKTGVRSAEALAALKKAGFSDAVHLQGGVVAW 381


                  ....
gi 2461866519 100 TGKV 103
Cdd:PRK07878  382 AKQV 385
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 15-99 1.97e-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: 63.05  E-value: 1.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  15 EEFRAGYRKAQLIDVREADEYA--SGHILGARNIPLTQMRMRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHL 92
Cdd:cd01444     8 AELLAAGEAPVLLDVRDPASYAalPDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAGFTDVRSL 87


                  ....*..
gi 2461866519  93 KGGFKTW 99
Cdd:cd01444    88 AGGFEAW 94
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 22-99 6.10e-14

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: 62.12  E-value: 6.10e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2461866519  22 RKAQLIDVREADEYASGHILGARNIPLTQMRMRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKGGFKTW 99
Cdd:cd01527    15 QGAVLVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIFHCRSGMRTQQNAERLAAISAGEAYVLEGGLDAW 92
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 24-99 7.89e-14

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: 61.67  E-value: 7.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  24 AQLIDVREADEY-ASGHILGARNIPLTQMRMRM--------KELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKG 94
Cdd:cd01447    15 VLLVDVRDPRELeRTGMIPGAFHAPRGMLEFWAdpdspyhkPAFAEDKPFVFYCASGWRSALAGKTLQDMGLKPVYNIEG 94


                  ....*
gi 2461866519  95 GFKTW 99
Cdd:cd01447    95 GFKDW 99
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 26-100 8.83e-14

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: 61.54  E-value: 8.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  26 LIDVREADEYASGHILGARNIPLTQMRMRMKEL------RKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKGGFKTW 99
Cdd:cd01529    15 LLDVRAEDEYAAGHLPGKRSIPGAALVLRSQELqaleapGRATRYVLTCDGSLLARFAAQELLALGGKPVALLDGGTSAW 94


                  .
gi 2461866519 100 T 100
Cdd:cd01529    95 V 95
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
24-99 2.92e-13

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 60.42  E-value: 2.92e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2461866519  24 AQLIDVREADEYASGHILGARNIPLTQMRMRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKGGFKTW 99
Cdd:PRK00162   21 AVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQQGFDVVYSIDGGFEAW 96
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 12-103 3.82e-13

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: 60.40  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  12 LTEEEFRAGYRKAQ---LIDVREADEYASGHILGARNIPLTQMRMRMKELR----------KDQPIYLYCQSGLRSGRAA 78
Cdd:cd01526    10 VSVKDYKNILQAGKkhvLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKslqelpldndKDSPIYVVCRRGNDSQTAV 89

                          90       100
                  ....*....|....*....|....*.
gi 2461866519  79 QMLYRKGY-RDLYHLKGGFKTWTGKV 103
Cdd:cd01526    90 RKLKELGLeRFVRDIIGGLKAWADKV 115
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 27-105 2.20e-12

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 58.32  E-value: 2.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  27 IDVREADEYASGHILGARNIPLTQMRMRMKELRKDQ--PIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKGGFKTWTGKVK 104
Cdd:PRK10287   24 IDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKndTVKLYCNAGRQSGQAKEILSEMGYTHAENAGGLKDIAMPKVK 103


                  .
gi 2461866519 105 K 105
Cdd:PRK10287  104 G 104
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 23-99 3.69e-12

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: 58.03  E-value: 3.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  23 KAQLIDVREADEYA-----------SGHILGARNIPLTQMRMRMK------ELRK---------DQPIYLYCQSGLRSGR 76
Cdd:cd01449    14 DVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPWTSLLDEDGtfkspeELRAlfaalgitpDKPVIVYCGSGVTACV 93

                          90       100
                  ....*....|....*....|...
gi 2461866519  77 AAQMLYRKGYRDLYHLKGGFKTW 99
Cdd:cd01449    94 LLLALELLGYKNVRLYDGSWSEW 116
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 26-99 5.12e-12

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: 56.73  E-value: 5.12e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2461866519  26 LIDVREADEYASGHILGARNIPLTQMRMRM--KELRKDQPIYLYCQSGLR--SGRAAQMLYRKGYRDLYHLKGGFKTW 99
Cdd:cd01532    13 LIDVREEDPFAQSHPLWAANLPLSRLELDAwvRIPRRDTPIVVYGEGGGEdlAPRAARRLSELGYTDVALLEGGLQGW 90
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 23-90 2.77e-11

