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Conserved domains on  [gi|768899212|gb|AJW27272|]
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Arr2p [Saccharomyces cerevisiae YJM981]

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 ...
 2-119 1.55e-57

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: 173.75  E-value: 1.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212   2 VSFITSRQLKGLIENQRKDFQVVDLRREDFARDHITNAWHVPvtAQITEKQLNQLIKGLsdtfSSSQFVKVIFHCTGSKN 81
Cdd:cd01531    1 VSYISPAQLKGWIRNGRPPFQVVDVRDEDYAGGHIKGSWHYP--STRFKAQLNQLVQLL----SGSKKDTVVFHCALSQV 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 768899212  82 RGPKVAAKFETYLQEEDI-TSKFESCILVGGFYAWETHC 119
Cdd:cd01531   75 RGPSAARKFLRYLDEEDLeTSKFEVYVLHGGFNAWESSY 113
 
Name Accession Description Interval E-value
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 2-119 1.55e-57

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: 173.75  E-value: 1.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212   2 VSFITSRQLKGLIENQRKDFQVVDLRREDFARDHITNAWHVPvtAQITEKQLNQLIKGLsdtfSSSQFVKVIFHCTGSKN 81
Cdd:cd01531    1 VSYISPAQLKGWIRNGRPPFQVVDVRDEDYAGGHIKGSWHYP--STRFKAQLNQLVQLL----SGSKKDTVVFHCALSQV 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 768899212  82 RGPKVAAKFETYLQEEDI-TSKFESCILVGGFYAWETHC 119
Cdd:cd01531   75 RGPSAARKFLRYLDEEDLeTSKFEVYVLHGGFNAWESSY 113
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 17-121 1.59e-13

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 61.71  E-value: 1.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212    17 QRKDFQVVDLR-REDFARDHITNAWHVPVTAQIT--EKQLNQLIKGLSDTFSSSQFVKVIFHCTGSkNRGPKVAAKFETY 93
Cdd:smart00450   1 NDEKVVLLDVRsPEEYEGGHIPGAVNIPLSELLDrrGELDILEFEELLKRLGLDKDKPVVVYCRSG-NRSAKAAWLLREL 79

                           90       100
                   ....*....|....*....|....*...
gi 768899212    94 LQEeditskfESCILVGGFYAWETHCRE 121
Cdd:smart00450  80 GFK-------NVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 17-115 2.75e-07

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: 45.17  E-value: 2.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212   17 QRKDFQVVDLR-REDFARDHITNAWHVPVTaqITEKQLNQLIKGLSDTFSSSQFVKVIFHCtGSKNRGPKvAAKFETYLQ 95
Cdd:pfam00581   2 EDGKVVLIDVRpPEEYAKGHIPGAVNVPLS--SLSLPPLPLLELLEKLLELLKDKPIVVYC-NSGNRAAA-AAALLKALG 77

                          90       100
                  ....*....|....*....|
gi 768899212   96 EEDItskfesCILVGGFYAW 115
Cdd:pfam00581  78 YKNV------YVLDGGFEAW 91
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-116 3.73e-07

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: 45.34  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212   1 MVSFITSRQLKGLIENqrKDFQVVDLR-REDFARDHITNAWHVPVtAQItEKQLNQLIKGlsdtfsssqfVKVIFHCtGS 79
Cdd:COG0607    2 SVKEISPAELAELLES--EDAVLLDVRePEEFAAGHIPGAINIPL-GEL-AERLDELPKD----------KPIVVYC-AS 66

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 768899212  80 KNRGPKVAAkfetYLQEEDITskfESCILVGGFYAWE 116
Cdd:COG0607   67 GGRSAQAAA----LLRRAGYT---NVYNLAGGIEAWK 96
 
Name Accession Description Interval E-value
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 2-119 1.55e-57

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: 173.75  E-value: 1.55e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212   2 VSFITSRQLKGLIENQRKDFQVVDLRREDFARDHITNAWHVPvtAQITEKQLNQLIKGLsdtfSSSQFVKVIFHCTGSKN 81
Cdd:cd01531    1 VSYISPAQLKGWIRNGRPPFQVVDVRDEDYAGGHIKGSWHYP--STRFKAQLNQLVQLL----SGSKKDTVVFHCALSQV 74

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 768899212  82 RGPKVAAKFETYLQEEDI-TSKFESCILVGGFYAWETHC 119
Cdd:cd01531   75 RGPSAARKFLRYLDEEDLeTSKFEVYVLHGGFNAWESSY 113
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 2-117 1.03e-47

