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Conserved domains on  [gi|241913259]
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Chain A, Uncharacterized protein YGR203W

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10107439)

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

PubMed:  8702871

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 9-132 1.61e-56

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: 172.21  E-value: 1.61e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259   9 VKYLDPTELHRWMQEGHtttlrEPFQVVDVRGSDYMGGHIKDGWHYAYSRLKQDPEYLRELKHrllekqadGRGALNVIF 88
Cdd:cd01531    1 VSYISPAQLKGWIRNGR-----PPFQVVDVRDEDYAGGHIKGSWHYPSTRFKAQLNQLVQLLS--------GSKKDTVVF 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 241913259  89 H*MLSQQRGPSAAMLLLRSLDTAEL--SRCRLWVLRGGFSRWQSVY 132
Cdd:cd01531   68 HCALSQVRGPSAARKFLRYLDEEDLetSKFEVYVLHGGFNAWESSY 113
 
Name Accession Description Interval E-value
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 9-132 1.61e-56

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: 172.21  E-value: 1.61e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259   9 VKYLDPTELHRWMQEGHtttlrEPFQVVDVRGSDYMGGHIKDGWHYAYSRLKQDPEYLRELKHrllekqadGRGALNVIF 88
Cdd:cd01531    1 VSYISPAQLKGWIRNGR-----PPFQVVDVRDEDYAGGHIKGSWHYPSTRFKAQLNQLVQLLS--------GSKKDTVVF 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 241913259  89 H*MLSQQRGPSAAMLLLRSLDTAEL--SRCRLWVLRGGFSRWQSVY 132
Cdd:cd01531   68 HCALSQVRGPSAARKFLRYLDEEDLetSKFEVYVLHGGFNAWESSY 113
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 30-134 2.47e-09

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: 51.31  E-value: 2.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259    30 REPFQVVDVRG-SDYMGGHIKDGWHYAYSRLKQDPEYLRELKHRLLEKQADGRGALNVIFH*MlSQQRGPsAAMLLLRSL 108
Cdd:smart00450   2 DEKVVLLDVRSpEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKDKPVVVYCR-SGNRSA-KAAWLLREL 79

                           90       100
                   ....*....|....*....|....*.
gi 241913259   109 DTAelsrcRLWVLRGGFSRWQSVYGD 134
Cdd:smart00450  80 GFK-----NVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 30-129 2.69e-06

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: 43.24  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259   30 REPFQVVDVRGSD-YMGGHIKDGWHYAYSRLKQDPEYLRELKHRLLEKQADGRgalnVIFH*mLSQQRGPSAAMLLLRsl 108
Cdd:pfam00581   3 DGKVVLIDVRPPEeYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLELLKDKP----IVVYC-NSGNRAAAAAALLKA-- 75

                          90       100
                  ....*....|....*....|.
gi 241913259  109 dtaeLSRCRLWVLRGGFSRWQ 129
Cdd:pfam00581  76 ----LGYKNVYVLDGGFEAWK 92
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 9-130 8.44e-05

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: 39.57  E-value: 8.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259   9 VKYLDPTELHRWMQEghtttlrEPFQVVDVRG-SDYMGGHIKDGWHYAYSRLkqdPEYLREL-KHRllekqadgrgalNV 86
Cdd:COG0607    3 VKEISPAELAELLES-------EDAVLLDVREpEEFAAGHIPGAINIPLGEL---AERLDELpKDK------------PI 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 241913259  87 IFH*MLSQQRGPSAAMLLlrsldtAELSRCRLWVLRGGFSRWQS 130
Cdd:COG0607   61 VVY-CASGGRSAQAAALL------RRAGYTNVYNLAGGIEAWKA 97
 
Name Accession Description Interval E-value
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 9-132 1.61e-56

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: 172.21  E-value: 1.61e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259   9 VKYLDPTELHRWMQEGHtttlrEPFQVVDVRGSDYMGGHIKDGWHYAYSRLKQDPEYLRELKHrllekqadGRGALNVIF 88
Cdd:cd01531    1 VSYISPAQLKGWIRNGR-----PPFQVVDVRDEDYAGGHIKGSWHYPSTRFKAQLNQLVQLLS--------GSKKDTVVF 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 241913259  89 H*MLSQQRGPSAAMLLLRSLDTAEL--SRCRLWVLRGGFSRWQSVY 132
Cdd:cd01531   68 HCALSQVRGPSAARKFLRYLDEEDLetSKFEVYVLHGGFNAWESSY 113
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 9-129 2.55e-20