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 57.88  E-value: 2.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  23 KAQLIDVREADEYA---------SGHILGARNIPLTQM-----RMR-MKELRK---------DQPIYLYCQSGLRSGRAA 78
Cdd:COG2897   153 DAVLVDARSPERYRgevepidprAGHIPGAVNLPWTDLldedgTFKsAEELRAlfaalgidpDKPVITYCGSGVRAAHTW 232

                          90
                  ....*....|....
gi 2461866519  79 QMLYRKGYRD--LY 90
Cdd:COG2897   233 LALELLGYPNvrLY 246
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 18-100 1.18e-10

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


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 53.90  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  18 RAGYRKAQLIDVREADEYASGHILGARNIPLTQMRMR-MKELRKDQPIYLYCQSGLRSG--RAAQMLYRKGYRdLYHLKG 94
Cdd:cd01521    20 KNGKPDFVLVDVRSAEAYARGHVPGAINLPHREICENaTAKLDKEKLFVVYCDGPGCNGatKAALKLAELGFP-VKEMIG 98


                  ....*.
gi 2461866519  95 GFKTWT 100
Cdd:cd01521    99 GLDWWK 104
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 3-99 1.80e-10

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: 53.56  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   3 FMQRRMVKALTEEEFRAGYRKAQLIDVREaDEYASGHILGARNIPLTQMRMRMKEL-------RKDQPIYlYC-QSGLRS 74
Cdd:cd01443     3 YISPEELVALLENSDSNAGKDFVVVDLRR-DDYEGGHIKGSINLPAQSCYQTLPQVyalfslaGVKLAIF-YCgSSQGRG 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2461866519  75 GRAAQML--YRKG----YRDLYHLKGGFKTW 99
Cdd:cd01443    81 PRAARWFadYLRKvgesLPKSYILTGGIKAW 111
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 26-95 6.21e-10

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: 51.81  E-value: 6.21e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2461866519  26 LIDVREADEYASGHILGARNIPLTQMR------MRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKGG 95
Cdd:cd01518    20 LLDVRNDYEYDIGHFKGAVNPDVDTFRefpfwlDENLDLLKGKKVLMYCTGGIRCEKASAYLKERGFKNVYQLKGG 95
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 23-96 6.76e-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: 46.94  E-value: 6.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  23 KAQLIDVR-EADEYASGHILGARNIP-------------LTQMRMRMKelrKDQPIYLYCQSGLRSGRAAQMLYRKGYRD 88
Cdd:cd01522    15 QAVLVDVRtEAEWKFVGGVPDAVHVAwqvypdmeinpnfLAELEEKVG---KDRPVLLLCRSGNRSIAAAEAAAQAGFTN 91


                  ....*...
gi 2461866519  89 LYHLKGGF 96
Cdd:cd01522    92 VYNVLEGF 99
PLN02160 PLN02160
thiosulfate sulfurtransferase
 25-101 6.87e-08

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 47.39  E-value: 6.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  25 QLIDVREADEYASGHILGAR--NIPLT----QMRMRMKE--------LRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLY 90
Cdd:PLN02160   31 QYLDVRTQDEFRRGHCEAAKivNIPYMlntpQGRVKNQEfleqvsslLNPADDILVGCQSGARSLKATTELVAAGYKKVR 110

                          90
                  ....*....|.
gi 2461866519  91 HLKGGFKTWTG 101
Cdd:PLN02160  111 NKGGGYLAWVD 121
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 15-99 7.83e-08

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 48.29  E-value: 7.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  15 EEFRA-GYRKAQLIDVREADEYASGHILGARNIPL--------------TQMRM------------RMKELRKDQ----- 62
Cdd:PRK11784    6 QDFRAlFLNDTPLIDVRSPIEFAEGHIPGAINLPLlndeeraevgtcykQQGQFaaialghalvagNIAAHREEAwadfp 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2461866519  63 ----PIYLYC-QSGLRSGRAAQMLYRKGYrDLYHLKGGFKTW 99
Cdd:PRK11784   86 ranpRGLLYCwRGGLRSGSVQQWLKEAGI-DVPRLEGGYKAY 126
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
26-103 1.30e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 47.81  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  26 LIDVREADEYASGHILGARNIPLTQMRM-----RMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLyHLKGGFKTWT 100
Cdd:PRK07411  302 LIDVRNPNEYEIARIPGSVLVPLPDIENgpgveKVKELLNGHRLIAHCKMGGRSAKALGILKEAGIEGT-NVKGGITAWS 380