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: 149.09  E-value: 1.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212   2 VSFITSRQLKGLIENQ----RKDFQVVDLRREDFARDHITNAWHVPvtAQITEKQLNQLIKGlsdtFSSSQFVKVIFHCT 77
Cdd:cd01443    1 LKYISPEELVALLENSdsnaGKDFVVVDLRRDDYEGGHIKGSINLP--AQSCYQTLPQVYAL----FSLAGVKLAIFYCG 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 768899212  78 GSKNRGPKVAAKFETYLQeEDITSKFESCILVGGFYAWET 117
Cdd:cd01443   75 SSQGRGPRAARWFADYLR-KVGESLPKSYILTGGIKAWYH 113
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 17-121 1.59e-13

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 61.71  E-value: 1.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212    17 QRKDFQVVDLR-REDFARDHITNAWHVPVTAQIT--EKQLNQLIKGLSDTFSSSQFVKVIFHCTGSkNRGPKVAAKFETY 93
Cdd:smart00450   1 NDEKVVLLDVRsPEEYEGGHIPGAVNIPLSELLDrrGELDILEFEELLKRLGLDKDKPVVVYCRSG-NRSAKAAWLLREL 79

                           90       100
                   ....*....|....*....|....*...
gi 768899212    94 LQEeditskfESCILVGGFYAWETHCRE 121
Cdd:smart00450  80 GFK-------NVYLLDGGYKEWSAAGPP 100
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 9-116 7.64e-10

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: 51.92  E-value: 7.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212   9 QLKGLIENqrKDFQVVDLR-REDFARDHITNAWHVPVTAQITEKQLNQLIKGlsdtfsssqfVKVIFHCtGSKNRGPKVA 87
Cdd:cd00158    1 ELKELLDD--EDAVLLDVRePEEYAAGHIPGAINIPLSELEERAALLELDKD----------KPIVVYC-RSGNRSARAA 67

                         90       100
                 ....*....|....*....|....*....
gi 768899212  88 AKFETYlqeeditSKFESCILVGGFYAWE 116
Cdd:cd00158   68 KLLRKA-------GGTNVYNLEGGMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 17-115 2.75e-07

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: 45.17  E-value: 2.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212   17 QRKDFQVVDLR-REDFARDHITNAWHVPVTaqITEKQLNQLIKGLSDTFSSSQFVKVIFHCtGSKNRGPKvAAKFETYLQ 95
Cdd:pfam00581   2 EDGKVVLIDVRpPEEYAKGHIPGAVNVPLS--SLSLPPLPLLELLEKLLELLKDKPIVVYC-NSGNRAAA-AAALLKALG 77

                          90       100
                  ....*....|....*....|
gi 768899212   96 EEDItskfesCILVGGFYAW 115
Cdd:pfam00581  78 YKNV------YVLDGGFEAW 91
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-116 3.73e-07

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: 45.34  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212   1 MVSFITSRQLKGLIENqrKDFQVVDLR-REDFARDHITNAWHVPVtAQItEKQLNQLIKGlsdtfsssqfVKVIFHCtGS 79
Cdd:COG0607    2 SVKEISPAELAELLES--EDAVLLDVRePEEFAAGHIPGAINIPL-GEL-AERLDELPKD----------KPIVVYC-AS 66

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 768899212  80 KNRGPKVAAkfetYLQEEDITskfESCILVGGFYAWE 116
Cdd:COG0607   67 GGRSAQAAA----LLRRAGYT---NVYNLAGGIEAWK 96
Cdc25 cd01530
Cdc25 phosphatases are members of the Rhodanese Homology Domain superfamily. They activate the ...
 5-98 4.65e-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: 4.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212   5 ITSRQLKGLIE----NQRKDFQVVDLRRE-DFARDHITNAWHVPVTAQITEKQLNQLIkglsdTFSSSQFVKVIFHCTGS 79
Cdd:cd01530    4 ISPETLARLLQgkydNFFDKYIIIDCRFPyEYNGGHIKGAVNLSTKDELEEFFLDKPG-----VASKKKRRVLIFHCEFS 78

                         90
                 ....*....|....*....
gi 768899212  80 KNRGPKVAAkfetYLQEED 98
Cdd:cd01530   79 SKRGPRMAR----HLRNLD 93
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 10-118 4.91e-04

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: 36.95  E-value: 4.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768899212  10 LKGLIENQRKDFQVVDLR-REDFARDHITNAWHVPvTAQITEKQLNQLIKG-LSDTFSSSQfvkvifHCTGSKnrgpKVA 87
Cdd:cd01521   15 VAIALKNGKPDFVLVDVRsAEAYARGHVPGAINLP-HREICENATAKLDKEkLFVVYCDGP------GCNGAT----KAA 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 768899212  88 AKFetylqeedITSKFESCILVGGFYAWETH 118
Cdd:cd01521   84 LKL--------AELGFPVKEMIGGLDWWKRE 106
 
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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