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: 80.14  E-value: 2.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259   9 VKYLDPTELHRWMqEGHTTTLREPFQVVDVRGSDYMGGHIKDGWHY----AYSRLKQDPEYLRELKHRLlekqadgrgal 84
Cdd:cd01443    1 LKYISPEELVALL-ENSDSNAGKDFVVVDLRRDDYEGGHIKGSINLpaqsCYQTLPQVYALFSLAGVKL----------- 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 241913259  85 nVIFH*MLSQQRGPSAAMLLLRSLDTAELSRCRLWVLRGGFSRWQ 129
Cdd:cd01443   69 -AIFYCGSSQGRGPRAARWFADYLRKVGESLPKSYILTGGIKAWY 112
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 30-134 2.47e-09

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: 51.31  E-value: 2.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259    30 REPFQVVDVRG-SDYMGGHIKDGWHYAYSRLKQDPEYLRELKHRLLEKQADGRGALNVIFH*MlSQQRGPsAAMLLLRSL 108
Cdd:smart00450   2 DEKVVLLDVRSpEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKDKPVVVYCR-SGNRSA-KAAWLLREL 79

                           90       100
                   ....*....|....*....|....*.
gi 241913259   109 DTAelsrcRLWVLRGGFSRWQSVYGD 134
Cdd:smart00450  80 GFK-----NVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 30-129 2.69e-06

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: 43.24  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259   30 REPFQVVDVRGSD-YMGGHIKDGWHYAYSRLKQDPEYLRELKHRLLEKQADGRgalnVIFH*mLSQQRGPSAAMLLLRsl 108
Cdd:pfam00581   3 DGKVVLIDVRPPEeYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLELLKDKP----IVVYC-NSGNRAAAAAALLKA-- 75

                          90       100
                  ....*....|....*....|.
gi 241913259  109 dtaeLSRCRLWVLRGGFSRWQ 129
Cdd:pfam00581  76 ----LGYKNVYVLDGGFEAWK 92
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 9-130 8.44e-05

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: 39.57  E-value: 8.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259   9 VKYLDPTELHRWMQEghtttlrEPFQVVDVRG-SDYMGGHIKDGWHYAYSRLkqdPEYLREL-KHRllekqadgrgalNV 86
Cdd:COG0607    3 VKEISPAELAELLES-------EDAVLLDVREpEEFAAGHIPGAINIPLGEL---AERLDELpKDK------------PI 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 241913259  87 IFH*MLSQQRGPSAAMLLlrsldtAELSRCRLWVLRGGFSRWQS 130
Cdd:COG0607   61 VVY-CASGGRSAQAAALL------RRAGYTNVYNLAGGIEAWKA 97
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 10-126 6.52e-04

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: 37.20  E-value: 6.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259  10 KYLDPTELHRWMQeGHTTTLREPFQVVDVR-GSDYMGGHIKDGWHYaYSRLKQDPEYLRELKHRLLEKQadgrgaLNVIF 88
Cdd:cd01530    2 KRISPETLARLLQ-GKYDNFFDKYIIIDCRfPYEYNGGHIKGAVNL-STKDELEEFFLDKPGVASKKKR------RVLIF 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 241913259  89 H*MLSQQRGPSAAmLLLRSLDTAE-------LSRCRLWVLRGGFS 126
Cdd:cd01530   74 HCEFSSKRGPRMA-RHLRNLDRELnsnryplLYYPEIYILEGGYK 117
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 12-132 8.57e-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: 37.26  E-value: 8.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241913259  12 LDPTELHRWMQEGHTTTLrepfqVVDVRGS-DYMGGHIKDGWHYAYS-----RLKQDPEYLR------ELKHRLLEkqad 79
Cdd:cd01446    2 IDCAWLAALLREGGERLL-----LLDCRPFlEYSSSHIRGAVNVCCPtilrrRLQGGKILLQqllscpEDRDRLRR---- 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 241913259  80 gRGALNVIFH*MLSQQRGP----SAAMLLLRSLDTAELSRCRLWVLRGGFSRWQSVY 132
Cdd:cd01446   73 -GESLAVVVYDESSSDRERlredSTAESVLGKLLRKLQEGCSVYLLKGGFEQFSSEF 128
 
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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