                  ...
gi 2461866519 101 GKV 103
Cdd:PRK07411  381 REV 383
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
26-95 1.55e-07

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 47.53  E-value: 1.55e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2461866519  26 LIDVREADEYASGHILGARNIPLTQMR------MRMKELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKGG 95
Cdd:PRK00142  130 FIDMRNDYEYEIGHFENAIEPDIETFRefppwvEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGG 205
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 26-99 3.19e-07

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: 46.82  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  26 LIDVREADEYASGHILGARNIPL------------------------------TQMRMRMKELRK--DQP--IYLYC-QS 70
Cdd:TIGR03167   5 LIDVRSPAEFAEGHLPGAINLPLlndeeraevgtlykqvgpfaaiklglalvsPNLAAHVEQWRAfaDGPpqPLLYCwRG 84

                          90       100
                  ....*....|....*....|....*....
gi 2461866519  71 GLRSGRAAQMLYRKGYRdLYHLKGGFKTW 99
Cdd:TIGR03167  85 GMRSGSLAWLLAQIGFR-VPRLEGGYKAY 112
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 12-99 4.87e-07

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: 44.41  E-value: 4.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  12 LTEEEFRAGYRKAQ---LIDVREADEYASGHILGARNIP--------LTQMRMRMKELRKDQPIYLYCQSGLRSGRAAQM 80
Cdd:cd01523     1 LDPEDLYARLLAGQplfILDVRNESDYERWKIDGENNTPyfdpyfdfLEIEEDILDQLPDDQEVTVICAKEGSSQFVAEL 80

                          90
                  ....*....|....*....
gi 2461866519  81 LYRKGYrDLYHLKGGFKTW 99
Cdd:cd01523    81 LAERGY-DVDYLAGGMKAW 98
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 17-99 1.24e-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: 43.56  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  17 FRAGYRKAQLIDVREADeYASGHILGARNIPLTQMRMRMKELRKD------QPIYLYC-QSGLRSGRAAQMLYR------ 83
Cdd:cd01531    13 IRNGRPPFQVVDVRDED-YAGGHIKGSWHYPSTRFKAQLNQLVQLlsgskkDTVVFHCaLSQVRGPSAARKFLRyldeed 91

                          90
                  ....*....|....*...
gi 2461866519  84 --KGYRDLYHLKGGFKTW 99
Cdd:cd01531    92 leTSKFEVYVLHGGFNAW 109
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 26-99 7.63e-06

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 42.47  E-value: 7.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  26 LIDVRE-----ADEYASGHILGARNIPLT------------------QMRMRMKEL--RKDQPIYLY-CQSGLRSGRAAQ 79
Cdd:COG2897    12 ILDVRWdlpdgRAAYEAGHIPGAVFLDLDtdlsdprspgrhplpspeAFAALLGALgiSNDTTVVVYdDGGGLFAARAWW 91

                          90       100
                  ....*....|....*....|
gi 2461866519  80 MLYRKGYRDLYHLKGGFKTW 99
Cdd:COG2897    92 LLRYAGHEDVRVLDGGLAAW 111
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 26-99 1.25e-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: 41.13  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  26 LIDVREADEYASGHILGARNIPL---------------------------------TQMRMRMKE--LRKDQPIYLYC-Q 69
Cdd:cd01520    16 LIDVRSPKEFFEGHLPGAINLPLlddeeralvgtlykqqgreaaielglelvsgklKRILNEAWEarLERDPKLLIYCaR 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 2461866519  70 SGLRSGRAAQMLYRKGYrDLYHLKGGFKTW 99
Cdd:cd01520    96 GGMRSQSLAWLLESLGI-DVPLLEGGYKAY 124
PRK01415 PRK01415
hypothetical protein; Validated
 26-95 4.77e-05

hypothetical protein; Validated


Pssm-ID: 167229 [Multi-domain]  Cd Length: 247  Bit Score: 40.31  E-value: 4.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2461866519  26 LIDVREADEYASGHILGARNiPLTQMRMRM-------KELRKDQPIYLYCQSGLRSGRAAQMLYRKGYRDLYHLKGG 95
Cdd:PRK01415  130 VIDTRNDYEVEVGTFKSAIN-PNTKTFKQFpawvqqnQELLKGKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGG 205
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 8-99 1.41e-04

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: 37.83  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   8 MVKALTEEEFRAGYRkaqlIDVREADEYASGHILGARNIPLTQMRMRMKE---LRKDQpIYLYCQSGLRSGRAAQMLYRK 84
Cdd:cd01534     5 ELARWAAEGDRTVYR----FDVRTPEEYEAGHLPGFRHTPGGQLVQETDHfapVRGAR-IVLADDDGVRADMTASWLAQM 79

                          90
                  ....*....|....*
gi 2461866519  85 GYrDLYHLKGGFKTW 99
Cdd:cd01534    80 GW-EVYVLEGGLAAA 93
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 26-99 1.93e-04

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


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 37.60  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  26 LIDVREA-------DEYASGHILGARNIPLTQMR-------------------MRMKELRKDQPIYLYCQSGLRS-GRAA 78
Cdd:cd01448    18 ILDARWYlpdrdgrKEYLEGHIPGAVFFDLDEDLddkspgphmlpspeefaelLGSLGISNDDTVVVYDDGGGFFaARAW 97

                          90       100
                  ....*....|....*....|.
gi 2461866519  79 QMLYRKGYRDLYHLKGGFKTW 99
Cdd:cd01448    98 WTLRYFGHENVRVLDGGLQAW 118
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 26-98 5.82e-04

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


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 36.49  E-value: 5.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  26 LIDVREADEYASGHILGARNIPL-TQMRMRMKE-------------------LRKDQPIYLYCQSGLRSGR--------- 76
Cdd:cd01446    20 LLDCRPFLEYSSSHIRGAVNVCCpTILRRRLQGgkillqqllscpedrdrlrRGESLAVVVYDESSSDRERlredstaes 99

                          90       100
                  ....*....|....*....|....
gi 2461866519  77 AAQMLYRKGYR--DLYHLKGGFKT 98
Cdd:cd01446   100 VLGKLLRKLQEgcSVYLLKGGFEQ 123
MIH1 COG5105
Mitotic inducer, protein phosphatase [Cell division and chromosome partitioning];
3-97 8.59e-04

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


Pssm-ID: 227436 [Multi-domain]  Cd Length: 427  Bit Score: 36.94  E-value: 8.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   3 FMQR---RMVKALTEEEFRAGYRKAQLIDVREADEYASGHILGARNIPLTQ---MRMRMKELRKDQPIYLYCQ-SGLRSG 75
Cdd:COG5105   240 SIQRisvETLKQVLEGMYNIDFLKCIIIDCRFEYEYRGGHIINAVNISSTKklgLLFRHKPLTHPRALIFHCEfSSHRAP 319

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2461866519  76 RAAQML-----------YRK-GYRDLYHLKGGFK 97
Cdd:COG5105   320 RLAQHLrnmdrmknpdhYPLlTYPEVYILEGGYK 353
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 5-100 9.50e-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: 35.90  E-value: 9.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519   5 QRRMVKALTEEEFR---AGYRKAQLIDVREADEYASGHILGARNIPLTQMRMRMKELRKD--QPIYLYCQSGLRSGRAAQ 79
Cdd:cd01533     5 AVRHTPSVSADELAalqARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDprTPIVVNCAGRTRSIIGAQ 84

                          90       100
                  ....*....|....*....|..
gi 2461866519  80 MLYRKGYRD-LYHLKGGFKTWT 100
Cdd:cd01533    85 SLINAGLPNpVAALRNGTQGWT 106
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 22-99 1.59e-03

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 36.32  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461866519  22 RKAQLIDVREADEY-----------ASGHILGARNIPLTQM------RMRMKELRK---------DQPIYLYCQSGLRSG 75
Cdd:PLN02723  204 KTYQHIDARSKARFdgaapeprkgiRSGHIPGSKCVPFPQMldssqtLLPAEELKKrfeqegislDSPIVASCGTGVTAC 283

                          90       100
                  ....*....|....*....|....
gi 2461866519  76 RAAQMLYRKGYRDLYHLKGGFKTW 99
Cdd:PLN02723  284 ILALGLHRLGKTDVPVYDGSWTEW 307
 
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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